BRENDA - Enzyme Database
show all sequences of 3.6.4.B10

The chaperonin TRiC forms an oligomeric complex in the malaria parasite cytosol

Spillman, N.J.; Beck, J.R.; Ganesan, S.M.; Niles, J.C.; Goldberg, D.E.; Cell. Microbiol. 19, e12719 (2017)

Data extracted from this reference:

Cloned(Commentary)
Cloned (Commentary)
Organism
recombinant ectopic overexpression in in Plasmodium falciparum of each of the N-terminally GFP-tagged PfTRiC subunits, under the expression of the strong, constitutively active HSP86 promoter, the subunits are additionally C-terminally tagged with a ten amino acid flexible linker sequence (PRPGAAHYAA) between the TRiC C-terminus and GFP to avoid disruption of heterohexadecamer formation. All GFP-tagged subunits are successfully overexpressed, except the PfTRiC-zeta subunit, where the GFP signal gets lost
Plasmodium falciparum
Engineering
Protein Variants
Commentary
Organism
additional information
generation of a regulatable PfTRiC-theta line expressing Myc-tagged subunit theta that forms a large complex in the parasite cytosol, and a theta subunit knockout line. The PfTRiC-theta-MYC clones retain between 4 and 10 aptamer elements. Knockout of PfTRiC-alpha and -zeta subunits using double homologous recombination
Plasmodium falciparum
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
cytoskeleton
upon heat stress, human TRiC-alpha translocates from the cytosolic fraction and associates with the cytoskeleton
Homo sapiens
5856
-
cytosol
chaperonin TRiC forms an heterohexadecameric complex in the malaria parasite cytosol
Plasmodium falciparum
5829
-
cytosol
chaperonin TRiC forms an heterohexadecameric complex in the red blood cell (RBC) cytosol. The stress of parasite infection may lead to translocation of human TRiC subunits from the soluble to insoluble fraction. But the human TRiC-beta and -delta subunits remain in the soluble cytosolic fraction in iRBC. Human TRiC subunits alpha and delta are present in the cytosol of RBC, and this localization is unchanged upon parasite infection
Homo sapiens
5829
-
additional information
the plasmodial subunit theta can form high molecular weight complexes in the parasite soluble fraction
Plasmodium falciparum
-
-
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Mg2+
required
Homo sapiens
Mg2+
required
Plasmodium falciparum
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
550000
-
about, recombinant heterohexadecameric myc-tagged subunit theta complex, native PAGE
Plasmodium falciparum
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
ATP + H2O
Homo sapiens
-
ADP + phosphate
-
-
?
ATP + H2O
Plasmodium falciparum
-
ADP + phosphate
-
-
?
Organism
Organism
UniProt
Commentary
Textmining
Homo sapiens
P17987 AND P78371 AND P49368 AND P50991 AND P48643 AND P40227 AND Q99832 AND P50990
genes CCT1-8 encoding subunits CCT-alpha, CCT-beta, CCT-gamma, CCT-delta, CCT-epsilon, CCT-zeta-1, CCT-eta, and CCT-theta
-
Plasmodium falciparum
Q8II43 AND O97247 AND Q8I5C4 AND C0H5I7 AND O97282 AND C6KST5 AND O77323 AND O96220
genes encoding subunits alpha, beta, gamma, delta, epsilon, zeta, eta, and theta
-
Source Tissue
Source Tissue
Commentary
Organism
Textmining
erythrocyte
-
Homo sapiens
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
ATP + H2O
-
756411
Homo sapiens
ADP + phosphate
-
-
-
?
ATP + H2O
-
756411
Plasmodium falciparum
ADP + phosphate
-
-
-
?
Subunits
Subunits
Commentary
Organism
heterohexadecamer
chaperonin TRiC forms an oligomeric complex in the malaria parasite cytosol. TRiC is a class II chaperonin, which typically forms a high molecular weight heterohexadecamer, comprised of two eight-membered rings
Homo sapiens
heterohexadecamer
chaperonin TRiC forms an oligomeric complex in the malaria parasite cytosol. TRiC is a class II chaperonin, which typically forms a high molecular weight heterohexadecamer, comprised of two eight-membered rings. PfTRiC forms a large complex in the parasite cytosol
Plasmodium falciparum
More
the theta subunit has a molecular weight of 60.9 kDa. The plasmodial subunit theta can form high molecular weight complexes in the parasite soluble fraction. Loss of one subunit (PfTRiC-theta) in the heterohexadecamer is disrupts formation of the entire complex
Plasmodium falciparum
Synonyms
Synonyms
Commentary
Organism
CCT
-
Homo sapiens
CCT
-
Plasmodium falciparum
chaperonin TRiC
-
Homo sapiens
chaperonin TRiC
-
Plasmodium falciparum
HsTRiC
-
Homo sapiens
PfTRiC
-
Plasmodium falciparum
Plasmodium TRiC
-
Plasmodium falciparum
T-complex protein 1
-
Homo sapiens
T-complex protein 1
-
Plasmodium falciparum
T-complex protein 1 ring complex
-
Homo sapiens
T-complex protein 1 ring complex
-
Plasmodium falciparum
TCP-1
-
Homo sapiens
TCP-1
-
Plasmodium falciparum
TriC
-
Homo sapiens
TriC
-
Plasmodium falciparum
Cloned(Commentary) (protein specific)
Commentary
Organism
recombinant ectopic overexpression in in Plasmodium falciparum of each of the N-terminally GFP-tagged PfTRiC subunits, under the expression of the strong, constitutively active HSP86 promoter, the subunits are additionally C-terminally tagged with a ten amino acid flexible linker sequence (PRPGAAHYAA) between the TRiC C-terminus and GFP to avoid disruption of heterohexadecamer formation. All GFP-tagged subunits are successfully overexpressed, except the PfTRiC-zeta subunit, where the GFP signal gets lost
Plasmodium falciparum
Engineering (protein specific)
Protein Variants
Commentary
Organism
additional information
generation of a regulatable PfTRiC-theta line expressing Myc-tagged subunit theta that forms a large complex in the parasite cytosol, and a theta subunit knockout line. The PfTRiC-theta-MYC clones retain between 4 and 10 aptamer elements. Knockout of PfTRiC-alpha and -zeta subunits using double homologous recombination
Plasmodium falciparum
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
cytoskeleton
upon heat stress, human TRiC-alpha translocates from the cytosolic fraction and associates with the cytoskeleton
Homo sapiens
5856
-
cytosol
chaperonin TRiC forms an heterohexadecameric complex in the malaria parasite cytosol
Plasmodium falciparum
5829
-
cytosol
chaperonin TRiC forms an heterohexadecameric complex in the red blood cell (RBC) cytosol. The stress of parasite infection may lead to translocation of human TRiC subunits from the soluble to insoluble fraction. But the human TRiC-beta and -delta subunits remain in the soluble cytosolic fraction in iRBC. Human TRiC subunits alpha and delta are present in the cytosol of RBC, and this localization is unchanged upon parasite infection
Homo sapiens
5829
-
additional information
the plasmodial subunit theta can form high molecular weight complexes in the parasite soluble fraction
Plasmodium falciparum
-
-
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Mg2+
required
Homo sapiens
Mg2+
required
Plasmodium falciparum
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
550000
-
about, recombinant heterohexadecameric myc-tagged subunit theta complex, native PAGE
Plasmodium falciparum
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
ATP + H2O
Homo sapiens
-
ADP + phosphate
-
-
?
ATP + H2O
Plasmodium falciparum
-
ADP + phosphate
-
-
?
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
erythrocyte
-
Homo sapiens
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
ATP + H2O
-
756411
Homo sapiens
ADP + phosphate
-
-
-
?
ATP + H2O
-
756411
Plasmodium falciparum
ADP + phosphate
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
heterohexadecamer
chaperonin TRiC forms an oligomeric complex in the malaria parasite cytosol. TRiC is a class II chaperonin, which typically forms a high molecular weight heterohexadecamer, comprised of two eight-membered rings
Homo sapiens
heterohexadecamer
chaperonin TRiC forms an oligomeric complex in the malaria parasite cytosol. TRiC is a class II chaperonin, which typically forms a high molecular weight heterohexadecamer, comprised of two eight-membered rings. PfTRiC forms a large complex in the parasite cytosol
Plasmodium falciparum
More
the theta subunit has a molecular weight of 60.9 kDa. The plasmodial subunit theta can form high molecular weight complexes in the parasite soluble fraction. Loss of one subunit (PfTRiC-theta) in the heterohexadecamer is disrupts formation of the entire complex
Plasmodium falciparum
General Information
General Information
Commentary
Organism
malfunction
knockdown of the PfTRiC-theta subunit is lethal, the lethality is not due to a change in protein export into the host red blood cell (RBC) compartment
Homo sapiens
malfunction
knockdown of the PfTRiC-theta subunit is lethal, the lethality is not due to a change in protein export into the host red blood cell (RBC) compartment. Loss of the PfTRiC complex does not alter export of PfSBP1 or PfREX1. The PfTRiC-theta-MYC clones of teh engineered regulatable line retain between 4 and 10 aptamer elements. The degree of regulation of expression correlates with the number of aptamers in the array, and knockdown reveals that PfTRiC-theta is essential for asexual parasite growth. But loss of one subunit in the heterohexadecamer disrupts formation of the entire complex
Plasmodium falciparum
additional information
human TRiC subunits interact with each other, but do not interact with export related parasite proteins from Plasmodium falciparum in extracts from trophozoite-stage infected red blood cells
Homo sapiens
physiological function
the malaria parasite exports numerous proteins into its host red blood cell (RBC). Proteins are first routed through the secretory system, into the parasitophorous vacuole (PV), a membranous compartment enclosing the parasite. Proteins are then translocated across the PV membrane in a process requiring ATP and unfolding. Once in the RBC compartment the exported proteins are then refolded and further trafficked to their final localizations. Chaperones are important in the unfolding and refolding processes. The parasite TRiC chaperonin complex is exported, and is involved in trafficking of exported effectors. Essential role for PfTRiC within the parasite compartment
Homo sapiens
physiological function
the malaria parasite exports numerous proteins into its host red blood cell (RBC). Proteins are first routed through the secretory system, into the parasitophorous vacuole (PV), a membranous compartment enclosing the parasite. Proteins are then translocated across the PV membrane in a process requiring ATP and unfolding. Once in the RBC compartment the exported proteins are then refolded and further trafficked to their final localizations. Chaperones are important in the unfolding and refolding processes. The parasite TRiC chaperonin complex is exported, and is involved in trafficking of exported effectors. Essential role for PfTRiC within the parasite compartment. Subunit PfTRiC-theta is essential for asexual parasite growth
Plasmodium falciparum
General Information (protein specific)
General Information
Commentary
Organism
malfunction
knockdown of the PfTRiC-theta subunit is lethal, the lethality is not due to a change in protein export into the host red blood cell (RBC) compartment
Homo sapiens
malfunction
knockdown of the PfTRiC-theta subunit is lethal, the lethality is not due to a change in protein export into the host red blood cell (RBC) compartment. Loss of the PfTRiC complex does not alter export of PfSBP1 or PfREX1. The PfTRiC-theta-MYC clones of teh engineered regulatable line retain between 4 and 10 aptamer elements. The degree of regulation of expression correlates with the number of aptamers in the array, and knockdown reveals that PfTRiC-theta is essential for asexual parasite growth. But loss of one subunit in the heterohexadecamer disrupts formation of the entire complex
Plasmodium falciparum
additional information
human TRiC subunits interact with each other, but do not interact with export related parasite proteins from Plasmodium falciparum in extracts from trophozoite-stage infected red blood cells
Homo sapiens
physiological function
the malaria parasite exports numerous proteins into its host red blood cell (RBC). Proteins are first routed through the secretory system, into the parasitophorous vacuole (PV), a membranous compartment enclosing the parasite. Proteins are then translocated across the PV membrane in a process requiring ATP and unfolding. Once in the RBC compartment the exported proteins are then refolded and further trafficked to their final localizations. Chaperones are important in the unfolding and refolding processes. The parasite TRiC chaperonin complex is exported, and is involved in trafficking of exported effectors. Essential role for PfTRiC within the parasite compartment
Homo sapiens
physiological function
the malaria parasite exports numerous proteins into its host red blood cell (RBC). Proteins are first routed through the secretory system, into the parasitophorous vacuole (PV), a membranous compartment enclosing the parasite. Proteins are then translocated across the PV membrane in a process requiring ATP and unfolding. Once in the RBC compartment the exported proteins are then refolded and further trafficked to their final localizations. Chaperones are important in the unfolding and refolding processes. The parasite TRiC chaperonin complex is exported, and is involved in trafficking of exported effectors. Essential role for PfTRiC within the parasite compartment. Subunit PfTRiC-theta is essential for asexual parasite growth
Plasmodium falciparum
Other publictions for EC 3.6.4.B10
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Synonyms
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
756368
Gestaut
The chaperonin TRiC/CCT assoc ...
Homo sapiens
Cell
177
751-765.e15
2019
-
-
1
-
-
-
-
-
-
1
-
1
-
1
-
-
-
-
-
-
-
-
2
1
2
-
-
-
-
-
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
2
1
-
-
-
-
-
-
-
-
-
2
2
-
-
-
756410
Yusof
Structural and functional ins ...
Glaciozyma antarctica
Cell Stress Chaperones
24
351-368
2019
-
-
1
-
1
-
-
-
-
1
-
1
-
7
-
-
1
-
-
1
-
-
2
1
5
1
1
-
-
1
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
1
-
1
-
-
-
1
-
1
-
-
2
1
1
1
-
-
1
-
-
-
-
3
3
-
-
-
757875
Kim
TRiC/CCT chaperonins are esse ...
Drosophila melanogaster
Oncogene
38
4739-4754
2019
-
-
-
-
1
-
-
-
-
-
-
1
-
6
-
1
-
-
-
1
-
-
1
1
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
1
-
-
1
-
-
1
1
-
-
-
-
-
-
-
-
-
3
3
-
-
-
758115
Ohhara
Chaperonin TRiC/CCT supports ...
Drosophila melanogaster, Drosophila melanogaster Oregon R
PLoS Genet.
15
e1008121
2019
-
-
1
-
1
-
-
-
-
-
-
-
-
4
-
-
-
-
-
2
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
3
3
-
-
-
749858
Willison
The structure and evolution o ...
Mus musculus, Saccharomyces cerevisiae, Drosophila melanogaster, Homo sapiens, Rattus norvegicus, Arabidopsis thaliana, Caenorhabditis elegans, Bos taurus, Dictyostelium discoideum, Candida albicans, Plasmodium falciparum, Danio rerio, Rattus norvegicus Sprague-Dawley, Candida albicans ATCC MYA-2876, Saccharomyces cerevisiae ATCC 204508
Biochem. J.
475
3009-3034
2018
-
2
1
1
2
-
-
12
13
12
-
15
-
16
-
-
-
-
-
7
-
-
15
4
60
-
-
-
-
-
-
-
10
-
-
-
-
2
1
10
1
2
-
-
-
-
12
13
12
-
15
-
-
-
-
-
7
-
-
15
4
-
-
-
-
-
-
-
-
-
45
45
-
-
-
756366
Balchin
Pathway of actin folding dire ...
Homo sapiens
Cell
174
1507-1521.e16
2018
1
-
-
-
-
-
-
-
-
1
-
1
-
2
-
-
-
-
-
-
-
-
2
1
3
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
2
1
-
-
-
-
-
-
-
-
-
3
3
-
-
-
756400
Berger
In vivo function of the chape ...
Danio rerio
Cell Rep.
22
313-322
2018
-
-
-
-
1
-
-
-
-
-
-
-
-
4
-
-
-
-
-
3
-
-
-
-
2
-
-
-
-
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-
-
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-
-
1
-
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-
-
-
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-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
2
2
-
-
-
757782
Knowlton
The TRiC chaperonin controls ...
Homo sapiens
Nat. Microbiol.
3
481-493
2018
-
1
-
-
-
-
-
-
-
1
-
1
-
5
-
-
-
-
-
4
-
-
2
-
3
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
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-
-
1
-
1
-
-
-
-
-
4
-
-
2
-
-
-
-
-
-
-
-
-
-
3
3
-
-
-
756411
Spillman
The chaperonin TRiC forms an ...
Homo sapiens, Plasmodium falciparum
Cell. Microbiol.
19
e12719
2017
-
-
1
-
1
-
-
-
5
2
1
2
-
6
-
-
-
-
-
1
-
-
2
3
15
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
5
2
1
2
-
-
-
-
-
1
-
-
2
3
-
-
-
-
-
-
-
-
-
5
5
-
-
-
756722
Melkani
TRiC/CCT chaperonins are esse ...
Drosophila melanogaster
FEBS Lett.
591
3447-3458
2017
-
-
-
-
1
-
-
-
1
-
-
-
-
1
-
-
-
-
-
1
-
-
-
1
4
-
-
-
-
-
-
-
-
-
-
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-
-
-
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
1
-
-
-
-
-
-
-
-
1
2
2
1
-
-
758147
Yamamoto
Asymmetry in the function and ...
Chaetomium thermophilum
PLoS ONE
12
e0176054
2017
-
-
1
1
1
-
-
-
1
1
2
1
-
3
-
-
1
-
-
1
-
-
2
2
7
1
-
-
-
1
-
-
-
-
-
-
-
-
1
-
1
1
-
-
-
-
-
1
1
2
1
-
-
-
1
-
1
-
-
2
2
1
-
-
-
1
-
-
-
1
3
3
1
-
-
751330
Korobko
Transient kinetic analysis of ...
Saccharomyces cerevisiae, Saccharomyces cerevisiae ATCC 204508
J. Mol. Biol.
428
4520-4527
2016
-
-
-
-
1
-
-
1
-
1
-
2
-
3
-
-
1
-
-
-
-
-
4
-
5
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
1
-
1
-
2
-
-
-
1
-
-
-
-
4
-
1
-
-
-
1
-
-
-
-
2
2
-
-
-
755946
Araki
Functional profiling of asymm ...
Homo sapiens
Biochem. Biophys. Res. Commun.
481
232-238
2016
-
-
-
-
-
-
-
-
-
-
-
-
-
3
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