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23 kDa fragment of photosystem II D1 protein + H2O
?
alpha-casein + H2O
?
-
ATP is required for the reaction. The enzyme is unable to degrade the substrate in the presence of AMPPNP
-
-
?
Anabaena apoflavodoxin + H2O
?
beta-casein + H2O
?
-
-
-
?
damaged PSII D1 protein + H2O
?
delta32 protein + H2O
?
-
-
-
-
?
EX1 + H2O
?
substrate chloroplast protein EXECUTER1, involved in signaling by singlet oxygen
-
-
?
Fur repressor protein + H2O
?
degraded by the FtsH1/FtsH3 complex
-
-
?
GgpS protein + H2O
?
-
soluble substrate
-
-
?
H+-ATPase F0alpha + H2O
?
-
membrane substrate of FtsH
-
-
?
heat shock transcription factor sigma 32 + H2O
?
-
-
-
-
?
light-harvesting complex II + H2O
?
-
AtFtsH6 is involved in the degradation of the light-harvesting complex II during high-light acclimation and senescence
-
-
?
LpxC + H2O
?
-
cytosolic substrate of FtsH
-
-
?
photodamaged D1 protein + H2O
?
photodamaged D2 protein + H2O
?
-
-
-
-
?
photosystem II reaction center subunit D1 + H2O
?
photosystem II reaction center subunit D2 + H2O
?
-
FtsH has a key role in the repair of UVB-damaged photosystem II
-
-
?
photosystem II subunit D1 + H2O
?
-
-
-
?
photosystem II subunit D2 + H2O
?
-
-
-
?
protein D2 + H2O
?
-
-
-
-
?
protein lambdaCII + H2O
?
-
-
-
-
?
protein sigma32 + H2O
?
-
-
-
-
?
proteins + H2O
peptides
-
-
?
PsbA protein + H2O
?
-
-
-
-
?
reaction center D1 protein + H2O
23-kDa N-terminal fragments of reaction center D1 protein
-
-
-
-
?
Rieske FeS protein + H2O
?
-
degradation of membrane protein, essentially required as a membrane-integrated quality control
-
?
sigma32 + H2O
?
-
substrate from Escherichia coli
-
-
?
subunit SecY of the SecAEG translocase + H2O
?
-
membrane substrate of FtsH
-
-
?
unassembled cytochrome b6f complex + H2O
?
-
-
-
?
unassembled Rieske FeS protein + H2O
?
-
recombinant wild-type protein and mutant C162S, recombinant protein substrate is imported in vitro into intact Pisum sativum chloroplasts
-
?
YccA + H2O
?
-
membrane substrate of FtsH
-
-
?
additional information
?
-
23 kDa fragment of photosystem II D1 protein + H2O
?
-
-
-
?
23 kDa fragment of photosystem II D1 protein + H2O
?
-
enzyme is required for protection against photoinhibition and induction of repair of photosystem II D1 protein, degradation of irreversible damaged D1 protein in form of the 23 kDa fragment
-
?
23 kDa fragment of photosystem II D1 protein + H2O
?
-
irreversibly damaged substrate by reactive oxygen species formed in the light
-
?
23 kDa fragment of photosystem II D1 protein + H2O
?
-
degradation, irreversibly damaged substrate by reactive oxygen species formed in the light
-
?
Anabaena apoflavodoxin + H2O
?
-
FtsH degradation of 31 point mutants of Anabaena apoflavodoxin is inversely proportional to their conformational stabilities. FtsH degrades the apo form of Anabaena flavodoxin, but it is unable to hydrolyze the holo form, activities with fully and partly unfolded substrate protein, overview
-
-
?
Anabaena apoflavodoxin + H2O
?
-
FtsH degradation of 31 point mutants of Anabaena apoflavodoxin from Anabaena PCC 7119 is inversely proportional to their conformational stabilities. FtsH degrades the apo form of Anabaena flavodoxin, but it is unable to hydrolyze the holo form
-
-
?
casein + H2O
?
-
-
-
?
casein + H2O
?
artificial resorufin-labeled substrate
-
-
?
D1 protein + H2O
?
-
-
-
-
?
D1 protein + H2O
?
-
-
-
?
D1 protein + H2O
?
-
-
-
-
?
D1 protein + H2O
?
-
FtsH protease is responsible for the primary cleavage of the D1 protein under moderate heat stress conditions
-
-
?
D1 protein + H2O
?
isoform FtsH2 is involved in selective D1 protein degradation during photosystem II repair
-
-
?
D1 protein + H2O
?
substrate for isoform FtsH2
-
-
?
damaged PSII D1 protein + H2O
?
O80860, O80983, Q1PDW5, Q39102, Q84WU8, Q8VZI8, Q8W585, Q9FGM0, Q9FH02, Q9FIM2, Q9SAJ3, Q9SD67 -
-
-
?
damaged PSII D1 protein + H2O
?
-
-
-
?
damaged PSII D1 protein + H2O
?
-
-
-
-
?
damaged PSII D1 protein + H2O
?
-
-
-
-
?
lambdaCII + H2O
?
-
-
-
-
?
lambdaCII + H2O
?
-
the key protein that influences the lysis/lysogeny decision of lambda by activating several phage promoters
-
-
?
photodamaged D1 protein + H2O
?
-
-
-
-
?
photodamaged D1 protein + H2O
?
-
-
the enzyme produces a 23000 Da N-terminal and a 9000 Da C-terminal fragment
-
?
photodamaged D1 protein + H2O
?
-
-
-
-
?
photodamaged D1 protein + H2O
?
-
-
the enzyme produces a 23000 Da N-terminal and a 9000 Da C-terminal fragment
-
?
photodamaged D1 protein + H2O
?
-
-
the enzyme produces a 23000 Da N-terminal and a 9000 Da C-terminal fragment
-
?
photodamaged D1 protein + H2O
?
degradation
-
-
?
photodamaged D1 protein + H2O
?
degradation, part of photosystem 2 repair
-
-
?
photosystem II reaction center subunit D1 + H2O
?
-
-
-
-
?
photosystem II reaction center subunit D1 + H2O
?
-
FtsH has a key role in the repair of UVB-damaged photosystem II
-
-
?
PhzC + H2O
?
-
substrate is a phenazine biosynthesis protein, and substrate of isoform FtsH1
-
-
?
PhzC + H2O
?
-
substrate is a phenazine biosynthesis protein, and substrate of isoform FtsH1
-
-
?
Protein + H2O
?
-
FtsH is involved in the degradation of unassembled proteins, the repair of photosystem II from photoinhibition, and the formation of thylakoids
-
-
?
Protein + H2O
?
-
FtsH11 protease plays a critical role in Arabidopsis thermotolerance. FtsH11 constitutively protects the photosynthesis apparatus from the damage caused by elevated temperatures
-
-
?
Protein + H2O
?
-
thylakoid FtsH protease is involved in the degradation of unassembled proteins, and in the turnover of the D1 protein of the PSII reaction center in the context of its repair from photoinhibition. FtsH proteases are involved in the formation of thylakoids
-
-
?
Protein + H2O
?
-
FtsH (slr0228) plays an important role in controlling the removal of unassembled PSII subunits from the thylakoid membrane
-
-
?
Protein + H2O
?
-
FtsH mediates repair of the photosystem II complex in response to light stress
-
-
?
protein + H2O
peptides
-
-
?
protein + H2O
peptides
-
-
?
protein + H2O
peptides
-
degradation of membrane proteins, essentially required as a membrane-integrated quality control
-
?
protein + H2O
peptides
-
unfoldase activity might be a common property of ATP-dependent proteases
-
?
protein + H2O
peptides
degradation of unassembled proteins, apoproteins lacking their prosthetic groups or pigments, photo- or otherwise damaged proteins, and of developmentally or environmentally regulated proteins
-
?
protein + H2O
peptides
enzyme is involved in chloroplast biogenesis
-
?
protein + H2O
peptides
-
-
-
?
protein + H2O
peptides
-
-
-
?
protein + H2O
peptides
-
degradation of unassembled proteins, apoproteins lacking their prostethic groups or pigments, photo-or otherwise damaged proteins, and of developmentally or environmentally regulated proteins
-
?
protein + H2O
peptides
-
-
-
?
protein + H2O
peptides
-
degradation of unassembled proteins, apoproteins lacking their prosthetic groups or pigments, photo- or otherwise damaged proteins, and of developmentally or environmentally regulated proteins
-
?
protein D1 + H2O
?
-
-
-
-
?
protein D1 + H2O
?
-
FtsH (slr0228) is required for selective D1 turnover during photosystem II repair
-
-
?
protein D1 + H2O
?
-
FtsH protease plays an essential role in the turnover of the reaction center D1 protein in Synechocystis PCC 6803 under heat stress as well as light stress conditions
-
-
?
RNase colicin D + H2O
?
-
the interaction of colicin D with LepB may ensure a stable association with the inner membrane that in turn allows the colicin recognition by FtsH
-
-
?
RNase colicin D + H2O
?
-
the interaction of colicin D with LepB may ensure a stable association with the inner membrane that in turn allows the colicin recognition by FtsH
-
-
?
RNase colicin E3 + H2O
?
-
-
-
-
?
RNase colicin E3 + H2O
?
-
-
-
-
?
RpoH + H2O
?
-
RpoH is rapidly degraded by chaperone-mediated FtsH-dependent proteolysis
-
-
?
RpoH + H2O
?
-
several RpoH residues critical for degradation are located in the highly conserved region 2.1. The double mutation A131E/K134V significantly stabilizes RpoH against degradation by the FtsH protease, while the single-point mutations at these positions only show a slight effect on RpoH stability. A minimal RpoH variant composed of residues L37-G147, including region 2.1 and C, is a sufficient FtsH substrate. Region 2.1 and region C might serve as interaction surfaces for FtsH-mediated degradation
-
-
?
RpoH + H2O
?
-
substrate heat shock transcription factor RpoH is degraded rapidly in the wild-type and FtsH2 deletion mutant background with a half-life of less than 10 min, and degraded with an estimated half-life between 10 and 30 min in the FtsH1 mutant and FtsH1 FtsH2 double mutant background
-
-
?
RpoH + H2O
?
-
substrate heat shock transcription factor RpoH is degraded rapidly in the wild-type and FtsH2 deletion mutant background with a half-life of less than 10 min, and degraded with an estimated half-life between 10 and 30 min in the FtsH1 mutant and FtsH1 FtsH2 double mutant background
-
-
?
Spo0E + H2O
?
-
-
-
-
?
Spo0E + H2O
?
-
the Spo0E phosphatase is distinguished from the YisI and YnzD phosphatases by a C-terminal extension of about 25 amino acids, the C-terminal region of Spo0E confers target specificity to FtsH
-
-
?
additional information
?
-
the AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence
-
-
?
additional information
?
-
the AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence
-
-
?
additional information
?
-
the AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence
-
-
?
additional information
?
-
the AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence
-
-
?
additional information
?
-
the AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence
-
-
?
additional information
?
-
the AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence
-
-
?
additional information
?
-
the AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence
-
-
?
additional information
?
-
the AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence
-
-
?
additional information
?
-
the AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence
-
-
?
additional information
?
-
the AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence
-
-
?
additional information
?
-
the AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence
-
-
?
additional information
?
-
the AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence
-
-
?
additional information
?
-
-
the D1 protein, a core subunit of the PSII reaction enter, is a substrate for FtsH protease
-
-
?
additional information
?
-
-
neither phosphatases YisI nor YnzD, homologues of Spo0E, are substrates of FtsH
-
-
?
additional information
?
-
FtsH is complexed with HflCK
-
-
?
additional information
?
-
-
fully unfolded states of proteins are the general substrates of FtsH, FtsH substrates can be either tagged proteins or proteins of low stability, substrate recognition and substrate specificity, overview
-
-
?
additional information
?
-
-
the six AAA domains bind and translocate proteins that are targeted for destruction in an ATP-dependent manner into the interior of the molecule, where the proteolytic sites are located and where substrate proteins are degraded in a processive manner
-
-
?
additional information
?
-
-
complex substrate recognition mechanisms, detailed overview. The ATPase domain forms the entrance to the central pore of FtsH with a diameter of about 15 A, a conserved Phe at position 228 of the pore is crucial for substrate binding. Substrates are pulled through the narrow gate and into the following protease domain using the energy of ATP hydrolysis for unfolding and translocation of the proteins. FtsH has only weak unfolding activity and is not able to degrade tightly folded model substrate proteins like GFP or DHFR
-
-
?
additional information
?
-
-
mutational substrate analysis, structure-function anaylsis, modelling, overview
-
-
?
additional information
?
-
-
no activity with GST and bovine serum albumin
-
?
additional information
?
-
the D1 processing mutants, D1-S345P and DELTACtpA, are unable to assemble a functional CaMn4 cluster
-
-
?
additional information
?
-
-
the D1 processing mutants, D1-S345P and DELTACtpA, are unable to assemble a functional CaMn4 cluster
-
-
?
additional information
?
-
photosystem II subunits CP47 and CP43 are much more resistant to proteolytic degradation in the dark than subunit D1 and D2
-
-
?
additional information
?
-
an active-site switch is formed by a substrate-binding beta-strand
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
23 kDa fragment of photosystem II D1 protein + H2O
?
Anabaena apoflavodoxin + H2O
?
-
FtsH degradation of 31 point mutants of Anabaena apoflavodoxin is inversely proportional to their conformational stabilities. FtsH degrades the apo form of Anabaena flavodoxin, but it is unable to hydrolyze the holo form, activities with fully and partly unfolded substrate protein, overview
-
-
?
damaged PSII D1 protein + H2O
?
delta32 protein + H2O
?
-
-
-
-
?
Fur repressor protein + H2O
?
degraded by the FtsH1/FtsH3 complex
-
-
?
heat shock transcription factor sigma 32 + H2O
?
-
-
-
-
?
lambdaCII + H2O
?
-
the key protein that influences the lysis/lysogeny decision of lambda by activating several phage promoters
-
-
?
light-harvesting complex II + H2O
?
-
AtFtsH6 is involved in the degradation of the light-harvesting complex II during high-light acclimation and senescence
-
-
?
photodamaged D1 protein + H2O
?
photodamaged D2 protein + H2O
?
-
-
-
-
?
protein D2 + H2O
?
-
-
-
-
?
proteins + H2O
peptides
-
-
?
PsbA protein + H2O
?
-
-
-
-
?
Rieske FeS protein + H2O
?
-
degradation of membrane protein, essentially required as a membrane-integrated quality control
-
?
RpoH + H2O
?
-
RpoH is rapidly degraded by chaperone-mediated FtsH-dependent proteolysis
-
-
?
Spo0E + H2O
?
-
the Spo0E phosphatase is distinguished from the YisI and YnzD phosphatases by a C-terminal extension of about 25 amino acids, the C-terminal region of Spo0E confers target specificity to FtsH
-
-
?
unassembled cytochrome b6f complex + H2O
?
-
-
-
?
additional information
?
-
23 kDa fragment of photosystem II D1 protein + H2O
?
-
enzyme is required for protection against photoinhibition and induction of repair of photosystem II D1 protein, degradation of irreversible damaged D1 protein in form of the 23 kDa fragment
-
?
23 kDa fragment of photosystem II D1 protein + H2O
?
-
degradation, irreversibly damaged substrate by reactive oxygen species formed in the light
-
?
D1 protein + H2O
?
-
-
-
-
?
D1 protein + H2O
?
-
-
-
?
D1 protein + H2O
?
-
-
-
-
?
D1 protein + H2O
?
-
FtsH protease is responsible for the primary cleavage of the D1 protein under moderate heat stress conditions
-
-
?
D1 protein + H2O
?
isoform FtsH2 is involved in selective D1 protein degradation during photosystem II repair
-
-
?
D1 protein + H2O
?
substrate for isoform FtsH2
-
-
?
damaged PSII D1 protein + H2O
?
O80860, O80983, Q1PDW5, Q39102, Q84WU8, Q8VZI8, Q8W585, Q9FGM0, Q9FH02, Q9FIM2, Q9SAJ3, Q9SD67 -
-
-
?
damaged PSII D1 protein + H2O
?
-
-
-
?
damaged PSII D1 protein + H2O
?
-
-
-
-
?
damaged PSII D1 protein + H2O
?
-
-
-
-
?
photodamaged D1 protein + H2O
?
-
-
-
-
?
photodamaged D1 protein + H2O
?
-
-
the enzyme produces a 23000 Da N-terminal and a 9000 Da C-terminal fragment
-
?
photodamaged D1 protein + H2O
?
-
-
-
-
?
photodamaged D1 protein + H2O
?
-
-
the enzyme produces a 23000 Da N-terminal and a 9000 Da C-terminal fragment
-
?
photodamaged D1 protein + H2O
?
-
-
the enzyme produces a 23000 Da N-terminal and a 9000 Da C-terminal fragment
-
?
photodamaged D1 protein + H2O
?
degradation, part of photosystem 2 repair
-
-
?
Protein + H2O
?
-
FtsH is involved in the degradation of unassembled proteins, the repair of photosystem II from photoinhibition, and the formation of thylakoids
-
-
?
Protein + H2O
?
-
FtsH11 protease plays a critical role in Arabidopsis thermotolerance. FtsH11 constitutively protects the photosynthesis apparatus from the damage caused by elevated temperatures
-
-
?
Protein + H2O
?
-
thylakoid FtsH protease is involved in the degradation of unassembled proteins, and in the turnover of the D1 protein of the PSII reaction center in the context of its repair from photoinhibition. FtsH proteases are involved in the formation of thylakoids
-
-
?
Protein + H2O
?
-
FtsH (slr0228) plays an important role in controlling the removal of unassembled PSII subunits from the thylakoid membrane
-
-
?
Protein + H2O
?
-
FtsH mediates repair of the photosystem II complex in response to light stress
-
-
?
protein + H2O
peptides
-
degradation of membrane proteins, essentially required as a membrane-integrated quality control
-
?
protein + H2O
peptides
degradation of unassembled proteins, apoproteins lacking their prosthetic groups or pigments, photo- or otherwise damaged proteins, and of developmentally or environmentally regulated proteins
-
?
protein + H2O
peptides
enzyme is involved in chloroplast biogenesis
-
?
protein + H2O
peptides
-
degradation of unassembled proteins, apoproteins lacking their prostethic groups or pigments, photo-or otherwise damaged proteins, and of developmentally or environmentally regulated proteins
-
?
protein + H2O
peptides
-
degradation of unassembled proteins, apoproteins lacking their prosthetic groups or pigments, photo- or otherwise damaged proteins, and of developmentally or environmentally regulated proteins
-
?
protein D1 + H2O
?
-
FtsH (slr0228) is required for selective D1 turnover during photosystem II repair
-
-
?
protein D1 + H2O
?
-
FtsH protease plays an essential role in the turnover of the reaction center D1 protein in Synechocystis PCC 6803 under heat stress as well as light stress conditions
-
-
?
RNase colicin D + H2O
?
-
the interaction of colicin D with LepB may ensure a stable association with the inner membrane that in turn allows the colicin recognition by FtsH
-
-
?
RNase colicin D + H2O
?
-
the interaction of colicin D with LepB may ensure a stable association with the inner membrane that in turn allows the colicin recognition by FtsH
-
-
?
RNase colicin E3 + H2O
?
-
-
-
-
?
RNase colicin E3 + H2O
?
-
-
-
-
?
additional information
?
-
the AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence
-
-
?
additional information
?
-
the AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence
-
-
?
additional information
?
-
the AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence
-
-
?
additional information
?
-
the AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence
-
-
?
additional information
?
-
the AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence
-
-
?
additional information
?
-
the AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence
-
-
?
additional information
?
-
the AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence
-
-
?
additional information
?
-
the AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence
-
-
?
additional information
?
-
the AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence
-
-
?
additional information
?
-
the AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence
-
-
?
additional information
?
-
the AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence
-
-
?
additional information
?
-
the AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence
-
-
?
additional information
?
-
-
the D1 protein, a core subunit of the PSII reaction enter, is a substrate for FtsH protease
-
-
?
additional information
?
-
FtsH is complexed with HflCK
-
-
?
additional information
?
-
-
fully unfolded states of proteins are the general substrates of FtsH, FtsH substrates can be either tagged proteins or proteins of low stability, substrate recognition and substrate specificity, overview
-
-
?
additional information
?
-
-
the six AAA domains bind and translocate proteins that are targeted for destruction in an ATP-dependent manner into the interior of the molecule, where the proteolytic sites are located and where substrate proteins are degraded in a processive manner
-
-
?
additional information
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the D1 processing mutants, D1-S345P and DELTACtpA, are unable to assemble a functional CaMn4 cluster
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-
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additional information
?
-
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the D1 processing mutants, D1-S345P and DELTACtpA, are unable to assemble a functional CaMn4 cluster
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evolution
O80860, O80983, Q1PDW5, Q39102, Q84WU8, Q8VZI8, Q8W585, Q9FGM0, Q9FH02, Q9FIM2, Q9SAJ3, Q9SD67 FtsH gene multiplication is of adaptive value during the course of evolution of oxygenic photosynthesis
evolution
-
the mode of action of FtsH proteases seems to be different between cyanobacteria and higher plants
malfunction
-
mutants lacking isoforms FtsH2 and FtsH5 are characterized by a typical leaf-variegated phenotype
malfunction
a mutant conditionally depleted in FtsH3 is unable to induce normal expression of the IsiA chlorophyll-protein and FutA1 iron transporter upon iron deficiency due to a block in transcription, which is regulated by the Fur transcriptional repressor
malfunction
a mutant depleted in isoform FtsH3 displays impaired protein D1 degradation
malfunction
A stabilizing effect on Fur is observed in a mutant conditionally depleted in the FtsH1 subunit
malfunction
the ftsh1-1 mutation Increases photosystem II sensitivity to photoinhibition, prevents photosystem II repair, and leads to the accumulation of D1 protein fragments
malfunction
-
the loss of isoform FtsH4 regulates Arabidopsis development and architecture by mediating the peroxidase-dependent interplay between hydrogen peroxide and auxin homeostasis
metabolism
-
enzyme regulation, overview
metabolism
-
enzyme regulation, overview
metabolism
enzyme regulation, overview
metabolism
O80860, O80983, Q1PDW5, Q39102, Q84WU8, Q8VZI8, Q8W585, Q9FGM0, Q9FH02, Q9FIM2, Q9SAJ3, Q9SD67 enzyme regulation, overview
metabolism
-
FtsH cellular functions and regulation involving several factors, overview
metabolism
-
FtsH5/VAR1, FtsH2/VAR2, VAR3 and THF1 control leaf variegation in Arabidopsis thaliana
metabolism
-
the thylakoid located FtsH complex in Arabidopsis is responsible for degradation of photodamaged D1 protein in concert with lumenal Deg proteases
physiological function
-
Chloroplast development promoted by the ectopic expression of cGPA1 is dependent on FtsH complexes. FtsH complexes, which are composed of type-A (FtsH1/FtsH5) and type-B (FtsH2/FtsH8) subunits, are required for cGPA1-promoted chloroplast development in the leaf-variegated mutant thylakoid formation 1, thf1, overview
physiological function
filamentation temperature-sensitive H, FtsH, is a membrane-anchored ATP-dependent metalloprotease
physiological function
FtsH converts the chemical energy stored in ATP via conformational rearrangements into a mechanical force that is used for substrate unfolding and translocation into the proteolytic chamber
physiological function
-
FtsH has both chaperone and protease activities, and it is a crucial element in protein quality control, involving a number of substrates and processes, including the degradation of unneeded and damaged membrane proteins as well as soluble signaling factors
physiological function
-
FtsH has to degrade or to regulate the steady-state level of one or more proteins that interfere with successful sporulation. In the absence of the ATP-dependent metalloprotease FtsH, the sporulation frequency of Bacillus subtilis cells is reduced by several orders of magnitude
physiological function
FtsH is a membrane-bound protein essential for the cell viability in Escherichia coli
physiological function
-
FtsH is a peculiar prokaryotic protease with low unfoldase activity. FtsH takes care of degrading unstable or inappropriately assembled proteins
physiological function
-
FtsH is an essential membrane-bound protease that degrades integral membrane proteins as well as cytoplasmic proteins. FtsH is a stress-response protein that promotes the pathogen's ability to deal with reactive oxygen intermediates stress and is possibly involved in the regulation of FtsZ levels. Optimal intracellular levels of the essential cell-division protein FtsZ are critical for cell division and viability, overview
physiological function
-
FtsH is the only known membrane-anchored AAA protease in bacteria that fulfills a variety of regulatory functions. FtsH-mediated regulation of LpxC levels by proteolysis crucial for cell viability. FtsH is involved in the quality control of misfolded or incorrectly inserted membrane proteins and acts either as a chaperone to help them refold or degrades them. Another important function of FtsH in Escherichia coli is control of heat shock gene expression, overview
physiological function
O80860, O80983, Q1PDW5, Q39102, Q84WU8, Q8VZI8, Q8W585, Q9FGM0, Q9FH02, Q9FIM2, Q9SAJ3, Q9SD67 in chloroplasts, the most clearly defined function of FtsH is in photosystem II, PSII, repair, where it degrades photooxidatively damaged D1 proteins
physiological function
-
in chloroplasts, the most clearly defined function of FtsH is in photosystem II, PSII, repair, where it degrades photooxidatively damaged D1 proteins. slr0228 is involved in the early steps of D1 degradation and also plays a role in the removal of other damaged or unassembled thylakoid proteins
physiological function
O80860, O80983, Q1PDW5, Q39102, Q84WU8, Q8VZI8, Q8W585, Q9FGM0, Q9FH02, Q9FIM2, Q9SAJ3, Q9SD67 in chloroplasts, the most clearly defined function of FtsH is in photosystem II, PSII, repair, where it degrades photooxidatively damaged D1 proteins. The AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence
physiological function
-
the ATP-dependent metalloprotease FtsH is involved in the degradation of the photo- or heat-damaged D1 protein. Damage occurs in the reaction center-binding D1 protein understrong visible light and heat stress, overview
physiological function
-
the ATP-dependent zinc metallopeptidase is a cell division protein
physiological function
O80860, O80983, Q1PDW5, Q39102, Q84WU8, Q8VZI8, Q8W585, Q9FGM0, Q9FH02, Q9FIM2, Q9SAJ3, Q9SD67 the ATP-dependent zinc metallopeptidase is a cell division protein
physiological function
O80860, O80983, Q1PDW5, Q39102, Q84WU8, Q8VZI8, Q8W585, Q9FGM0, Q9FH02, Q9FIM2, Q9SAJ3, Q9SD67 the ATP-dependent zinc metallopeptidase is a cell division protein. FtsH2 and FtsH5 are responsible for leaf variegation and proteolysis of photodamaged D1 protein in Arabidopsis
physiological function
O80860, O80983, Q1PDW5, Q39102, Q84WU8, Q8VZI8, Q8W585, Q9FGM0, Q9FH02, Q9FIM2, Q9SAJ3, Q9SD67 the ATP-dependent zinc metallopeptidase is involved in the degradation of both Lhcb3 and Lhcb1 during senescence and high-light acclimation
physiological function
O80860, O80983, Q1PDW5, Q39102, Q84WU8, Q8VZI8, Q8W585, Q9FGM0, Q9FH02, Q9FIM2, Q9SAJ3, Q9SD67 the ATP-dependent zinc metallopeptidase is involved in the repair of PSII following damage incurred during photoinhibition. FtsH2 and FtsH5 are responsible for leaf variegation and proteolysis of photodamaged D1 protein in Arabidopsis
physiological function
the FtsH2 protease plays a key role in the degradation of both precursor and mature forms of D1 following donor-side photoinhibition, and in the selective degradation of photodamaged D1 protein and incompletely processed forms of the D1 protein during the repair of photosystem II in the cyanobacterium, overview. The FtsH2 protease participates in fast D1 replacement in the psbO deletion strain
physiological function
O80860, O80983, Q1PDW5, Q39102, Q84WU8, Q8VZI8, Q8W585, Q9FGM0, Q9FH02, Q9FIM2, Q9SAJ3, Q9SD67 VAR2, a subunit of the chloroplast FtsH complex, is involved in turnover of the photosystem II reaction center D1 protein, as well as in other processes required for the development and maintenance of the photosynthetic apparatus
physiological function
-
FtsH is necessary for the processing of colicinsDand E3 during their import
physiological function
-
interplay between N-terminal methionine excision and FtsH protease is essential for normal chloroplast development and function. The N-terminally processed D1 and D2 polypeptide chains are primarily degraded by the FtsH complex, which ensures their quality control
physiological function
-
part of the FtsH hexamers are juxtapositioned to PSII complexes in the grana in darkness, carrying out immediate degradation of the photodamaged D1 protein under light stress
physiological function
-
the heteromeric FtsH complex is important for maintaining thylakoid membranes
physiological function
FtsH is involved in quality control and the regulation of accumulation of cytochrome b6f complexes and complex C subunit B proteins. The enzyme regulates the degradation of photosystem II upon photoinhibition and phosphorus and sulfur starvation
physiological function
FtsH metalloproteases are key components of the photosystem II repair cycle which operates to maintain photosynthetic activity in the light. isoforms FtsH1 and FtsH3 are required for cell viability, whereas FtsH2 and FtsH4 are dispensable. isoform FtsH3 is more important than FtsH2 for cell viability
physiological function
-
FtsH1 is a regulatory protein for organelle biogenesis in Plasmodium falciparum
physiological function
isoform FtsH2 is involved in the repair of photosystem II within the thylakoid membranes
physiological function
the FtsH1 protease is involved in the acclimation of cells to iron deficiency
physiological function
the FtsH2/FtsH3 complex is involved in photoprotection
physiological function
the FtsH2/FtsH3 complex is involved in photoprotection. The FtsH3 protease is involved in the acclimation of cells to iron deficiency
physiological function
Q7V1V9; Q7V362
comparison of the low light, high nutrient strain Prochlorococcus marinus MIT 9313, the high light, low nutrient Prochlorococcus marinus MED 4, and the high light, high nutrient marine Synechococcus strain WH 8102, under low and high growth light levels. The strains differ significantly in their rates of photosystem II repair under high light and in their capacity to remove the PsbA protein as the first step in the photosystem II repair process. All strains remove the PsbD subunit at the same rate that they remove PsbA. When grown under low light, MIT 9313 loses active photosystem II quickly when shifted to high light, but has no measurable capacity to remove PsbA. MED 4 and WH 8102 show less rapid loss of photosystem II and considerable capacity to remove PsbA
physiological function
comparison of the low light, high nutrient strain Prochlorococcus marinus MIT 9313, the high light, low nutrient Prochlorococcus marinus MED 4, and the high light, high nutrient marine Synechococcus strain WH 8102, under low and high growth light levels. The strains differ significantly in their rates of photosystem II repair under high light and in their capacity to remove the PsbA protein as the first step in the photosystem II repair process. All strains remove the PsbD subunit at the same rate that they remove PsbA. When grown under low light, MIT 9313 loses active photosystem II quickly when shifted to high light, but has no measurable capacity to remove PsbA. MED 4 and WH 8102 show less rapid loss of photosystem II and considerable capacity to remove PsbA. MIT 9313 has less of the FtsH protease
physiological function
-
deletion mutants of isoform FtsH1 display a severe growth retardation both in LB and M63 medium. The lag phase is extended from 6 to 8 h and retardation of growth at the second phase of the biphasic growth curve leads to a 1.5 h longer doubling time in the FtsH1 FtsH2 double mutant compared to the FtsH1 mutant. The FtsH2 mutant does not show a pronounced growth retardation phenotype. Deletion of FtsH1, but not FtsH2 moderately enhances sensitivity to a lethal heat shock. Deletion of FtsH1 causes a 13% reduction in swimming motility, which is 38% reduction the FtsH1 FtsH2 double deletion background. The FtsH1 mutant forms an undifferentiated flat biofilm. The FtsH1 FtsH2 double mutant forms dense irregular biofilm structures anchored to the substratum at a few contact points
physiological function
FtsH is a highly dynamic protease undergoing sequential transitions between five conformational states on the second timescale. Addition of ATP does not influence the number of states or change the timescale of domain motions but affects the state occupancy distribution leading to an interdomain compaction
physiological function
initiation of singlet oxygen signaling in grana margins depends on EX1 and the ATP-dependent zinc metalloprotease FtsH. FtsH cleaves also the D1 protein during the disassembly of damaged PSII, EX1-and singlet oxygen-mediated may be spatially but also functionally associated with the repair of PSII
physiological function
mutation of FtsH11 gene causes significant decreases in photosynthetic efficiency of photosystems when environmental temperature raises above optimal. Under moderately high temperatures, the FtsH11 mutant shows significant decreases in electron transfer rates of photosystem II (PSII) and photosystem I (PSI), decreases in photosynthetic capabilities of PSII and PSI, increases in non-photochemical quenching, and a host of other chlorophyll fluorescence parameter changes. For plants grown under normal temperature and subjected to the high light treatment, no significant difference in chlorophyll fluorescence parameters is found between the FtsH11 mutant and Col-0 WT plants
physiological function
-
phylogenetic analysis of over 6000 FtsH protease sequences. The FtsH proteases involved in PSII repair form a distinct clade branching out before the divergence of FtsH proteases found in all groups of anoxygenic phototrophic bacteria. The phylogenetic tree of FtsH proteases in phototrophic bacteria is similar to that for Type I and Type II reaction centre proteins
physiological function
protein Psb29a minor component of His-tagged photosystem II preparations, physically interacts with FtsH complexes in vivo and is required for normal accumulation of the FtsH2/FtsH3 hetero-oligomeric complex involved in photosystem II repair. In a Psb29 null mutant, levels of FtsH2 and FtsH3 are substantially decreased
physiological function
the proteolytic activity, and not only the ATPase one, is essential for conferring thermotolerance to the plants. FTSH11 interacts with different components of the CPN60 chaperonin. CPN60s as well as a number of envelope, stroma and thylakoid proteins are found associated with proteolytically inactive FTSH11. In a knockout strain, protein TIC40 is highly stabilized. The nucleotide antiporter PAPST2, the fatty acid binding protein FAP1 and the chaperone HSP70 are trapped in an affinity enrichment assay
physiological function
upon high light exposure, the FtsH1 and FtsH2 and subunits display a shorter half-life, which is counterbalanced by an increase in FTSH1/2 mRNA levels, resulting in modest upregulation of FtsH1/2 proteins. High light increases the protease activity through a redox-controlled reduction of intermolecular disulfide bridges. In a FTSH1 promoter-deficient mutant, the abundance of FtsH1 and FtsH2 proteins are loosely coupled (decreased by 70% and 30%, respectively) with no formation of large and stable homo-oligomers. High light tolerance is tightly correlated with the abundance of the FtsH protease
physiological function
-
filamentation temperature-sensitive H, FtsH, is a membrane-anchored ATP-dependent metalloprotease
-
physiological function
-
comparison of the low light, high nutrient strain Prochlorococcus marinus MIT 9313, the high light, low nutrient Prochlorococcus marinus MED 4, and the high light, high nutrient marine Synechococcus strain WH 8102, under low and high growth light levels. The strains differ significantly in their rates of photosystem II repair under high light and in their capacity to remove the PsbA protein as the first step in the photosystem II repair process. All strains remove the PsbD subunit at the same rate that they remove PsbA. When grown under low light, MIT 9313 loses active photosystem II quickly when shifted to high light, but has no measurable capacity to remove PsbA. MED 4 and WH 8102 show less rapid loss of photosystem II and considerable capacity to remove PsbA. MIT 9313 has less of the FtsH protease
-
physiological function
-
comparison of the low light, high nutrient strain Prochlorococcus marinus MIT 9313, the high light, low nutrient Prochlorococcus marinus MED 4, and the high light, high nutrient marine Synechococcus strain WH 8102, under low and high growth light levels. The strains differ significantly in their rates of photosystem II repair under high light and in their capacity to remove the PsbA protein as the first step in the photosystem II repair process. All strains remove the PsbD subunit at the same rate that they remove PsbA. When grown under low light, MIT 9313 loses active photosystem II quickly when shifted to high light, but has no measurable capacity to remove PsbA. MED 4 and WH 8102 show less rapid loss of photosystem II and considerable capacity to remove PsbA
-
physiological function
-
FtsH is a highly dynamic protease undergoing sequential transitions between five conformational states on the second timescale. Addition of ATP does not influence the number of states or change the timescale of domain motions but affects the state occupancy distribution leading to an interdomain compaction
-
physiological function
-
FtsH is an essential membrane-bound protease that degrades integral membrane proteins as well as cytoplasmic proteins. FtsH is a stress-response protein that promotes the pathogen's ability to deal with reactive oxygen intermediates stress and is possibly involved in the regulation of FtsZ levels. Optimal intracellular levels of the essential cell-division protein FtsZ are critical for cell division and viability, overview
-
physiological function
-
FtsH is necessary for the processing of colicinsDand E3 during their import
-
physiological function
-
deletion mutants of isoform FtsH1 display a severe growth retardation both in LB and M63 medium. The lag phase is extended from 6 to 8 h and retardation of growth at the second phase of the biphasic growth curve leads to a 1.5 h longer doubling time in the FtsH1 FtsH2 double mutant compared to the FtsH1 mutant. The FtsH2 mutant does not show a pronounced growth retardation phenotype. Deletion of FtsH1, but not FtsH2 moderately enhances sensitivity to a lethal heat shock. Deletion of FtsH1 causes a 13% reduction in swimming motility, which is 38% reduction the FtsH1 FtsH2 double deletion background. The FtsH1 mutant forms an undifferentiated flat biofilm. The FtsH1 FtsH2 double mutant forms dense irregular biofilm structures anchored to the substratum at a few contact points
-
additional information
-
ftsH interferes with the expression or activity of phosphatases RapA, RapB, RapE and Spo0E, and interferes with the phosphorylation status of Spo0A through Spo0E
additional information
mechanisms of variegation suppression, including an unexpected link between var2 variegation and chloroplast translation
additional information
mechanisms of variegation suppression, including an unexpected link between var2 variegation and chloroplast translation
additional information
mechanisms of variegation suppression, including an unexpected link between var2 variegation and chloroplast translation
additional information
mechanisms of variegation suppression, including an unexpected link between var2 variegation and chloroplast translation
additional information
mechanisms of variegation suppression, including an unexpected link between var2 variegation and chloroplast translation
additional information
mechanisms of variegation suppression, including an unexpected link between var2 variegation and chloroplast translation
additional information
mechanisms of variegation suppression, including an unexpected link between var2 variegation and chloroplast translation
additional information
mechanisms of variegation suppression, including an unexpected link between var2 variegation and chloroplast translation
additional information
mechanisms of variegation suppression, including an unexpected link between var2 variegation and chloroplast translation
additional information
mechanisms of variegation suppression, including an unexpected link between var2 variegation and chloroplast translation
additional information
mechanisms of variegation suppression, including an unexpected link between var2 variegation and chloroplast translation
additional information
mechanisms of variegation suppression, including an unexpected link between var2 variegation and chloroplast translation
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?
x * 78000, SDS-PAGE
?
O80860, O80983, Q1PDW5, Q39102, Q84WU8, Q8VZI8, Q8W585, Q9FGM0, Q9FH02, Q9FIM2, Q9SAJ3, Q9SD67 x * 115105, FtsH12, sequence calculation
?
O80860, O80983, Q1PDW5, Q39102, Q84WU8, Q8VZI8, Q8W585, Q9FGM0, Q9FH02, Q9FIM2, Q9SAJ3, Q9SD67 x * 73198, FtsH8, sequence calculation
?
O80860, O80983, Q1PDW5, Q39102, Q84WU8, Q8VZI8, Q8W585, Q9FGM0, Q9FH02, Q9FIM2, Q9SAJ3, Q9SD67 x * 74515, FtsH6, sequence calculation
?
O80860, O80983, Q1PDW5, Q39102, Q84WU8, Q8VZI8, Q8W585, Q9FGM0, Q9FH02, Q9FIM2, Q9SAJ3, Q9SD67 x * 75232, FtsH5, sequence calculation
?
O80860, O80983, Q1PDW5, Q39102, Q84WU8, Q8VZI8, Q8W585, Q9FGM0, Q9FH02, Q9FIM2, Q9SAJ3, Q9SD67 x * 76759, FtsH1, sequence calculation
?
O80860, O80983, Q1PDW5, Q39102, Q84WU8, Q8VZI8, Q8W585, Q9FGM0, Q9FH02, Q9FIM2, Q9SAJ3, Q9SD67 x * 77275, FtsH4, sequence calculation
?
O80860, O80983, Q1PDW5, Q39102, Q84WU8, Q8VZI8, Q8W585, Q9FGM0, Q9FH02, Q9FIM2, Q9SAJ3, Q9SD67 x * 87802, FtsH7, sequence calculation
?
O80860, O80983, Q1PDW5, Q39102, Q84WU8, Q8VZI8, Q8W585, Q9FGM0, Q9FH02, Q9FIM2, Q9SAJ3, Q9SD67 x * 87838, FtsH9, sequence calculation
?
O80860, O80983, Q1PDW5, Q39102, Q84WU8, Q8VZI8, Q8W585, Q9FGM0, Q9FH02, Q9FIM2, Q9SAJ3, Q9SD67 x * 88717, FtsH11, sequence calculation
?
O80860, O80983, Q1PDW5, Q39102, Q84WU8, Q8VZI8, Q8W585, Q9FGM0, Q9FH02, Q9FIM2, Q9SAJ3, Q9SD67 x * 89353, FtsH3, sequence calculation
?
O80860, O80983, Q1PDW5, Q39102, Q84WU8, Q8VZI8, Q8W585, Q9FGM0, Q9FH02, Q9FIM2, Q9SAJ3, Q9SD67 x * 89555, FtsH10, sequence calculation
?
x * 70709, sequence calculation
?
-
x * 78000, mature form, SDS-PAGE, x * 80000, pro-form, SDS-PAGE
?
-
x * 68199, sll1463, sequence calculation, x * 68496, slr0228, sequence calculation, x * 67250, slr1640, sequence calculation, x * 69304, slr1390, sequence calculation
heterohexamer
-
-
heterohexamer
-
FtsH hexamer is composed of two A-type (FtsH 1 and 5) and four B-type (FtsH 2 and 8) subunits. FtsH monomers form an active hexamer in the thylakoid under light stress
heterohexamer
-
the Arabidopsis thylakoid FtsH protease complex is composed of FtsH1/FtsH5 (type A) and FtsH2/FtsH8 (type B) subunits
heterohexamer
the thylakoid FtsH hexamer is composed of four type B (FtsH2 and FtsH8) subunits
heterohexamer
the thylakoid FtsH hexamer is composed of two type A (FtsH1 and FtsH5) subunits
heterohexamer
the thylakoid FtsH hexamer is composed of two type A (FtsH1) and four type B (FtsH8) subunits
heterohexamer
-
FtsH hexamer is composed of two A-type (FtsH 1 and 5) and four B-type (FtsH 2 and 8) subunits. FtsH monomers form an active hexamer in the thylakoid under light stress
heterohexamer
-
FtsH hexamer is composed of two A-type (FtsH 1 and 5) and four B-type (FtsH 2 and 8) subunits. FtsH monomers form an active hexamer in the thylakoid under light stress
hexamer
x-ray crystallography
hexamer
-
6 * 71000, FtsH forms a barrel-shaped oligomer
hexamer
hexameric assembly consisting of a 6fold symmetric protease disk and a 2fold symmetric AAA ring
homohexamer
-
-
homohexamer
-
FtsH forms homohexameric ring structures and large heterocomplexes with HflK/C
homohexamer
-
6 * 104000, GST-tagged FtsH1, SDS-PAGE
homohexamer
-
6 * 66000, isoform FtsH1, calculated from amino acid sequence
homohexamer
-
6 * 70000, SDS-PAGE
homohexamer
6 * 100000, isoform FtsH2-GST fusion protein, SDS-PAGE
homohexamer
6 * 70000, isoform FtsH3, SDS-PAGE
additional information
-
ATP binding is not necessary for enzyme assembly, enzyme probably forms high molecular weight complexes
additional information
-
FtsH2 and FtsH5 are present in a heteromeric complex
additional information
-
interchangeability of subunits in chloroplast oligomeric complexes
additional information
the duplicated genes, FTSH1 and FTSH5 (subunit type A) and FTSH2 and FTSH8 (subunit type B), are redundant.The presence of two types of subunits is essential for complex formation, photosystem II repair, and chloroplast biogenesis
additional information
the duplicated genes, FTSH1 and FTSH5 (subunit type A) and FTSH2 and FTSH8 (subunit type B), are redundant.The presence of two types of subunits is essential for complex formation, photosystem II repair, and chloroplast biogenesis
additional information
the duplicated genes, FTSH1 and FTSH5 (subunit type A) and FTSH2 and FTSH8 (subunit type B), are redundant.The presence of two types of subunits is essential for complex formation, photosystem II repair, and chloroplast biogenesis
additional information
the duplicated genes, FTSH1 and FTSH5 (subunit type A) and FTSH2 and FTSH8 (subunit type B), are redundant.The presence of two types of subunits is essential for complex formation, photosystem II repair, and chloroplast biogenesis
additional information
-
the duplicated genes, FTSH1 and FTSH5 (subunit type A) and FTSH2 and FTSH8 (subunit type B), are redundant.The presence of two types of subunits is essential for complex formation, photosystem II repair, and chloroplast biogenesis
additional information
chloroplast FtsH proteins form complexes, likely hexamers of 400-450 kDa. Most of these are heterocomplexes built by different FtsH isozymes
additional information
chloroplast FtsH proteins form complexes, likely hexamers of 400-450 kDa. Most of these are heterocomplexes built by different FtsH isozymes
additional information
chloroplast FtsH proteins form complexes, likely hexamers of 400-450 kDa. Most of these are heterocomplexes built by different FtsH isozymes
additional information
chloroplast FtsH proteins form complexes, likely hexamers of 400-450 kDa. Most of these are heterocomplexes built by different FtsH isozymes
additional information
chloroplast FtsH proteins form complexes, likely hexamers of 400-450 kDa. Most of these are heterocomplexes built by different FtsH isozymes
additional information
chloroplast FtsH proteins form complexes, likely hexamers of 400-450 kDa. Most of these are heterocomplexes built by different FtsH isozymes
additional information
chloroplast FtsH proteins form complexes, likely hexamers of 400-450 kDa. Most of these are heterocomplexes built by different FtsH isozymes
additional information
chloroplast FtsH proteins form complexes, likely hexamers of 400-450 kDa. Most of these are heterocomplexes built by different FtsH isozymes
additional information
chloroplast FtsH proteins form complexes, likely hexamers of 400-450 kDa. Most of these are heterocomplexes built by different FtsH isozymes
additional information
chloroplast FtsH proteins form complexes, likely hexamers of 400-450 kDa. Most of these are heterocomplexes built by different FtsH isozymes
additional information
chloroplast FtsH proteins form complexes, likely hexamers of 400-450 kDa. Most of these are heterocomplexes built by different FtsH isozymes
additional information
chloroplast FtsH proteins form complexes, likely hexamers of 400-450 kDa. Most of these are heterocomplexes built by different FtsH isozymes
additional information
chloroplast FtsH proteins form complexes, likely hexamers of 400-450 kDa. Most of these are heterocomplexes built by different FtsH isozymes, but some might be homocomplexes composed of VAR2
additional information
chloroplast FtsH proteins form complexes, likely hexamers of 400-450 kDa. Most of these are heterocomplexes built by different FtsH isozymes, but some might be homocomplexes composed of VAR2
additional information
chloroplast FtsH proteins form complexes, likely hexamers of 400-450 kDa. Most of these are heterocomplexes built by different FtsH isozymes, but some might be homocomplexes composed of VAR2
additional information
chloroplast FtsH proteins form complexes, likely hexamers of 400-450 kDa. Most of these are heterocomplexes built by different FtsH isozymes, but some might be homocomplexes composed of VAR2
additional information
chloroplast FtsH proteins form complexes, likely hexamers of 400-450 kDa. Most of these are heterocomplexes built by different FtsH isozymes, but some might be homocomplexes composed of VAR2
additional information
chloroplast FtsH proteins form complexes, likely hexamers of 400-450 kDa. Most of these are heterocomplexes built by different FtsH isozymes, but some might be homocomplexes composed of VAR2
additional information
chloroplast FtsH proteins form complexes, likely hexamers of 400-450 kDa. Most of these are heterocomplexes built by different FtsH isozymes, but some might be homocomplexes composed of VAR2
additional information
chloroplast FtsH proteins form complexes, likely hexamers of 400-450 kDa. Most of these are heterocomplexes built by different FtsH isozymes, but some might be homocomplexes composed of VAR2
additional information
chloroplast FtsH proteins form complexes, likely hexamers of 400-450 kDa. Most of these are heterocomplexes built by different FtsH isozymes, but some might be homocomplexes composed of VAR2
additional information
chloroplast FtsH proteins form complexes, likely hexamers of 400-450 kDa. Most of these are heterocomplexes built by different FtsH isozymes, but some might be homocomplexes composed of VAR2
additional information
chloroplast FtsH proteins form complexes, likely hexamers of 400-450 kDa. Most of these are heterocomplexes built by different FtsH isozymes, but some might be homocomplexes composed of VAR2
additional information
chloroplast FtsH proteins form complexes, likely hexamers of 400-450 kDa. Most of these are heterocomplexes built by different FtsH isozymes, but some might be homocomplexes composed of VAR2
additional information
-
the C-terminus comprise the cytoplasmic ATPase and protease domain. The ATPase domain contains the Walker A/B motifs and the second region of homology responsible for the binding and hydrolysis of ATP
additional information
comparison of the apo- and ADP-bound structure visualizes an inward movement of the aromatic pore residues and generates a model of substrate translocation by AAA+ proteases, modelling of the apo- and ADP bound state
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D326N
-
the mutant does not cleave delta32 protein
G195D
-
the mutant does not cleave delta32 protein
G267D
-
the mutant does not cleave delta32 protein
G302S
-
the mutant does not cleave delta32 protein
G433R
-
the mutant does not cleave delta32 protein
H417L
-
the mutant accumulates about 20% relative to the wild type enzyme and does not cleave delta32 protein
H488L
-
the FtsH2 mutation inhibits zinc binding and inactivates proteolysis
P320L
-
the mutant does not cleave delta32 protein
H416Y
-
mutation in isoform Ftsh1, inactive
H420Y
-
mutation in isoform Ftsh2, inactive
H416Y
-
mutation in isoform Ftsh1, inactive
-
H420Y
-
mutation in isoform Ftsh2, inactive
-
A359V
homolog of the human pathogenic A510V mutation of paraplegin (SPG7), does not affect the dynamic behavior of the protease but impairs the ATP-coupled domain compaction
G404L
site-directed mutagenesis, the mutant is monomeric and inactive in the ATPase assay and possesses only very low proteolytic activity
K207A
site-directed mutagenesis, crystal structure determination
A359V
-
homolog of the human pathogenic A510V mutation of paraplegin (SPG7), does not affect the dynamic behavior of the protease but impairs the ATP-coupled domain compaction
-
additional information
-
construction of deficient mutant
additional information
-
a FtsH11 null mutant (salk033047) displays thermosensitive phenotypes using both acquired and basal thermotolerance assays
additional information
-
ectopic expression of cGPA1 rescues the leaf variegation of ftsh2 and partially corrects mis-regulated gene expression in thf1, the leaf-variegated mutant thylakoid formation 1, phenotype, overview
additional information
the cells in green sectors of variegation mutant var2 have normal-appearing chloroplasts whereas cells in the white sectors have abnormal plastids that lack pigments and organized lamellae. The mutant serves as threshold model in which the formation of chloroplasts is due to the presence of activities/processes that are able to compensate for a lack of VAR2, mechanisms of variegation suppression, including an unexpected link between var2 variegation and chloroplast translation, phenotype and mutant screening, detailed overview. The enhancement in green sector formation is accompanied by an increased accumulation of chloroplast FtsH mRNA and protein. Overexpressionj of isozyme AtFtsH8 suppresses the var2 phenotype. Isolation and analysis of mutant svr1-1, i.e. suppression of variegation1-1, and of svr2 mutant, overview. Examples of var2 suppressors are clpC2, fug1, sco1, and GPA1, mutational effets, overview
additional information
the cells in green sectors of variegation mutant var2 have normal-appearing chloroplasts whereas cells in the white sectors have abnormal plastids that lack pigments and organized lamellae. The mutant serves as threshold model in which the formation of chloroplasts is due to the presence of activities/processes that are able to compensate for a lack of VAR2, mechanisms of variegation suppression, including an unexpected link between var2 variegation and chloroplast translation, phenotype and mutant screening, detailed overview. The enhancement in green sector formation is accompanied by an increased accumulation of chloroplast FtsH mRNA and protein. Overexpressionj of isozyme AtFtsH8 suppresses the var2 phenotype. Isolation and analysis of mutant svr1-1, i.e. suppression of variegation1-1, and of svr2 mutant, overview. Examples of var2 suppressors are clpC2, fug1, sco1, and GPA1, mutational effets, overview
additional information
the cells in green sectors of variegation mutant var2 have normal-appearing chloroplasts whereas cells in the white sectors have abnormal plastids that lack pigments and organized lamellae. The mutant serves as threshold model in which the formation of chloroplasts is due to the presence of activities/processes that are able to compensate for a lack of VAR2, mechanisms of variegation suppression, including an unexpected link between var2 variegation and chloroplast translation, phenotype and mutant screening, detailed overview. The enhancement in green sector formation is accompanied by an increased accumulation of chloroplast FtsH mRNA and protein. Overexpressionj of isozyme AtFtsH8 suppresses the var2 phenotype. Isolation and analysis of mutant svr1-1, i.e. suppression of variegation1-1, and of svr2 mutant, overview. Examples of var2 suppressors are clpC2, fug1, sco1, and GPA1, mutational effets, overview
additional information
the cells in green sectors of variegation mutant var2 have normal-appearing chloroplasts whereas cells in the white sectors have abnormal plastids that lack pigments and organized lamellae. The mutant serves as threshold model in which the formation of chloroplasts is due to the presence of activities/processes that are able to compensate for a lack of VAR2, mechanisms of variegation suppression, including an unexpected link between var2 variegation and chloroplast translation, phenotype and mutant screening, detailed overview. The enhancement in green sector formation is accompanied by an increased accumulation of chloroplast FtsH mRNA and protein. Overexpressionj of isozyme AtFtsH8 suppresses the var2 phenotype. Isolation and analysis of mutant svr1-1, i.e. suppression of variegation1-1, and of svr2 mutant, overview. Examples of var2 suppressors are clpC2, fug1, sco1, and GPA1, mutational effets, overview
additional information
the cells in green sectors of variegation mutant var2 have normal-appearing chloroplasts whereas cells in the white sectors have abnormal plastids that lack pigments and organized lamellae. The mutant serves as threshold model in which the formation of chloroplasts is due to the presence of activities/processes that are able to compensate for a lack of VAR2, mechanisms of variegation suppression, including an unexpected link between var2 variegation and chloroplast translation, phenotype and mutant screening, detailed overview. The enhancement in green sector formation is accompanied by an increased accumulation of chloroplast FtsH mRNA and protein. Overexpressionj of isozyme AtFtsH8 suppresses the var2 phenotype. Isolation and analysis of mutant svr1-1, i.e. suppression of variegation1-1, and of svr2 mutant, overview. Examples of var2 suppressors are clpC2, fug1, sco1, and GPA1, mutational effets, overview
additional information
the cells in green sectors of variegation mutant var2 have normal-appearing chloroplasts whereas cells in the white sectors have abnormal plastids that lack pigments and organized lamellae. The mutant serves as threshold model in which the formation of chloroplasts is due to the presence of activities/processes that are able to compensate for a lack of VAR2, mechanisms of variegation suppression, including an unexpected link between var2 variegation and chloroplast translation, phenotype and mutant screening, detailed overview. The enhancement in green sector formation is accompanied by an increased accumulation of chloroplast FtsH mRNA and protein. Overexpressionj of isozyme AtFtsH8 suppresses the var2 phenotype. Isolation and analysis of mutant svr1-1, i.e. suppression of variegation1-1, and of svr2 mutant, overview. Examples of var2 suppressors are clpC2, fug1, sco1, and GPA1, mutational effets, overview
additional information
the cells in green sectors of variegation mutant var2 have normal-appearing chloroplasts whereas cells in the white sectors have abnormal plastids that lack pigments and organized lamellae. The mutant serves as threshold model in which the formation of chloroplasts is due to the presence of activities/processes that are able to compensate for a lack of VAR2, mechanisms of variegation suppression, including an unexpected link between var2 variegation and chloroplast translation, phenotype and mutant screening, detailed overview. The enhancement in green sector formation is accompanied by an increased accumulation of chloroplast FtsH mRNA and protein. Overexpressionj of isozyme AtFtsH8 suppresses the var2 phenotype. Isolation and analysis of mutant svr1-1, i.e. suppression of variegation1-1, and of svr2 mutant, overview. Examples of var2 suppressors are clpC2, fug1, sco1, and GPA1, mutational effets, overview
additional information
the cells in green sectors of variegation mutant var2 have normal-appearing chloroplasts whereas cells in the white sectors have abnormal plastids that lack pigments and organized lamellae. The mutant serves as threshold model in which the formation of chloroplasts is due to the presence of activities/processes that are able to compensate for a lack of VAR2, mechanisms of variegation suppression, including an unexpected link between var2 variegation and chloroplast translation, phenotype and mutant screening, detailed overview. The enhancement in green sector formation is accompanied by an increased accumulation of chloroplast FtsH mRNA and protein. Overexpressionj of isozyme AtFtsH8 suppresses the var2 phenotype. Isolation and analysis of mutant svr1-1, i.e. suppression of variegation1-1, and of svr2 mutant, overview. Examples of var2 suppressors are clpC2, fug1, sco1, and GPA1, mutational effets, overview
additional information
the cells in green sectors of variegation mutant var2 have normal-appearing chloroplasts whereas cells in the white sectors have abnormal plastids that lack pigments and organized lamellae. The mutant serves as threshold model in which the formation of chloroplasts is due to the presence of activities/processes that are able to compensate for a lack of VAR2, mechanisms of variegation suppression, including an unexpected link between var2 variegation and chloroplast translation, phenotype and mutant screening, detailed overview. The enhancement in green sector formation is accompanied by an increased accumulation of chloroplast FtsH mRNA and protein. Overexpressionj of isozyme AtFtsH8 suppresses the var2 phenotype. Isolation and analysis of mutant svr1-1, i.e. suppression of variegation1-1, and of svr2 mutant, overview. Examples of var2 suppressors are clpC2, fug1, sco1, and GPA1, mutational effets, overview
additional information
the cells in green sectors of variegation mutant var2 have normal-appearing chloroplasts whereas cells in the white sectors have abnormal plastids that lack pigments and organized lamellae. The mutant serves as threshold model in which the formation of chloroplasts is due to the presence of activities/processes that are able to compensate for a lack of VAR2, mechanisms of variegation suppression, including an unexpected link between var2 variegation and chloroplast translation, phenotype and mutant screening, detailed overview. The enhancement in green sector formation is accompanied by an increased accumulation of chloroplast FtsH mRNA and protein. Overexpressionj of isozyme AtFtsH8 suppresses the var2 phenotype. Isolation and analysis of mutant svr1-1, i.e. suppression of variegation1-1, and of svr2 mutant, overview. Examples of var2 suppressors are clpC2, fug1, sco1, and GPA1, mutational effets, overview
additional information
the cells in green sectors of variegation mutant var2 have normal-appearing chloroplasts whereas cells in the white sectors have abnormal plastids that lack pigments and organized lamellae. The mutant serves as threshold model in which the formation of chloroplasts is due to the presence of activities/processes that are able to compensate for a lack of VAR2, mechanisms of variegation suppression, including an unexpected link between var2 variegation and chloroplast translation, phenotype and mutant screening, detailed overview. The enhancement in green sector formation is accompanied by an increased accumulation of chloroplast FtsH mRNA and protein. Overexpressionj of isozyme AtFtsH8 suppresses the var2 phenotype. Isolation and analysis of mutant svr1-1, i.e. suppression of variegation1-1, and of svr2 mutant, overview. Examples of var2 suppressors are clpC2, fug1, sco1, and GPA1, mutational effets, overview
additional information
the cells in green sectors of variegation mutant var2 have normal-appearing chloroplasts whereas cells in the white sectors have abnormal plastids that lack pigments and organized lamellae. The mutant serves as threshold model in which the formation of chloroplasts is due to the presence of activities/processes that are able to compensate for a lack of VAR2, mechanisms of variegation suppression, including an unexpected link between var2 variegation and chloroplast translation, phenotype and mutant screening, detailed overview. The enhancement in green sector formation is accompanied by an increased accumulation of chloroplast FtsH mRNA and protein. Overexpressionj of isozyme AtFtsH8 suppresses the var2 phenotype. Isolation and analysis of mutant svr1-1, i.e. suppression of variegation1-1, and of svr2 mutant, overview. Examples of var2 suppressors are clpC2, fug1, sco1, and GPA1, mutational effets, overview
additional information
the knockout mutant of gene AtFtsH1 shows no visible phenotype
additional information
the knockout mutant of gene AtFtsH1 shows no visible phenotype
additional information
the knockout mutant of gene AtFtsH1 shows no visible phenotype
additional information
the knockout mutant of gene AtFtsH1 shows no visible phenotype
additional information
the knockout mutant of gene AtFtsH1 shows no visible phenotype
additional information
the knockout mutant of gene AtFtsH1 shows no visible phenotype
additional information
the knockout mutant of gene AtFtsH1 shows no visible phenotype
additional information
the knockout mutant of gene AtFtsH1 shows no visible phenotype
additional information
the knockout mutant of gene AtFtsH1 shows no visible phenotype
additional information
the knockout mutant of gene AtFtsH1 shows no visible phenotype
additional information
the knockout mutant of gene AtFtsH1 shows no visible phenotype
additional information
the knockout mutant of gene AtFtsH1 shows no visible phenotype
additional information
the knockout mutant of gene AtFtsH10 shows reduced activity of mitochondrial complex I and V
additional information
the knockout mutant of gene AtFtsH10 shows reduced activity of mitochondrial complex I and V
additional information
the knockout mutant of gene AtFtsH10 shows reduced activity of mitochondrial complex I and V
additional information
the knockout mutant of gene AtFtsH10 shows reduced activity of mitochondrial complex I and V
additional information
the knockout mutant of gene AtFtsH10 shows reduced activity of mitochondrial complex I and V
additional information
the knockout mutant of gene AtFtsH10 shows reduced activity of mitochondrial complex I and V
additional information
the knockout mutant of gene AtFtsH10 shows reduced activity of mitochondrial complex I and V
additional information
the knockout mutant of gene AtFtsH10 shows reduced activity of mitochondrial complex I and V
additional information
the knockout mutant of gene AtFtsH10 shows reduced activity of mitochondrial complex I and V
additional information
the knockout mutant of gene AtFtsH10 shows reduced activity of mitochondrial complex I and V
additional information
the knockout mutant of gene AtFtsH10 shows reduced activity of mitochondrial complex I and V
additional information
the knockout mutant of gene AtFtsH10 shows reduced activity of mitochondrial complex I and V
additional information
the knockout mutant of gene AtFtsH3 shows reduced activity of mitochondrial complex I and V
additional information
the knockout mutant of gene AtFtsH3 shows reduced activity of mitochondrial complex I and V
additional information
the knockout mutant of gene AtFtsH3 shows reduced activity of mitochondrial complex I and V
additional information
the knockout mutant of gene AtFtsH3 shows reduced activity of mitochondrial complex I and V
additional information
the knockout mutant of gene AtFtsH3 shows reduced activity of mitochondrial complex I and V
additional information
the knockout mutant of gene AtFtsH3 shows reduced activity of mitochondrial complex I and V
additional information
the knockout mutant of gene AtFtsH3 shows reduced activity of mitochondrial complex I and V
additional information
the knockout mutant of gene AtFtsH3 shows reduced activity of mitochondrial complex I and V
additional information
the knockout mutant of gene AtFtsH3 shows reduced activity of mitochondrial complex I and V
additional information
the knockout mutant of gene AtFtsH3 shows reduced activity of mitochondrial complex I and V
additional information
the knockout mutant of gene AtFtsH3 shows reduced activity of mitochondrial complex I and V
additional information
the knockout mutant of gene AtFtsH3 shows reduced activity of mitochondrial complex I and V
additional information
the knockout mutant of gene AtFtsH4 shows altered late rosette leaf development and chloroplasts and mitochondria ultrastructure under short-day conditions
additional information
the knockout mutant of gene AtFtsH4 shows altered late rosette leaf development and chloroplasts and mitochondria ultrastructure under short-day conditions
additional information
the knockout mutant of gene AtFtsH4 shows altered late rosette leaf development and chloroplasts and mitochondria ultrastructure under short-day conditions
additional information
the knockout mutant of gene AtFtsH4 shows altered late rosette leaf development and chloroplasts and mitochondria ultrastructure under short-day conditions
additional information
the knockout mutant of gene AtFtsH4 shows altered late rosette leaf development and chloroplasts and mitochondria ultrastructure under short-day conditions
additional information
the knockout mutant of gene AtFtsH4 shows altered late rosette leaf development and chloroplasts and mitochondria ultrastructure under short-day conditions
additional information
the knockout mutant of gene AtFtsH4 shows altered late rosette leaf development and chloroplasts and mitochondria ultrastructure under short-day conditions
additional information
the knockout mutant of gene AtFtsH4 shows altered late rosette leaf development and chloroplasts and mitochondria ultrastructure under short-day conditions
additional information
the knockout mutant of gene AtFtsH4 shows altered late rosette leaf development and chloroplasts and mitochondria ultrastructure under short-day conditions
additional information
the knockout mutant of gene AtFtsH4 shows altered late rosette leaf development and chloroplasts and mitochondria ultrastructure under short-day conditions
additional information
the knockout mutant of gene AtFtsH4 shows altered late rosette leaf development and chloroplasts and mitochondria ultrastructure under short-day conditions
additional information
the knockout mutant of gene AtFtsH4 shows altered late rosette leaf development and chloroplasts and mitochondria ultrastructure under short-day conditions
additional information
the knockout mutant of gene AtFtsH4 shows no visible phenotype, but is unable to degrade LHC II
additional information
the knockout mutant of gene AtFtsH4 shows no visible phenotype, but is unable to degrade LHC II
additional information
the knockout mutant of gene AtFtsH4 shows no visible phenotype, but is unable to degrade LHC II
additional information
the knockout mutant of gene AtFtsH4 shows no visible phenotype, but is unable to degrade LHC II
additional information
the knockout mutant of gene AtFtsH4 shows no visible phenotype, but is unable to degrade LHC II
additional information
the knockout mutant of gene AtFtsH4 shows no visible phenotype, but is unable to degrade LHC II
additional information
the knockout mutant of gene AtFtsH4 shows no visible phenotype, but is unable to degrade LHC II
additional information
the knockout mutant of gene AtFtsH4 shows no visible phenotype, but is unable to degrade LHC II
additional information
the knockout mutant of gene AtFtsH4 shows no visible phenotype, but is unable to degrade LHC II
additional information
the knockout mutant of gene AtFtsH4 shows no visible phenotype, but is unable to degrade LHC II
additional information
the knockout mutant of gene AtFtsH4 shows no visible phenotype, but is unable to degrade LHC II
additional information
the knockout mutant of gene AtFtsH4 shows no visible phenotype, but is unable to degrade LHC II
additional information
the knockout mutant of gene AtFtsH5 shows variegated leaves, overexpression of isozyme AtFtsH1 suppresses the var1 phenotype
additional information
the knockout mutant of gene AtFtsH5 shows variegated leaves, overexpression of isozyme AtFtsH1 suppresses the var1 phenotype
additional information
the knockout mutant of gene AtFtsH5 shows variegated leaves, overexpression of isozyme AtFtsH1 suppresses the var1 phenotype
additional information
the knockout mutant of gene AtFtsH5 shows variegated leaves, overexpression of isozyme AtFtsH1 suppresses the var1 phenotype
additional information
the knockout mutant of gene AtFtsH5 shows variegated leaves, overexpression of isozyme AtFtsH1 suppresses the var1 phenotype
additional information
the knockout mutant of gene AtFtsH5 shows variegated leaves, overexpression of isozyme AtFtsH1 suppresses the var1 phenotype
additional information
the knockout mutant of gene AtFtsH5 shows variegated leaves, overexpression of isozyme AtFtsH1 suppresses the var1 phenotype
additional information
the knockout mutant of gene AtFtsH5 shows variegated leaves, overexpression of isozyme AtFtsH1 suppresses the var1 phenotype
additional information
the knockout mutant of gene AtFtsH5 shows variegated leaves, overexpression of isozyme AtFtsH1 suppresses the var1 phenotype
additional information
the knockout mutant of gene AtFtsH5 shows variegated leaves, overexpression of isozyme AtFtsH1 suppresses the var1 phenotype
additional information
the knockout mutant of gene AtFtsH5 shows variegated leaves, overexpression of isozyme AtFtsH1 suppresses the var1 phenotype
additional information
the knockout mutant of gene AtFtsH5 shows variegated leaves, overexpression of isozyme AtFtsH1 suppresses the var1 phenotype
additional information
the knockout mutant of gene AtFtsH8 shows no visible phenotype
additional information
the knockout mutant of gene AtFtsH8 shows no visible phenotype
additional information
the knockout mutant of gene AtFtsH8 shows no visible phenotype
additional information
the knockout mutant of gene AtFtsH8 shows no visible phenotype
additional information
the knockout mutant of gene AtFtsH8 shows no visible phenotype
additional information
the knockout mutant of gene AtFtsH8 shows no visible phenotype
additional information
the knockout mutant of gene AtFtsH8 shows no visible phenotype
additional information
the knockout mutant of gene AtFtsH8 shows no visible phenotype
additional information
the knockout mutant of gene AtFtsH8 shows no visible phenotype
additional information
the knockout mutant of gene AtFtsH8 shows no visible phenotype
additional information
the knockout mutant of gene AtFtsH8 shows no visible phenotype
additional information
the knockout mutant of gene AtFtsH8 shows no visible phenotype
additional information
-
generation of ftsH knockouts, that show a sporulation frequency reduced by several orders of magnitude. The combination of ftsH knockout with knockout of one of the phosphatases RapA, RapB, RapE or Spo0E results in a sporulation frequency, that is increased by two to three orders of magnitude, but still remains below 1% of wild-type level, overview
additional information
-
mutants lacking 5 or 10 amino acid residues in the exposed N-terminal region of the D1 protein are blocked in the synthesis of D1 protein, photosystem II repair and selective D1 degradation are inhibited in the A20 truncation mutant
additional information
-
insertional inactivation of two of the four genes, slr1390 and slr1604, is lethal, while inactivation of sll1463 does not have an obvious affect and inactivation of slr0228 produces cells with altered pigmentation and a significant reduction in the amount of PSI
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Boeckmann, B.; Bairoch, A.; Apweiler, R.; Blatter, M.C.; Estreicher, A.; Gasteiger, E.; Martin M.J.; Michoud, K.; O'Donovan, C.; Phan, I.; Pilbout, S.; Schneider, M.
The SWISS-PROT protein knowledgebase and its supplement TrEMBL
Nucleic Acids Res.
31
365-370
2003
Arabidopsis thaliana (O80860)
brenda
Langer, T.; Kaser, M.; Klanner, C.; Leonhard, K.
AAA proteases of mitochondria: quality control of membrane proteins and regulatory functions during mitochondrial biogenesis
Biochem. Soc. Trans.
29
431-436
2001
Arabidopsis thaliana
brenda
Lindahl, M.; Tabak, S.; Cseke, L.; Pichersky, E.; Andersson, B.; Adam, Z.
Identification, characterization, and molecular cloning of a homologue of the bacterial FtsH protease in chloroplasts of higher plants
J. Biol. Chem.
271
29329-29334
1996
Pisum sativum, Spinacia oleracea, Arabidopsis thaliana (Q39102)
brenda
Bailey, S.; Thompson, E.; Nixon, P.J.; Horton, P.; Mullineaux, C.W.; Robinson, C.; Mann, N.H.
A critical role for the Var2 FtsH homologue of Arabidopsis thaliana in the photosystem II repair cycle in vivo
J. Biol. Chem.
277
2006-2011
2002
Arabidopsis thaliana
brenda
Lindahl, M.; Spetea, C.; Hundal, T.; Oppenheim, A.B.; Adam, Z.; Andersson, B.
The thylakoid FtsH protease plays a role in the light-induced turnover of the photosystem II D1 protein
Plant Cell
12
419-431
2000
Pisum sativum
brenda
Ostersetzer, O.; Adam, Z.
Light-stimulated degradation of an unassembled Rieske FeS protein by a thylakoid-bound protease: the possible role of the FtsH protease
Plant Cell
9
957-965
1997
Pisum sativum
brenda
Chen, M.; Choi, Y.; Voytas, D.F.; Rodermel, S.
Mutations in the Arabidopsis VAR2 locus cause leaf variegation due to the loss of a chloroplast FtsH protease
Plant J.
22
303-313
2000
Arabidopsis thaliana (Q39102)
brenda
Adam, Z.
The chloroplast proteolytic machinery
Annu. Plant Rev.
13
214-236
2005
Synechocystis sp., Arabidopsis thaliana
-
brenda
Adam, Z.; Rudella, A.; van Wijk, K.J.
Recent advances in the study of Clp, FtsH and other proteases located in chloroplasts
Curr. Opin. Plant Biol.
9
234-240
2006
Arabidopsis thaliana
brenda
Komenda, J.; Barker, M.; Kuvikova, S.; de Vries, R.; Mullineaux, C.W.; Tichy, M.; Nixon, P.J.
The FtsH protease slr0228 is important for quality control of photosystem II in the thylakoid membrane of Synechocystis sp. PCC 6803
J. Biol. Chem.
281
1145-1151
2006
Synechocystis sp.
brenda
Yoshioka, M.; Uchida, S.; Mori, H.; Komayama, K.; Ohira, S.; Morita, N.; Nakanishi, T.; Yamamoto, Y.
Quality control of photosystem II. Cleavage of reaction center D1 protein in spinach thylakoids by FtsH protease under moderate heat stress
J. Biol. Chem.
281
21660-21669
2006
Spinacia oleracea
brenda
Nixon, P.J.; Barker, M.; Boehm, M.; de Vries, R.; Komenda, J.
FtsH-mediated repair of the photosystem II complex in response to light stress
J. Exp. Bot.
56
357-363
2005
Synechocystis sp.
brenda
Kamata, T.; Hiramoto, H.; Morita, N.; Shen, J.R.; Mann, N.H.; Yamamoto, Y.
Quality control of Photosystem II: an FtsH protease plays an essential role in the turnover of the reaction center D1 protein in Synechocystis PCC 6803 under heat stress as well as light stress conditions
Photochem. Photobiol. Sci.
4
983-990
2005
Synechocystis sp.
brenda
Zaltsman, A.; Ori, N.; Adam, Z.
Two types of FtsH protease subunits are required for chloroplast biogenesis and photosystem II repair in Arabidopsis
Plant Cell
17
2782-2790
2005
Arabidopsis thaliana (O80860), Arabidopsis thaliana (Q39102), Arabidopsis thaliana (Q8W585), Arabidopsis thaliana (Q9FH02), Arabidopsis thaliana
brenda
Yu, F.; Park, S.; Rodermel, S.R.
The Arabidopsis FtsH metalloprotease gene family: interchangeability of subunits in chloroplast oligomeric complexes
Plant J.
37
864-876
2004
Arabidopsis thaliana
brenda
Zaltsman, A.; Feder, A.; Adam, Z.
Developmental and light effects on the accumulation of FtsH protease in Arabidopsis chloroplasts--implications for thylakoid formation and photosystem II maintenance
Plant J.
42
609-617
2005
Arabidopsis thaliana
brenda
Chen, J.; Burke, J.J.; Velten, J.; Xin, Z.
FtsH11 protease plays a critical role in Arabidopsis thermotolerance
Plant J.
48
73-84
2006
Arabidopsis thaliana
brenda
Sinvany-Villalobo, G.; Davydov, O.; Ben-Ari, G.; Zaltsman, A.; Raskind, A.; Adam, Z.
Expression in multigene families. Analysis of chloroplast and mitochondrial proteases
Plant Physiol.
135
1336-1345
2004
Arabidopsis thaliana
brenda
Yu, F.; Park, S.; Rodermel, S.R.
Functional redundancy of AtFtsH metalloproteases in thylakoid membrane complexes
Plant Physiol.
138
1957-1966
2005
Arabidopsis thaliana
brenda
Zelisko, A.; Garcia-Lorenzo, M.; Jackowski, G.; Jansson, S.; Funk, C.
AtFtsH6 is involved in the degradation of the light-harvesting complex II during high-light acclimation and senescence
Proc. Natl. Acad. Sci. USA
102
13699-13704
2005
Arabidopsis thaliana
brenda
Cheregi, O.; Sicora, C.; Kos, P.B.; Barker, M.; Nixon, P.J.; Vass, I.
The role of the FtsH and Deg proteases in the repair of UV-B radiation-damaged Photosystem II in the cyanobacterium Synechocystis PCC 6803
Biochim. Biophys. Acta
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820-828
2007
Synechocystis sp.
brenda
Stirnberg, M.; Fulda, S.; Huckauf, J.; Hagemann, M.; Kraemer, R.; Marin, K.
A membrane-bound FtsH protease is involved in osmoregulation in Synechocystis sp. PCC 6803: the compatible solute synthesizing enzyme GgpS is one of the targets for proteolysis
Mol. Microbiol.
63
86-102
2007
Synechocystis sp.
brenda
Zhang, P.; Sicora, C.I.; Vorontsova, N.; Allahverdiyeva, Y.; Battchikova, N.; Nixon, P.J.; Aro, E.M.
FtsH protease is required for induction of inorganic carbon acquisition complexes in Synechocystis sp. PCC 6803
Mol. Microbiol.
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2007
Synechocystis sp.
brenda
Kolodziejczak, M.; Gibala, M.; Urantowka, A.; Janska, H.
The significance of Arabidopsis AAA proteases for activity and assembly/stability of mitochondrial OXPHOS complexes
Physiol. Plant.
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2007
Arabidopsis thaliana
brenda
Komenda, J.; Tichy, M.; Prasil, O.; Knoppova, J.; Kuvikova, S.; de Vries, R.; Nixon, P.J.
The exposed N-terminal tail of the D1 subunit is required for rapid D1 degradation during photosystem II repair in Synechocystis sp PCC 6803
Plant Cell
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2839-2854
2007
Synechocystis sp.
brenda
Shen, G.; Adam, Z.; Zhang, H.
The E3 ligase AtCHIP ubiquitylates FtsH1, a component of the chloroplast FtsH protease, and affects protein degradation in chloroplasts
Plant J.
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309-321
2007
Arabidopsis thaliana
brenda
Sun, A.; Yi, S.; Yang, J.; Zhao, C.; Liu, J.
Identification and characterization of a heat-inducible ftsH gene from tomato (Lycopersicon esculentum Mill.)
Plant Sci.
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551-562
2006
Solanum lycopersicum (Q4W5U8)
brenda
Obrist, M.; Langklotz, S.; Milek, S.; Fuehrer, F.; Narberhaus, F.
Region C of the Escherichia coli heat shock sigma factor RpoH (sigma 32) contains a turnover element for proteolysis by the FtsH protease
FEMS Microbiol. Lett.
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199-208
2009
Escherichia coli
brenda
Bandyopadhyay, K.; Parua, P.K.; Datta, A.B.; Parrack, P.
Escherichia coli HflK and HflC can individually inhibit the HflB (FtsH)-mediated proteolysis of lambdaCII in vitro
Arch. Biochem. Biophys.
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2010
Escherichia coli
brenda
Komenda, J.; Knoppova, J.; Krynicka, V.; Nixon, P.J.; Tichy, M.
Role of FtsH2 in the repair of photosystem II in mutants of the cyanobacterium Synechocystis PCC 6803 with impaired assembly or stability of the CaMn4 cluster
Biochim. Biophys. Acta
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566-575
2010
Synechocystis sp. (Q55700), Synechocystis sp.
brenda
Liu, X.; Yu, F.; Rodermel, S.
Arabidopsis chloroplast FtsH, var2 and suppressors of var2 leaf variegation: a review
J. Integr. Plant Biol.
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750-761
2010
Synechocystis sp., Escherichia coli, Arabidopsis thaliana (O80860), Arabidopsis thaliana (O80983), Arabidopsis thaliana (Q1PDW5), Arabidopsis thaliana (Q39102), Arabidopsis thaliana (Q84WU8), Arabidopsis thaliana (Q8VZI8), Arabidopsis thaliana (Q8W585), Arabidopsis thaliana (Q9FGM0), Arabidopsis thaliana (Q9FH02), Arabidopsis thaliana (Q9FIM2), Arabidopsis thaliana (Q9SAJ3), Arabidopsis thaliana (Q9SD67)
brenda
Ayuso-Tejedor, S.; Nishikori, S.; Okuno, T.; Ogura, T.; Sancho, J.
FtsH cleavage of non-native conformations of proteins
J. Struct. Biol.
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2010
Escherichia coli
brenda
Le, A.T.; Schumann, W.
The Spo0E phosphatase of Bacillus subtilis is a substrate of the FtsH metalloprotease
Microbiology
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1122-1132
2009
Bacillus subtilis
brenda
Yue, G.; Hu, X.; He, Y.; Yang, A.; Zhang, J.
Identification and characterization of two members of the FtsH gene family in maize (Zea mays L.)
Mol. Biol. Rep.
37
855-863
2010
Zea mays (B1P2H3), Zea mays (B1P2H4), Zea mays, Zea mays DH4866 (B1P2H3), Zea mays DH4866 (B1P2H4)
brenda
Yamamoto, Y.; Aminaka, R.; Yoshioka, M.; Khatoon, M.; Komayama, K.; Takenaka, D.; Yamashita, A.; Nijo, N.; Inagawa, K.; Morita, N.; Sasaki, T.; Yamamoto, Y.
Quality control of photosystem II: impact of light and heat stresses
Photosynth. Res.
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589-608
2008
Synechocystis sp., Spinacia oleracea, Arabidopsis thaliana (O80860), Arabidopsis thaliana (O80983), Arabidopsis thaliana (Q1PDW5), Arabidopsis thaliana (Q39102), Arabidopsis thaliana (Q84WU8), Arabidopsis thaliana (Q8VZI8), Arabidopsis thaliana (Q8W585), Arabidopsis thaliana (Q9FGM0), Arabidopsis thaliana (Q9FH02), Arabidopsis thaliana (Q9FIM2), Arabidopsis thaliana (Q9SAJ3), Arabidopsis thaliana (Q9SD67), Escherichia coli (P0AAI3)
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brenda
Zhang, L.; Wei, Q.; Wu, W.; Cheng, Y.; Hu, G.; Hu, F.; Sun, Y.; Zhu, Y.; Sakamoto, W.; Huang, J.
Activation of the heterotrimeric G protein alpha-subunit GPA1 suppresses the ftsh-mediated inhibition of chloroplast development in Arabidopsis
Plant J.
58
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2009
Arabidopsis thaliana
brenda
Bieniossek, C.; Niederhauser, B.; Baumann, U.M.
The crystal structure of apo-FtsH reveals domain movements necessary for substrate unfolding and translocation
Proc. Natl. Acad. Sci. USA
106
21579-21584
2009
Thermotoga maritima (Q9WZ49)
brenda
Gomez-Baena, G.; Rangel, O.A.; Lopez-Lozano, A.; Garcia-Fernandez, J.M.; Diez, J.
Stress responses in Prochlorococcus MIT9313 vs. SS120 involve differential expression of genes encoding proteases ClpP, FtsH and Lon
Res. Microbiol.
160
567-575
2009
Prochlorococcus marinus
brenda
Narberhaus, F.; Obrist, M.; Fuehrer, F.; Langklotz, S.
Degradation of cytoplasmic substrates by FtsH, a membrane-anchored protease with many talents
Res. Microbiol.
160
652-659
2009
Escherichia coli
brenda
Kiran, M.; Chauhan, A.; Dziedzic, R.; Maloney, E.; Mukherji, S.K.; Madiraju, M.; Rajagopalan, M.
Mycobacterium tuberculosis ftsH expression in response to stress and viability
Tuberculosis
89 Suppl 1
S70-S73
2009
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
brenda
Yoshioka, M.; Nakayama, Y.; Yoshida, M.; Ohashi, K.; Morita, N.; Kobayashi, H.; Yamamoto, Y.
Quality control of photosystem II: FtsH hexamers are localized near photosystem II at grana for the swift repair of damage
J. Biol. Chem.
285
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2010
Spinacia oleracea
brenda
Chauleau, M.; Mora, L.; Serba, J.; de Zamaroczy, M.
FtsH-dependent processing of RNase colicins D and E3 means that only the cytotoxic domains are imported into the cytoplasm
J. Biol. Chem.
286
29397-29407
2011
Escherichia coli
brenda
Yoshioka, M.; Yamamoto, Y.
Quality control of Photosystem II: Where and how does the degradation of the D1 protein by FtsH proteases start under light stress? - Facts and hypotheses
J. Photochem. Photobiol. B
104
229-235
2011
Synechocystis sp., Arabidopsis thaliana, Spinacia oleracea
brenda
Kato, Y.; Kouso, T.; Sakamoto, W.
Variegated tobacco leaves generated by chloroplast FtsH suppression: implication of FtsH function in the maintenance of thylakoid membranes
Plant Cell Physiol.
53
391-404
2012
Nicotiana tabacum
brenda
Zhang, D.; Kato, Y.; Zhang, L.; Fujimoto, M.; Tsutsumi, N.; Sodmergen, N.; Sakamoto, W.
The FtsH protease heterocomplex in Arabidopsis: dispensability of type-B protease activity for proper chloroplast development
Plant Cell
22
3710-3725
2010
Arabidopsis thaliana
brenda
Adam, Z.; Frottin, F.; Espagne, C.; Meinnel, T.; Giglione, C.
Interplay between N-terminal methionine excision and FtsH protease is essential for normal chloroplast development and function in Arabidopsis
Plant Cell
23
3745-3760
2011
Arabidopsis thaliana
brenda
Rodrigues, R.A.; Silva-Filho, M.C.; Cline, K.
FtsH2 and FtsH5: two homologous subunits use different integration mechanisms leading to the same thylakoid multimeric complex
Plant J.
65
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2011
Arabidopsis thaliana
brenda
Vostrukhina, M.; Popov, A.; Brunstein, E.; Lanz, M.A.; Baumgartner, R.; Bieniossek, C.; Schacherl, M.; Baumann, U.
The structure of Aquifex aeolicus FtsH in the ADP-bound state reveals a C2-symmetric hexamer
Acta Crystallogr. Sect. D
71
1307-1318
2015
Aquifex aeolicus (O67077)
brenda
Yoshioka-Nishimura, M.; Yamamoto, Y.
Quality control of Photosystem II: The molecular basis for the action of FtsH protease and the dynamics of the thylakoid membranes
J. Photochem. Photobiol. B
137
100-106
2014
Arabidopsis thaliana, Spinacia oleracea
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brenda
Krynicka, V.; Tichy, M.; Krafl, J.; Yu, J.; Ka?a, R.; Boehm, M.; Nixon, P.J.; Komenda, J.
Two essential FtsH proteases control the level of the Fur repressor during iron deficiency in the cyanobacterium Synechocystis sp. PCC 6803
Mol. Microbiol.
94
609-624
2014
Synechocystis sp. (P72991), Synechocystis sp. (P73179), Synechocystis sp. (P73437), Synechocystis sp. (Q55700), Synechocystis sp.
brenda
Sacharz, J.; Bryan, S.J.; Yu, J.; Burroughs, N.J.; Spence, E.M.; Nixon, P.J.; Mullineaux, C.W.
Sub-cellular location of FtsH proteases in the cyanobacterium Synechocystis sp. PCC 6803 suggests localised PSII repair zones in the thylakoid membranes
Mol. Microbiol.
96
448-462
2015
Synechocystis sp. (P72991), Synechocystis sp. (P73179), Synechocystis sp. (P73437), Synechocystis sp. (Q55700), Synechocystis sp.
brenda
Seemueller, E.; Sule, S.; Kube, M.; Jelkmann, W.; Schneider, B.
The AAA+ ATPases and HflB/FtsH proteases of Candidatus Phytoplasma mali: phylogenetic diversity, membrane topology, and relationship to strain virulence
Mol. Plant Microbe Interact.
26
367-376
2013
Candidatus Phytoplasma mali
brenda
Campbell, D.A.; Hossain, Z.; Cockshutt, A.M.; Zhaxybayeva, O.; Wu, H.; Li, G.
Photosystem II protein clearance and FtsH function in the diatom Thalassiosira pseudonana
Photosynth. Res.
115
43-54
2013
Thalassiosira pseudonana
brenda
Wagner, R.; Aigner, H.; Funk, C.
FtsH proteases located in the plant chloroplast
Physiol. Plant.
145
203-214
2012
Arabidopsis thaliana
brenda
Yoshioka-Nishimura, M.; Nanba, D.; Takaki, T.; Ohba, C.; Tsumura, N.; Morita, N.; Sakamoto, H.; Murata, K.; Yamamoto, Y.
Quality control of photosystem II: direct imaging of the changes in the thylakoid structure and distribution of FtsH proteases in spinach chloroplasts under light stress
Plant Cell Physiol.
55
1255-1265
2014
Spinacia oleracea
brenda
Boehm, M.; Yu, J.; Krynicka, V.; Barker, M.; Tichy, M.; Komenda, J.; Nixon, P.J.; Nield, J.
Subunit organization of a Synechocystis hetero-oligomeric thylakoid FtsH complex involved in photosystem II repair
Plant Cell
24
3669-3683
2012
Synechocystis sp. (Q55700), Synechocystis sp.
brenda
Malnoe, A.; Wang, F.; Girard-Bascou, J.; Wollman, F.A.; de Vitry, C.
Thylakoid FtsH protease contributes to photosystem II and cytochrome b6f remodeling in Chlamydomonas reinhardtii under stress conditions
Plant Cell
26
373-390
2014
Chlamydomonas reinhardtii (A8IL08), Chlamydomonas reinhardtii
brenda
Zhang, S.; Zhang, D.; Yang, C.
AtFtsH4 perturbs the mitochondrial respiratory chain complexes and auxin homeostasis in Arabidopsis
Plant Signal. Behav.
9
1-4
2014
Arabidopsis thaliana
brenda
Moldavski, O.; Levin-Kravets, O.; Ziv, T.; Adam, Z.; Prag, G.
The hetero-hexameric nature of a chloroplast AAA+ FtsH protease contributes to its thermodynamic stability
PLoS ONE
7
e36008
2012
Arabidopsis thaliana, Arabidopsis thaliana (O80860), Arabidopsis thaliana (Q9FH02)
brenda
Tanveer, A.; Allen, S.M.; Jackson, K.E.; Charan, M.; Ralph, S.A.; Habib, S.
An FtsH protease is recruited to the mitochondrion of Plasmodium falciparum
PLoS ONE
8
e74408
2013
Plasmodium falciparum
brenda
Chen, J.; Burke, J.J.; Xin, Z.
Chlorophyll fluorescence analysis revealed essential roles of FtsH11 protease in regulation of the adaptive responses of photosynthetic systems to high temperature
BMC Plant Biol.
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11
2018
Arabidopsis thaliana (Q9FGM0)
brenda
Kamal, S.; Rybtke, M.; Nimtz, M.; Sperlein, S.; Giske, C.; Trcek, J.; Deschamps, J.; Briandet, R.; Dini, L.; Jaensch, L.; Tolker-Nielsen, T.; Lee, C.; Roemling, U.
Two FtsH proteases contribute to fitness and adaptation of Pseudomonas aeruginosa clone C strains
Front. Microbiol.
10
1372
2019
Pseudomonas aeruginosa, Pseudomonas aeruginosa SG17M
brenda
Adam, Z.; Aviv-Sharon, E.; Keren-Paz, A.; Naveh, L.; Rozenberg, M.; Savidor, A.; Chen, J.
The chloroplast envelope protease FTSH11 - interaction with CPN60 and identification of potential substrates
Front. Plant Sci.
10
428
2019
Arabidopsis thaliana (Q9FGM0)
brenda
Ruer, M.; Krainer, G.; Groeger, P.; Schlierf, M.
ATPase and protease domain movements in the bacterial AAA+ protease FtsH are driven by thermal fluctuations
J. Mol. Biol.
430
4592-4602
2018
Thermotoga maritima (Q9WZ49), Thermotoga maritima DSM 3109 (Q9WZ49)
brenda
Uthoff, M.; Baumann, U.
Conformational flexibility of pore loop-1 gives insights into substrate translocation by the AAA+ protease FtsH
J. Struct. Biol.
204
199-206
2018
Aquifex aeolicus (O67077)
brenda
Wang, F.; Qi, Y.; Malnoe, A.; Choquet, Y.; Wollman, F.A.; de Vitry, C.
The high light response and redox control of thylakoid FtsH protease in Chlamydomonas reinhardtii
Mol. Plant
10
99-114
2017
Chlamydomonas reinhardtii (A8IL08 and A8J6C7), Chlamydomonas reinhardtii
brenda
Krynicka, V.; Shao, S.; Nixon, P.J.; Komenda, J.
Accessibility controls selective degradation of photosystem II subunits by FtsH protease
Nat. Plants
1
15168
2015
Synechocystis sp. PCC 6803 (Q55700 and P72991)
brenda
Beckova, M.; Yu, J.; Krynicka, V.; Kozlo, A.; Shao, S.; Konik, P.; Komenda, J.; Murray, J.W.; Nixon, P.J.
Structure of Psb29/Thf1 and its association with the FtsH protease complex involved in photosystem II repair in cyanobacteria
Philos. Trans. R. Soc. Lond. B Biol. Sci.
372
20160394
2017
Synechocystis sp. PCC 6803 (Q55700 and P72991)
brenda
Shao, S.; Cardona, T.; Nixon, P.
Early emergence of the FtsH proteases involved in photosystem II repair
Photosynthetica
56
163-177
2018
cellular organisms
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brenda
Bonisteel, E.; Turner, B.; Murphy, C.; Melanson, J.; Duff, N.; Beardsall, B.; Xu, K.; Campbell, D.; Cockshutt, A.
Strain specific differences in rates of photosystem II repair in picocyanobacteria correlate to differences in FtsH protein levels and isoform expression patterns
PLoS ONE
13
e0209115
2018
Prochlorococcus marinus (Q7V8H0), Prochlorococcus marinus, Prochlorococcus marinus MIT 9313 (Q7V8H0), Prochlorococcus marinus subsp. pastoris (Q7V1V9 and Q7V362), Prochlorococcus marinus subsp. pastoris MED4 (Q7V1V9 and Q7V362)
brenda
Wang, L.; Kim, C.; Xu, X.; Piskurewicz, U.; Dogra, V.; Singh, S.; Mahler, H.; Apel, K.
Singlet oxygen- and EXECUTER1-mediated signaling is initiated in grana margins and depends on the protease FtsH2
Proc. Natl. Acad. Sci. USA
113
E3792-E3800
2016
Arabidopsis thaliana (O80860)
brenda