3.4.21.53: Endopeptidase La
This is an abbreviated version!
For detailed information about Endopeptidase La, go to the full flat file.
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3.4.21.53
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amyloid
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clot
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kallikreins
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antithrombin
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urokinase-type
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pai-1
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fibrinolytic
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granzyme
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tissue-type
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tryptase
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medicine
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biotechnology
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agriculture
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diagnostics
- 3.4.21.53
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antiretroviral
- transcriptase
- cathepsins
- plasminogen
- coagulation
-
hiv-infected
- thrombin
- elastase
-
virological
- nucleoside
- neutrophil
- viruses
- endothelial
- pancreatic
- chymotrypsin
- lysosomal
- cd4
- collagen
- leukocyte
- plasmin
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caspase
- calpains
- proteasome
- platelet
- metalloproteinase
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amyloid
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anticoagulant
- clot
- kallikreins
- amylase
- heparin
- fibrinogen
- upa
- venom
- urokinase
- fibrin
- sars-cov-2
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mast
- covid-19
- coronavirus
-
zymography
-
thrombotic
- antithrombin
- papain
-
urokinase-type
- pai-1
-
fibrinolytic
-
granzyme
-
tissue-type
- tryptase
- medicine
- biotechnology
- agriculture
- diagnostics
Reaction
hydrolysis of proteins in presence of ATP =
Synonyms
AAA+ Lon protease, AAA+ protease, AAAP, AF0364, AfLon, archaeal Lon protease, ATP-dependent lon protease, ATP-dependent Lon proteinase, ATP-dependent PIM1 protease, ATP-dependent protease La, ATP-dependent protease lon, ATP-dependent protease LonA, ATP-dependent serine proteinase, ATP-independent Lon-like protease, bacterial protease lon, BPP1347, ClpXP, EcLon, Ec-Lon, Ec-Lon protease, EcLon, EcLon protease, ELon, Escherichia coli proteinase La, Escherichia coli serine proteinase La, Gene lon protease, Gene lon proteins, hLon, human ATP-dependent protease, human lon protease, HVO_0783, i-AAA Protease, la, La protease, lon, lon (la) protease, lon (Pim1p) protease, Lon AAA+ protease, lon ATP-dependent protease, lon protease, LON protease 1, Lon protein, Lon proteinase, lon-like protease, Lon-like-Ms, lon1, lon2, lon3, lon4, lonA, lonB, lonB protease, LonC, LonC protease, lonD, LONP1, lonR9, LONRF1, lonS, lonTK, lonV, mitochondrial ATP-dependent protease, mitochondrial ATP-dependent protease La, mitochondrial Lon protease, MLon, Ms-Lon, Msm 1754, Msm_1754, MtaLonA, MtaLonC, Nmag_2822, NmLon, non-canonical RNA viral Lon proteinase, peroxisomal Lon protease, PIM1, PIM1 protease, PIM1 proteinase, Pim1p, PLon, protease, Protease La, protease lon, Proteinase La, Proteinase, Escherichia coli serine, La, Proteinase, La, Proteins, gene lon, Proteins, specific or class, gene lon, ScLon, serine protease, Serine protease La, Ta1081, Thela2p4_005149, Thela2p4_006664, TK1264, TonLonB, TON_0529, yeast mitochondrial lon, yeast protease
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3.4.21.53 Endopeptidase LaAdvanced search results
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Engineering on EC 3.4.21.53 - Endopeptidase La
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
deltaTM(1)-lon-S509A
possesses neither proteolytic nor ATPase activity, is completely stable, can be considered as model of initial active delta TM(1)-lon forms
deltaTM(2)-lon-S509A
possesses neither proteolytic nor ATPase activity, is completely stable, can be considered as model of initial active delta TM(2)-lon forms
deltaTM1-lon
deletion of 100-186, leads to the removal of the predicted hydrophobic site of the transmembrane domain
deltaTM2-lon
deletion of 119-222, leads to the removal of the predicted hydrophobic site of the transmembrane domain
S684A
S714A
mutation of the predicted catalytic site serine residue. Mutant does not show catalytic activity. In presence of ATP, mutant exhibits a chaperone-like activity by inhibiting the aggregation of insulin beta-chain
D676N
E424Q
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site-directed mutagenesis, the mutant is unable to inactivate SulA in vivo and displays reduced rates of both basal and substrate-stimulated ATP hydrolysis. The mutant translocates and degrades CM-titinI27-sul20 and CM-titinI27-beta20 at a very slow rate. The mutation stabilizes the enzyme conformation that is active in relieving stress
E424Q/S679A
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site-directed mutagenesis, the mutant is unable to inactivate SulA in vivo and displays reduced rates of both basal and substrate-stimulated ATP hydrolysis
E614K
K362Q
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intersubunit domain-domain interactions between ATPase and proteolytic sites by complementation
K371E/K376E/R379E
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site-directed mutagenesis, mutant demonstrates significantly reduced DNA binding capabilities compared to wild-type enzyme. The Lon mutant does not restore cell length in the lon-/- strain, cells remained filamentous
Q220C
site-directed mutagenesis, the mutant reproducibly yields fast and robust intermolecular disulfide crosslinking. The cysteine-based disulfide crosslinking is responsible for the formation of the SDS-resistant dimers
R164A
R192A
site-directed mutagenesis, mutation of a HI(CC) domain residue, the mutant shows highly reduced ATPase activity in presence of beta-casein compared to the wild-type
R306E/K308E/K310E/K311E
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site-directed mutagenesis, the mutant demonstrates significantly reduced DNA binding capabilities compared to wild-type enzyme. The Lon mutant does not restore cell length in the lon-/- strain, cells remained filamentous
R542A
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site-directed mutagenesis, the mutant completely loses its ability to hydrolyze ATP, the mutant retains the ability to hydrolyze PepTBE in the absence of effectors
S679A
S679W
V217A/Q220A
site-directed mutagenesis, residues Val217 and Gln220 are present in a region predicted to form intermolecular coiled coils between hexamers, the Lon mutant variant (LonVQ) forms a dodecamer with increased stability compared to wild-type. The dodecamer is active, but it exhibits alterations in substrate selection and/or degradation. Mutant LonVQ is altered in recognition of dodecamer-sensitive substrates in vivo
V217C
site-directed mutagenesis, the mutant reproducibly yields fast and robust intermolecular disulfide crosslinking. The cysteine-based disulfide crosslinking is responsible for the formation of the SDS-resistant dimers
Y294A
site-directed mutagenesis, mutation of a HI(CC) domain residue, the mutant shows highly reduced ATPase activity in presence of beta-casein compared to the wild-type
Y398A
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site-directed mutagenesis, the mutant has basal ATP-hydrolysis activity similar to wild-type Lon, but displays substantially reduced rates of ATP hydrolysis in the presence of sul20- or beta20-tagged substrates
delta75-490
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dominant negative mutant, exhibits a remarkable decrease in acyl-CoA oxidase and mislocalization of catalase to the cytoplasm. Shows lower beta-oxidation activity than wild-type
G893A
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site-directed mutagenesis, the mutant shows 63% of wild-type ATPase activity, 80% of wild-type protease activity, and 2.27fold of the activation by beta-casein compared to the wild-type enzyme
G893A/G894A
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site-directed mutagenesis, the mutant shows 103% of wild-type ATPase activity, 79% of wild-type protease activity, and 0.745fold of the activation by beta-casein compared to the wild-type enzyme
G893A/G894P
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site-directed mutagenesis, the mutant shows 112% of wild-type ATPase activity, no protease activity, and 0.32fold of the activation by beta-casein compared to the wild-type enzyme
G893P
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site-directed mutagenesis, the mutant shows 89% of wild-type ATPase activity, no protease activity, and 0.49fold of the activation by beta-casein compared to the wild-type enzyme
G893P/G894A
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site-directed mutagenesis, the mutant shows 71% of wild-type ATPase activity, 8% of wild-type protease activity, and 0.23fold of the activation by beta-casein compared to the wild-type enzyme
G894A
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site-directed mutagenesis, the mutant shows 139% of wild-type ATPase activity, 76% of wild-type protease activity, and 0.49fold of the activation by beta-casein compared to the wild-type enzyme
G894P
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site-directed mutagenesis, the mutant shows 130% of wild-type ATPase activity, 84% of wild-type protease activity, and 0.23fold of the activation by beta-casein compared to the wild-type enzyme
G894S
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site-directed mutagenesis, the mutant shows 140% of wild-type ATPase activity, 47% of wild-type protease activity, and 0.88fold of the activation by beta-casein compared to the wild-type enzyme
S855A
S885A
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site-directed mutagenesis, three-dimensional structure of the ADP-bound Lon S885A mutant obtained by electron microscopy as a result of preliminary negative staining studies
T880V
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site-directed mutagenesis, the mutant shows 46% of wild-type ATPase activity, 107% of wild-type protease activity, and 3.28fold of the activation by beta-casein compared to the wild-type enzyme
W770A
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site-directed mutagenesis, the mutant shows 98.5% of wild-type ATPase activity, 6.4% of wild-type protease activity, and 0.305fold of the activation by beta-casein compared to the wild-type enzyme
W770P
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site-directed mutagenesis, the mutant shows 123% of wild-type ATPase activity, 55.3% of wild-type protease activity, and 0.64fold of the activation by beta-casein compared to the wild-type enzyme
E423Q
L91M/I359M
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site-directed mutagenesis, structure analysis with bound inhibitors
L91M/L188M/I359M
site-directed mutagenesis, the three mutations are introduced into the wild-type sequence to facilitate de novo phasing
R536/R584
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paddle-like movement of R536/R584 induced by the ATPase cycle at the groove may play an important role in substrate degradation
Y397G/I398G
site-directed mutagenesis, the mutant fails to degrade alpha-casein with Mg2+ and ATP. The Mg2+-activated double mutant showed wild-type-like ATP-independent proteolysis
K332A
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mutation results mostly in splicing, with some accumulation of branched-ester intermediate
K332H
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mutation results mostly in splicing, with some accumulation of branched-ester intermediate
N333A
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prevention of step three of the intein splicing, mutation results in the accumulation of precursor and branched-ester intermediate
K638N
S1015A
S680A
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displays both intrinsic and peptide-stimulated ATP hydrolysis activity comparable to that of the wild-type enzyme but is unable to catalyze peptide bond hydrolysis. Active site serine is required for interaction of inhibitor with lon
V378I
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naturally occurring conservative mutation
K568A
loss of peptidase activity, retention of ATPase activity and oligomerization to hexamer
S525A
loss of peptidase activity, retention of ATPase activity and oligomerization to hexamer
S654A
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site-directed mutagenesis, LonS654A is no longer able to be phosphorylated and the mutant loses its virulence. Pathogenicity can fully be restored by addition of exogenous wild-type N-terminally His-tagged HrpG, although not by C-terminally His-tagged HrpG
S654D
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site-directed mutagenesis, the mutant partially retaines its pathogenicity
S654E
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site-directed mutagenesis, the mutant retaines its pathogenicity
additional information
D676N
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is completely inactive for protein degradation, it retains some basal ATPase activity, but no activation of ATPase activity occurs upon binding of protein substrates
E614K
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is a dominant-negative mutant, can form mixed oligomers with wild-type lon and interferes with its activity
E614K
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mixed oligomeric complexes composed of wild-type lon and the inactive lon E614K mutant, results in an enzymatically inactive protein
R164A
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site-directed mutagenesis, the ATPase activity of the mutant is markedly reduced compared to the wild-type enzyme, thhe mutant retains the ability to hydrolyze PepTBE in the absence of effectors
R164A
site-directed mutagenesis, mutation of a HI(CC) domain residue, helix H3, the mutant shows highly reduced ATPase activity in presence of beta-casein compared to the wild-type
S679A
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inactive, intersubunit domain-domain interactions between ATPase and proteolytic sites by complementation
S679A
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proteolytically inactive, but wild-type-like intrinsic and peptide-stimulated ATPase activitiy. Two-step peptide S4 binding event, where a conformational change occurs after a rapid equilibrium peptide binding step
S679A
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complete loss of activity. Mutant is not capable of restoring the secB cold sensitive phenotype, indicating that the deleterious effect of Lon in the secB mutant is due to its protease activity
S679A
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site-directed mutagenesis, the S679A mutation destabilizes the enzyme conformation that is active in relieving stress
S679A
site-directed mutagenesis, the Lon trapping variant is able to translocate substrates but unable to degrade them, it is established and used for substrate determinations by mass spectrometry
S679W
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proteolytically inactive mutant. ATPase activity is affected by a variety of mutations generated at the vicinity of the proteolytic site Ser 679. Mutation of the ATP-binding site abolishes both the ATPase and protease activities of lon
S679W
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proteolytically inactive, but wild-type-like intrinsic and peptide-stimulated ATPase activitiy. Two-step peptide S4 binding event, where a conformational change occurs after a rapid equilibrium peptide binding step
S855A
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site-directed mutagenesis, the mutant shows 78% of wild-type ATPase activity, no protease activity, and 0.35fold of the activation by beta-casein compared to the wild-type enzyme
S855A
site-directed mutagenesis, a proteolytically inactive hLon mutant which retains near wild-type levels of ATPase activity
S855A
the Lon mutant, which lacks both ATPase and proteolytic activity, still maintains DNA binding activity but, in this case, does not undergo conformational changes
E423Q
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site-directed mutagenesis, mutation of the conserved catalytic glutamate 423 in Walker B motif treatment of Core-E423Q with Mg2+ induces the formation of the open-chambered hexamer. In the crystal, each asymmetric unit contains one hexameric assembly, with three non-neighboring protomers (B/D/F) bound to ADP and the other three (A/C/E) nucleotide free. The bound nucleotide is identified as ADP, which may have resulted from spontaneous hydrolysis of ATP. Each Core-E423Q protomer forms an alpha/beta domain capped with a distinct N-terminal three-helix bundle, a middle a domain, and a C-terminal PD, which are together organized into an elongated structure. Six LonA protomers are packed against one another like an orange's carpels and assembled into a cupcake-shaped complex
additional information
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enzyme null mutant, very slow growth of strain, being not filamentous and exhibiting normal resistance to UV irradiation. Mutant displays severe defects in morphology, 80% of cells appear Y-shaped. Mutant is highly attenuated for virulence
additional information
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deletion of the transmembrane domain results in uncontrollable activation of the enzyme proteolytic site and in vivo autolysis yielding a stable and functionally inactive fragment consisting of both alpha-helical and proteolytic domains
additional information
deletion of the transmembrane domain results in uncontrollable activation of the enzyme proteolytic site and in vivo autolysis yielding a stable and functionally inactive fragment consisting of both alpha-helical and proteolytic domains
additional information
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deletion of the transmembrane domain of LonB protease results in uncontrollable activation of the enzyme proteolytic site and in vivo autolysis yielding a stable and functionally inactive fragment consisting of both alpha-helical and proteolytic domains. The enzyme form with a transmembrane deletion and an additional site-directed mutagenesis at S509A (the catalytic Ser residue), is capable of recombination with the proteolytic-domain fragment. The mixed oligomers are proteolytically active, which indicates a crucial role of subunit interactions in the activation of the proteolytic site
additional information
deletion of the transmembrane domain of LonB protease results in uncontrollable activation of the enzyme proteolytic site and in vivo autolysis yielding a stable and functionally inactive fragment consisting of both alpha-helical and proteolytic domains. The enzyme form with a transmembrane deletion and an additional site-directed mutagenesis at S509A (the catalytic Ser residue), is capable of recombination with the proteolytic-domain fragment. The mixed oligomers are proteolytically active, which indicates a crucial role of subunit interactions in the activation of the proteolytic site
additional information
knockout mutant generation by lon gene deletion, generation of a lon/reb double knockout mutant
additional information
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knockout mutant generation by lon gene deletion, generation of a lon/reb double knockout mutant
additional information
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knockout mutant generation by lon gene deletion, generation of a lon/reb double knockout mutant
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additional information
Lon-2 is able to functionally complement an Escherichia coli Lon mutant
additional information
Lon-2 is able to functionally complement an Escherichia coli Lon mutant
additional information
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Lon-2 is able to functionally complement an Escherichia coli Lon mutant
additional information
design of truncated enzyme mutants. N-terminal domain is essential for oligomerization. Truncation of N-terminal domain also leads to inactivation of proteolytic, ATPase, and chaperone-like activities of enzyme but retains the DNA-binding activity
additional information
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design of truncated enzyme mutants. N-terminal domain is essential for oligomerization. Truncation of N-terminal domain also leads to inactivation of proteolytic, ATPase, and chaperone-like activities of enzyme but retains the DNA-binding activity
additional information
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construction of randomly chosen N-terminally truncated mutants. Mutants lacking amino acids from 1 to 247 of N-terminus retain significant peptidase and ATPase activities, but lose 90% of protease activity. Further truncation of the protein results in the loss of all three activities. Mutants lacking amino acids 246-259 or 248-256 also lose all activities and quaternary structure
additional information
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construction of randomly chosen N-terminally truncated mutants. Mutants lacking amino acids from 1 to 247 of N-terminus retain significant peptidase and ATPase activities, but lose 90% of protease activity. Further truncation of the protein results in the loss of all three activities. Mutants lacking amino acids 246-259 or 248-256 also lose all activities and quaternary structure
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additional information
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design of truncated enzyme mutants. N-terminal domain is essential for oligomerization. Truncation of N-terminal domain also leads to inactivation of proteolytic, ATPase, and chaperone-like activities of enzyme but retains the DNA-binding activity
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additional information
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mutant in the lon gene, growth is impaired at high temperature. Mutants show reduced motility, less autoagglutination, and lower levels of invasion of INT407 epithelial cells. Inactivation of lon has a minor effect on the proteome
additional information
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mutant in the lon gene, growth is impaired at high temperature. Mutants show reduced motility, less autoagglutination, and lower levels of invasion of INT407 epithelial cells. Inactivation of lon has a minor effect on the proteome
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additional information
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lon mutants, show defects in cell division, are unable to control initiation of DNA replication
additional information
generation of an insertional mutant strain with a defect in the lon gene in the background of the wild-type strain Ea1189. The Ea1189 lon mutant exhibits a mucoid colony on growth medium and produces about 10 times more amylovoran than that of the wild-type strain, which can be partially complemented. The Ea1189 lon mutant induces a typical hypersensitive response lesion on tobacco and is as pathogenic as wild-type on immature pears, although the disease progress is similar or slightly faster in the mutant at 4 days post-inoculation
additional information
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generation of an insertional mutant strain with a defect in the lon gene in the background of the wild-type strain Ea1189. The Ea1189 lon mutant exhibits a mucoid colony on growth medium and produces about 10 times more amylovoran than that of the wild-type strain, which can be partially complemented. The Ea1189 lon mutant induces a typical hypersensitive response lesion on tobacco and is as pathogenic as wild-type on immature pears, although the disease progress is similar or slightly faster in the mutant at 4 days post-inoculation
additional information
Erwinia amylovora Ea1189
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generation of an insertional mutant strain with a defect in the lon gene in the background of the wild-type strain Ea1189. The Ea1189 lon mutant exhibits a mucoid colony on growth medium and produces about 10 times more amylovoran than that of the wild-type strain, which can be partially complemented. The Ea1189 lon mutant induces a typical hypersensitive response lesion on tobacco and is as pathogenic as wild-type on immature pears, although the disease progress is similar or slightly faster in the mutant at 4 days post-inoculation
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additional information
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overproduction of enzyme is lethal. Overproduction specifically inhibits translation through specific activation of YoeB-dependent mRNA cleavage
additional information
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in an endogenous protein tagging assay, lon mutants accumulate excessive levels of tmRNA-tagged proteins. In a reporter protein tagging assay with lambda-CI-N, lon mutants efficiently tag the reporter protein, but the tagged protein exhibits increased stability. GFP construct containing a hard-coded C-terminal tmRNA tag exhibits increased stability in lon mutant cells
additional information
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lon clp ppk triple mutant, rate of protein turnover ist nearly identical to that of the lon clp double mutant. Deletion mutants of lon fused to the C-terminus of maltose-binding protein
additional information
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lon gene mutants, form long undivided filaments upon UV irradiation
additional information
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lon mutant altered in substrate specificity. A mutation in lon that converts Glu240 to Lys results in stabilization of lon substrate RcsA in vivo but does not affect the degradation of lon substrate SulA. lon lacking 107 N-terminal residues has drastically reduced protein degrading activity in vitro
additional information
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lon mutant, confers partial resistance against colicin. Sensitivity of lon mutant to colicin can be rescued by complementation. Decrease in the protein expression levels of BtuB and OmpF in the lon mutant, which are involved in colicin translocation. Elevation of expression of the oxyS gene, which can negatively control on the expression of BtuB protein
additional information
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lon mutants, accumulate abnormal proteins, form mucoid colonies and long filaments, fail to adapt rapidly to a nutrional downshift, are sensitive to UV at 30°C because of SulA accumulation, at higher temperatures they lose their sensitivity because ClpYQ takes over SulA degredation
additional information
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lon- mutants survive equally well under aerobic conditions as the wild-type, but die more rapidly than the wild-type under anaerobiosis. Effect is not mediated through a compensatory increase in the Clp protease
additional information
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in gene disruption mutant lon::Tn10 members of the RcsA regulon and many genes of the sigmaS-dependent general stress response are upregulated. The lon mutation does not affect sigmaS levels nor sigmaS activity in general. Lon-affected genes also include the major acid resistance genes
additional information
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the combined absence of Lon and SecB leads to a significant increase in protein aggregation at 37°C. The most abundant aggregated species are proteins destined for export. Data suggest that Lon and SecB share some substrates and that the SecB chaperone protects them from Lon degradation at both high and low temperatures
additional information
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construction of enzyme mutants, fusion of the Lon N domain to Escherichia coli ClpXDELTAN, a AAA+ enzyme that forms stable ring hexamers. Chimera307 contained the entire Lon N domain (residues 1-307) fused to ClpXDELTAN, whereas chimera211 contains the first 211 residues of Lon, which includes a globular region of the N domain but not an extended helical region. In addition, chimera211 contains disulfide bonds between the subunits of ClpXDELTAN, which have been shown to stabilize functional covalent hexamers. The ClpXDELTAN hexamerization is required for functional interaction with ClpP
additional information
analysis of the propensity of C-His-Lon and mutant enzymes Lon-R164A, Lon-R192A, and Lon-Y294A for autodegradation reveals that Lon-Y294A is most prone to autolysis. Slight autolysis of the intact enzyme and the mutant forms of Lon-R164A and Lon-R192A is observed only in the absence of nucleotides
additional information
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analysis of the propensity of C-His-Lon and mutant enzymes Lon-R164A, Lon-R192A, and Lon-Y294A for autodegradation reveals that Lon-Y294A is most prone to autolysis. Slight autolysis of the intact enzyme and the mutant forms of Lon-R164A and Lon-R192A is observed only in the absence of nucleotides
additional information
construction of a recombinant form des-CC(G5)-Lon in which the deleted CC fragment, a deleted 108-unit coiled-coil fragment (residues M173-M280) is replaced by a pentaglycine peptide, the the ClpB chaperone of Thermus thermophilus. Analysis of enzymatic properties of des-CC(G5)-Lon-H6 (DELTArLon) mutant, overview. In the absence of nucleotide effectors as well as in the presence of free nucleotides or the ADP-Mg complex, casein is not hydrolyzed by rLon even if the duration of the experiment is increased many times. The deletion form DELTArLon is incapable of hydrolyzing beta-casein in the time interval in which the proteolytic activity of full-length rLon protease is tested
additional information
construction of an N-terminally truncated ClpX lacking residues 1-62, ClpXDELTAN
additional information
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generation of mutant LonDELTANP lacking the ATP domain. Deletion of Lon's ATPase domain abrogates interactions with DNA. The DNA-binding defect of Lon protease affects TrfA proteolysis. And the Lon mutants are defective in proper cellular localization, most probably due to their impaired ability to form a nucleoprotein complex
additional information
removal of the HI(CC) domain, deletion of the HI(CC) domain leads to a complete loss of the proteolytic activity towards beta-casein by the deletion form. The deletion form Lon-dHI(CC) is unstable and it undergoes autolysis both in the absence and presence of nucleotide effectors, the autolysis of Lon-dHI(CC) is most pronounced in the presence of Mg2+ ions
additional information
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removal of the HI(CC) domain, deletion of the HI(CC) domain leads to a complete loss of the proteolytic activity towards beta-casein by the deletion form. The deletion form Lon-dHI(CC) is unstable and it undergoes autolysis both in the absence and presence of nucleotide effectors, the autolysis of Lon-dHI(CC) is most pronounced in the presence of Mg2+ ions
additional information
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lon mutant, confers partial resistance against colicin. Sensitivity of lon mutant to colicin can be rescued by complementation. Decrease in the protein expression levels of BtuB and OmpF in the lon mutant, which are involved in colicin translocation. Elevation of expression of the oxyS gene, which can negatively control on the expression of BtuB protein
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additional information
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lon- mutant, steroidogenic acute regulatory protein turnover is blocked
additional information
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lon-depleted cells show little if any mitochondrial DNA damage
additional information
construction of a hLon mutant lacking the first 156 amino acids, the mutant's enzymatic activities and its 3D structure are severely disturbed
additional information
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construction of a hLon mutant lacking the first 156 amino acids, the mutant's enzymatic activities and its 3D structure are severely disturbed
additional information
generation of deletion mutations MtaLonCdelta (removing residues 506-511) and MtaLonCDELTAHHE (replacing residues 118-205 with a triglycine linker) by a PCR-based strategy
additional information
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generation of deletion mutations MtaLonCdelta (removing residues 506-511) and MtaLonCDELTAHHE (replacing residues 118-205 with a triglycine linker) by a PCR-based strategy
additional information
generation of truncated enzyme versions, AAAP(residues 295-793) and AP(residues 492-793)
additional information
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several truncated constructs of Meiothermus taiwanensis LonA (MtaLonA) without the LAN domain are prepared for crystallization. The DELTAhairpin mutant loses allosteric stimulation of ATPase activity by substrate or inhibitor. DELTALoop-2 mutant, which can degrade casein but has a defective Ig2-translocating activity, shows a wild-type-like ATPase stimulation by casein, but the mutant exhibits a severely reduced ATPase allostery by Ig2
additional information
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attempts to construct a lonV mutant fail, lonD mutants are unable to sporulate
additional information
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mini-Tn5lacZ1 transposon insertion in the Lon protease gene confers a hyper-swarming phenotype on Proteus mirabilis. The lon mutation increases the accumulation of mRNA for representative class 1, flhDC, class 2, fliA, and class 3, flaA genes during swarmer cell differentiation. In addition, the stability of the FlhD protein is fourfold higher in the lon::mini-Tn5lacZ1 background. Expression of a single-copy lon::lacZ fusion increases during the swarming cycle and reaches peak levels of expression at a point just after swarmer cell differentiation has initiated. In liquid media, the lon::mini-Tn5lacZ1 insertion results in motile, highly elongated cells that overexpress flagellin. The lon::mini-Tn5lacZ1 mutation results in increased expression of the hpmBA and zapA virulence genes during swarmer cell differentiation
additional information
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lon mutants show impaired motility compared to the wild-type and a defect in biofilm formation
additional information
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mutants in PA1803, a close homolog of the ATP-dependent lon protease, exhibit more than 4fold-increased susceptibilities to ciprofloxacin and 2fold more susceptibilities to norfloxacin and nalidixic acid, but not to gentamicin or imipenem, as well as a characteristic elongated morphology. Complementation of the lon mutant restores wild-type antibiotic susceptibility and cell morphology
additional information
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construction of quorum-sensing signaling system mutant strains, gene lon disrupted cells of mutant strain, CS9008 overproduce pyocyanin, the biosynthesis of which depends on the RhlR/RhlI system, and show increased levels of a transcriptional regulator RhlR, phenotype, overview
additional information
construction of quorum-sensing signaling system mutant strains, gene lon disrupted cells of mutant strain, CS9008 overproduce pyocyanin, the biosynthesis of which depends on the RhlR/RhlI system, and show increased levels of a transcriptional regulator RhlR, phenotype, overview
additional information
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cells with Lon protease gene disruption overproduce pyocyanin and show increased levels of transcriptional regulator RhlR and increased expression of LasR/LasI. Regulation of RhlR/RhlI by Lon is independent of LasR/LasI
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cells with Lon protease gene disruption overproduce pyocyanin and show increased levels of transcriptional regulator RhlR and increased expression of LasR/LasI. Regulation of RhlR/RhlI by Lon is independent of LasR/LasI
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Pseudomonas protegens CHA1321(pycA-)/pME7402 is mutagenized by inserting transposon Tn5 in a mating with Escherichia coli W3110/pLG221. Complementation of the lon-negative mutant
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Pseudomonas protegens CHA1321(pycA-)/pME7402 is mutagenized by inserting transposon Tn5 in a mating with Escherichia coli W3110/pLG221. Complementation of the lon-negative mutant
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Pseudomonas protegens CHA1321(pycA-)/pME7402 is mutagenized by inserting transposon Tn5 in a mating with Escherichia coli W3110/pLG221. Complementation of the lon-negative mutant
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lon mutant, acyl homoserine lactone levels, PpuR levels and ppuI promoter activity all increase significantly
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lon mutant, acyl homoserine lactone levels, PpuR levels and ppuI promoter activity all increase significantly
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lon mutant, acyl homoserine lactone levels, PpuR levels and ppuI promoter activity all increase significantly
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lon mutants, constitutively express the hrp regulon, hypersecrete effector proteins
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lon- mutant, most genes induced in the mutant belong to the HrpL regulon or are related to transcription, protein synthesis, and energy metabolism. A major group of genes reduced in the mutant are related to cell wall biogenesis. Exhibits elevated hrpL expression in rich medium Kings B, but reduced hrpL expression in minimal medium. Reduced hrpL RNA is correlated with reduced hrpR and hrpS RNAs. Shows reduced bacterial pathogenicity
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the lon protease of Pyrococcus abyssi is interupted by an intein. The intein splices essentially to completion when over-expressed in Escherichia coli. Blocking the first step of splicing with a Cys1 to Ala mutation or step two of splicing with a Ser+1 to Ala mutation leads to the accumulation of precursor. Substitution of Ser+1 with Thr results in precursor, whereas substitution to Cys results in efficient splicing. The influence of the flanking extein residues on splicing efficiency is as follows. Mutation of Gly+2, Gly+3, Gly+5 or Gly+2/Gly+3 to Ala results mostly in splicing, but mutation of Gly+2 also results in the accumulation of branched-ester intermediate. The identity of the C-terminal residue of the N-extein seems less important, as mutation of Gln1 to Asn, Ala, Glu or Gly results in efficient splicing
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absence of lon, results in a lack of ATP-dependent proteolysis in the mitochondrial matrix, accumulation of electron dense aggregates and large mitochondrial DNA deletions. Mutant lacking both ATPase and protease activity also fails to suppress COX assembly defects
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Pim1 mutants, are respiratory-deficient and unable to grow on non-fermentable carbon sources
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lon mutants, accumulate abnormal proteins
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lon mutants, are unable to survive and proliferate murine macrophages, are extremely susceptible to hydrogen peroxide
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deletion mutant lacking the putative membrane-anchoring region, residues 134-170, and introduction of mutations S523A and K566A to avoid self-degrading activity. Mutant is active for peptide cleavage and both ATP-dependent and -independent protein degradation
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generation of a single-deletion Lon mutant by gene replacement, DELTAMLon showing decreased production of conidia but increased growth of mycelia
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generation of a single-deletion Lon mutant by gene replacement, DELTAPLon showing increased production of conidia but decreased growth of mycelia
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generation of a single-deletion Lon mutant by gene replacement, DELTAMLon showing decreased production of conidia but increased growth of mycelia
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generation of a single-deletion Lon mutant by gene replacement, DELTAPLon showing increased production of conidia but decreased growth of mycelia
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Walker A and B motifs, and the sensor 1 and sensor 2 are essential for the ATPase activity, while sensor 2 and the arginine finger are involved in activation of the protease domain
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lonS mutants, constitutively differentiated in the swarmer mode
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enzyme and protease ClpXP deletion mutant, no expression of a functional type II secretion system partly because of high cytosolic levels of small histone-like protein YmoA
