3.6.4.B10: chaperonin ATPase (protein-folding, protecting from aggregation, protein stabilizing)
This is an abbreviated version!
For detailed information about chaperonin ATPase (protein-folding, protecting from aggregation, protein stabilizing), go to the full flat file.
Word Map on EC 3.6.4.B10
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3.6.4.B10
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chaperonins
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tubulins
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actin
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hetero-oligomeric
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cytoskeletal
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groel
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prefoldin
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chaperonin-containing
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huntingtin
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proteostasis
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double-ring
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tailless
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polyglutamine
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polyq
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inter-ring
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phosducin-like
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synthesis
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back-to-back
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drug development
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protein-folding
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homo-oligomeric
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acidophilum
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beta-tubulin
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thermoplasma
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medicine
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cryo-electron
- 3.6.4.B10
- chaperonins
- tubulins
- actin
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hetero-oligomeric
- cytoskeletal
- groel
- prefoldin
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chaperonin-containing
- huntingtin
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proteostasis
-
double-ring
-
tailless
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polyglutamine
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polyq
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inter-ring
-
phosducin-like
- synthesis
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back-to-back
- drug development
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protein-folding
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homo-oligomeric
- acidophilum
- beta-tubulin
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thermoplasma
- medicine
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cryo-electron
Reaction
Synonyms
alpha/beta-thermosome, ApCpnB, archaeal chaperonin, CCT, CCT ATPase, CCT chaperonin, CCT complex, CCT/TRiC, CCT/TRiC chaperonin, CCT/TRiC complex, CCT2, chaperonin B, chaperonin containing t-complex polypeptide-1, chaperonin containing TCP-1, chaperonin containing TCP1, chaperonin TCP-1 ring complex, chaperonin TRiC, chaperonin TRiC/CCT, chaperonin-containing t-complex polypeptide 1, cPKA, CpkB, CtCCT, cytosolic chaperonin TRiC, eukaryotic chaperone complex, eukaryotic chaperonin, eukaryotic chaperonin TRiC, eukaryotic group II chaperonin, GaTRiC, group II chaperonin, group II chaperonin CCT/TRiC, group II CPN, HsTRiC, Mm-cpn, MmCpn, More, PfCPN, PfTRiC, PhCPN, Plasmodium TRiC, protein P45, T-complex polypeptide-1 ring complex, T-complex protein 1, T-complex protein 1 ring complex, T-complex protein-1 ring complex, TCP-1, TCP-1 ring complex, TCP1, TCP1 ring complex, thermosome, TKS1-CPN, TriC, TRiC chaperonin, TRiC chaperonin complex, TRiC/CCT, type II chaperonin
ECTree
3.6.4.B10 chaperonin ATPase (protein-folding, protecting from aggregation, protein stabilizing)Advanced search results
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results (Engineering
Engineering on EC 3.6.4.B10 - chaperonin ATPase (protein-folding, protecting from aggregation, protein stabilizing)
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
H147R
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
naturally occuring mutation of subunit CCT5
D386A
site-directed mutagenesis, introduction of D386A into Mm-cpn significantly reduces its ability to complement for loss of GroES and GroEL, loss of ATPase activity severely affects the complementing ability of the wild-type and mutant Mm-cpn proteins
G160S
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the TRiC-like mutant G160S of MmCpn has a drastically slower rate of ATP hydrolysis, roughly equivalent to the steady-state hydrolysis of eukaryotic TRiC
K216A
site-directed mutagenesis, the mutant enzyme moderately complements the GroEL-deletion mutant Escherichia coli strain TAB21
K216C
site-directed mutagenesis, the mutant enzyme complements the GroEL-deletion mutant Escherichia coli strain TAB21 well
K216D
site-directed mutagenesis, the mutant enzyme complements the GroEL-deletion mutant Escherichia coli strain TAB21 well
K216E
random mutagenesis, growth for the mutants is clearly faster than for wild-type Mm-cpn organisms under GroES/GroEL-limiting conditions, improved phenotype in Escherichia coli under GroEL- and GroES-depleting conditions. The mutant can effectively hydrolyze ATP
K216E/D386A
site-directed mutagenesis, introduction of D386A into Mm-cpn significantly reduces its ability to complement for loss of GroES and GroEL, loss of ATPase activity severely affects the complementing ability of the wild-type and mutant Mm-cpn proteins
K216F
site-directed mutagenesis, the mutant enzyme moderately complements the GroEL-deletion mutant Escherichia coli strain TAB21
K216G
site-directed mutagenesis, the mutant enzyme complements the GroEL-deletion mutant Escherichia coli strain TAB21 well
K216L
site-directed mutagenesis, the mutant enzyme moderately complements the GroEL-deletion mutant Escherichia coli strain TAB21
K216P
site-directed mutagenesis, the mutant enzyme moderately complements the GroEL-deletion mutant Escherichia coli strain TAB21
K216Q
site-directed mutagenesis, the mutant enzyme complements the GroEL-deletion mutant Escherichia coli strain TAB21 well
K216R
site-directed mutagenesis, the mutant enzyme slightly complements the GroEL-deletion mutant Escherichia coli strain TAB21
K216S
site-directed mutagenesis, the mutant enzyme complements the GroEL-deletion mutant Escherichia coli strain TAB21 well
K216T
site-directed mutagenesis, the mutant enzyme moderately complements the GroEL-deletion mutant Escherichia coli strain TAB21
K216V
site-directed mutagenesis, the mutant enzyme complements the GroEL-deletion mutant Escherichia coli strain TAB21 well
K216Y
site-directed mutagenesis, the mutant enzyme moderately complements the GroEL-deletion mutant Escherichia coli strain TAB21
M223E
site-directed mutagenesis, the mutant enzyme complements the GroEL-deletion mutant Escherichia coli strain TAB21 well
M223F
site-directed mutagenesis, the mutant enzyme complements the GroEL-deletion mutant Escherichia coli strain TAB21 well
M223G
site-directed mutagenesis, the mutant enzyme complements the GroEL-deletion mutant Escherichia coli strain TAB21 well
M223I
M223I/D386A
site-directed mutagenesis, introduction of D386A into Mm-cpn significantly reduces its ability to complement for loss of GroES and GroEL, loss of ATPase activity severely affects the complementing ability of the wild-type and mutant Mm-cpn proteins
M223L
site-directed mutagenesis, the mutant enzyme complements the GroEL-deletion mutant Escherichia coli strain TAB21 well
M223R
site-directed mutagenesis, the mutant enzyme complements the GroEL-deletion mutant Escherichia coli strain TAB21 well
M223S
site-directed mutagenesis, the mutant enzyme complements the GroEL-deletion mutant Escherichia coli strain TAB21 well
M223V
site-directed mutagenesis, the mutant enzyme complements the GroEL-deletion mutant Escherichia coli strain TAB21 well
M223W
site-directed mutagenesis, the mutant enzyme complements the GroEL-deletion mutant Escherichia coli strain TAB21 well
M223Y
site-directed mutagenesis, the mutant enzyme complements the GroEL-deletion mutant Escherichia coli strain TAB21 well
C450Y
G345D
D545G
site-directed mutagenesis, the mutant shows a stabilities similar to the wild-type CpkA
D545M
site-directed mutagenesis, the mutant shows slightly higher stabilities than that of wild-type CpkA
E530G
site-directed mutagenesis, the mutant strain DA4 shows increased ATPase activity. The CpkA-E530G mutation prevents cold denaturation of proteins under cold-stress conditions, thereby enabling cells to grow in cooler environments
E530M
site-directed mutagenesis, the mutant shows a stabilities similar to the wild-type CpkA
P538G
site-directed mutagenesis, the mutant shows slightly higher stabilities than that of wild-type CpkA
P538M
site-directed mutagenesis, the mutant shows a stabilities similar to the wild-type CpkA
Q533M
site-directed mutagenesis, the mutant shows a stabilities similar to the wild-type CpkA
D64A/D393A
site-directed mutagenesis, an ATPase-deficient mutant, the mutant also does not exhibit ATPase-dependent conformational change
D64A/D393A/K485W
site-directed mutagenesis, an ATPase-deficient mutant, the mutant also does not exhibit ATPase-dependent conformational change, the mutant lacks ATP-dependent refolding activity, nucleotide binding and ATP-dependent conformational change kinetics, overview
K165A/K485W
site-directed mutagenesis, ATPase inactive mutant that can partially prevent the spontaneous refolding ofGFP and refold it in an ATP-dependent manner
K485W
L265W
site-directed mutagenesis, replacement of amino acid L265 with Trp partially impairs the protein folding activity, eight Trp residues are thought to come close in the closed conformation. The resulting steric hindrance might interrupt the conformational changes required for protein folding. Although ATP hydrolysis activity is almost completely lost in the absence of K+, slight ATP-dependent folding activity is observed
L56W
site-directed mutagenesis, the mutant exhibits nearly the same level of protein folding activity as the wild-type protein
D64A/D393A
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site-directed mutagenesis, an ATPase-deficient mutant, the mutant also does not exhibit ATPase-dependent conformational change
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D64A/D393A/K485W
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site-directed mutagenesis, an ATPase-deficient mutant, the mutant also does not exhibit ATPase-dependent conformational change, the mutant lacks ATP-dependent refolding activity, nucleotide binding and ATP-dependent conformational change kinetics, overview
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K165A/K485W
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site-directed mutagenesis, ATPase inactive mutant that can partially prevent the spontaneous refolding ofGFP and refold it in an ATP-dependent manner
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K485W
L265W
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site-directed mutagenesis, replacement of amino acid L265 with Trp partially impairs the protein folding activity, eight Trp residues are thought to come close in the closed conformation. The resulting steric hindrance might interrupt the conformational changes required for protein folding. Although ATP hydrolysis activity is almost completely lost in the absence of K+, slight ATP-dependent folding activity is observed
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L56W
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site-directed mutagenesis, the mutant exhibits nearly the same level of protein folding activity as the wild-type protein
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K165A/K485W
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site-directed mutagenesis, ATPase inactive mutant that can partially prevent the spontaneous refolding ofGFP and refold it in an ATP-dependent manner
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K485W
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site-directed mutagenesis, the mutant shows ATP binding and conformational change upon ATP binding
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additional information
M223I
random mutagenesis, growth for the mutants is clearly faster than for wild-type Mm-cpn organisms under GroES/GroEL-limiting conditions, improved phenotype in Escherichia coli under GroEL- and GroES-depleting conditions. The mutant can effectively hydrolyze ATP
M223I
site-directed mutagenesis, the mutant enzyme complements the GroEL-deletion mutant Escherichia coli strain TAB21 well
C450Y
P28480; Q5XIM9; Q6P502; Q7TPB1; Q68FQ0; Q3MHS9; D4AC23; D4ACB8
naturally occuring mutation in subunit CCT4
G345D
P12612; P39076; P39077; P39078; P40413; P39079; P42943; P47079
site-directed mutagenesis in subunit CCT4 decreases cooperativity in ATP binding compared to wild-type
G345D
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site-directed mutagenesis in subunit CCT4 decreases cooperativity in ATP binding compared to wild-type
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K485W
site-directed mutagenesis, the mutant lacks ATP-dependent refolding activity, nucleotide binding and ATP-dependent conformational change kinetics, overview
K485W
site-directed mutagenesis, the mutant shows ATP binding and conformational change upon ATP binding
K485W
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site-directed mutagenesis, the mutant lacks ATP-dependent refolding activity, nucleotide binding and ATP-dependent conformational change kinetics, overview
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K485W
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site-directed mutagenesis, the mutant shows ATP binding and conformational change upon ATP binding
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additional information
Q9PW76; Q6PBW6; Q7T2P2; Q6P123; Q6NVI6; E9QGU4; B3DKJ0; A0A0R4IJT8
a missense mutation in cct5 causes muscle impairment within cct5tf212b, mapping of tf212b links the phenotype-causing mutation to the gene encoding the TRiC subunit Cct5 on chromosome 24, severe reduction in the amount of myofibrils. Knockdown of cct5 by two independent morpholinos, both validated for their functionality, results in a reduction of birefringence comparable with cct5tf212b homozygotes. A second mutant allele of cct5, cct5hi2972Tg, carries a single retroviral insertion in cct5 and fails to complement the bire-fringence reduction of cct5tf212b. In addition, both cct5 mutants are significantly ameliorated by injection of full-length cct5 mRNA, confirming that the phenotype-causing mutation of cct5tf212b resides within cct5. In addition to the trunk muscle, the head musculature of cct5tf212b mutants is also affected. Mutations in other TRiC subunits, e.g. CCT3 or CCT4, also cause impaired myofibril assembly. Mutants cct3sa1761 and cct4x0114 null develop into relatively normal larvae that exhibit skeletal muscle defects grossly similar to the other cct mutants
additional information
P12613; Q9W392; P48605; Q9VK69; Q7KKI0; Q9VXQ5; Q9VHL2; Q7K3J0
cardiac-specific knockdown of chaperonin CCT in Drosophila melanogaster resulting in disorganization of cardiac actin- and myosin-containing myofibrils and severe physiological dysfunction, including restricted heart diameters, elevated cardiac dysrhythmia and compromised cardiac performance. Knockdown of Cct3, Cct4, Cct5, Cct6 or Cct7 with the TinCDELTA4 driver resulted in cardiac morphological defects in one or more non-beating regions of the heart and completely non-beating hearts. These defects are not observed with TinC/+. Moreover, defects are even more severe with knockdown of Cct3, Cct4, Cct5, Cct6 or Cct7 with the Hand-Gal4 driver, whereas Hand/+ hearts do not show these defects.In addition to cardiac defects, cardiac-specific knockdown of Cct3, Cct4, Cct5, Cct6 or Cct7 has a drastic impact on the lifespan of the flies (female and male combined) compared to TinCDELTA4/+ and Hand/+ flies. Extremely severe cardiac dysfunction observed with Hand/+ upon cardiac-specific knockdown of Cct3, Cct4, Cct5, Cct6 or Cct7, correlate with further shortening of lifespan compared to TinCDELTA4/+. Quantitative analysis of additional cardiac physiological parameters, mutant phenotypes, overview
additional information
P12613; Q9W392; P48605; Q9VK69; Q7KKI0; Q9VXQ5; Q9VHL2; Q7K3J0
gene CCT4 is knocked down by RNAi (v106099) in eye discs by using ey-Gal4 that drives GAL4 expression in eye and head primordia, all progeny die during the late pupal stage. Similar results are obtained by an additional CCT4 RNAi line (5525R-3). Dead flies in pupal cases have relatively intact thorax and abdomen but completely lack the eye-head structures. The eye-head field in larval eye discs targeted by ey-Gal4 is lost, resulting in the headless phenotype and late pupal lethality. Loss of any CCT subunit leads to similar loss-of-function phenotypes by disrupting the function of the CCT complex in vivo. Mutant phenotype, overview
additional information
P12613; Q9W392; P48605; Q9VK69; Q7KKI0; Q9VXQ5; Q9VHL2; Q7K3J0
knockdown of each cct subunit gene in the prothoracic gland (PG). Cell number and C value in the mutant PG are increased compared to wild-type. Usage of an PG-selective RNAi screen to identify MES regulator(s). A statistically significant difference occurs in pH3 expression between control and cct RNAi. cct genes are also required for proper progression of mitotic cell cycle, development is mainly arrested at the L3 stage in cct RNAi animals (phm>cct-RNAi). Ecdysteroidogenic gene expression is significantly reduced in cct RNAi, and 20E administration restores larval-to-pupal transition in 20-30% of animals
additional information
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knockdown of each cct subunit gene in the prothoracic gland (PG). Cell number and C value in the mutant PG are increased compared to wild-type. Usage of an PG-selective RNAi screen to identify MES regulator(s). A statistically significant difference occurs in pH3 expression between control and cct RNAi. cct genes are also required for proper progression of mitotic cell cycle, development is mainly arrested at the L3 stage in cct RNAi animals (phm>cct-RNAi). Ecdysteroidogenic gene expression is significantly reduced in cct RNAi, and 20E administration restores larval-to-pupal transition in 20-30% of animals
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additional information
A0A1S6LQX4; A0A1S6LQU3; A0A1S6LQU0; A0A1S6LQU6; A0A1S6LQU1; A0A1S6LQU9; A0A1S6LQW6; A0A1S6LQW7
three categories of residue substitutions are found in alpha, beta, and gamma subunits: (i) bulky/polar side chains to alanine or valine, (ii) charged residues to alanine, and (iii) isoleucine to valine that is expected to increase intramolecular flexibility within the GaTRiC
additional information
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three categories of residue substitutions are found in alpha, beta, and gamma subunits: (i) bulky/polar side chains to alanine or valine, (ii) charged residues to alanine, and (iii) isoleucine to valine that is expected to increase intramolecular flexibility within the GaTRiC
additional information
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
RNAi based gene knockout via shRNA expressing lentivirus constructs. Analysis of overexpressed genes playing a role in mediating the growth and survival of SUM-52 breast cancer cells via large-scale RNAi-based growth and viability screen, overview. RNAi-mediated knockdown targeting CCT2 inhibits growth and colony formation of SUM-52 breast cancer cells. Knocking downTCP1 has a cell-type-specific effect on cell growth and colony forming capacity in SUM-52 cells
additional information
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RNAi based gene knockout via shRNA expressing lentivirus constructs. Analysis of overexpressed genes playing a role in mediating the growth and survival of SUM-52 breast cancer cells via large-scale RNAi-based growth and viability screen, overview. RNAi-mediated knockdown targeting CCT2 inhibits growth and colony formation of SUM-52 breast cancer cells. Knocking downTCP1 has a cell-type-specific effect on cell growth and colony forming capacity in SUM-52 cells
additional information
summary of the functional growth analysis of Escherichia coli TAB21 cells expressing diverse Mm-cpn-M223 and Mm-cpn-K216 mutants at 30°C, overview. The Mm-cpn-K216E and Mm-cpn-M223I mutants act as genuine chaperonins and must complete an ATP-dependent chaperonin cycle to function in Escherichia coli
additional information
Q8II43; O97247; Q8I5C4; C0H5I7; O97282; C6KST5; O77323; O96220
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
additional information
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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
additional information
Thermochaetoides thermophila
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generation of CtCCT variants containing ATPase-deficient subunits. Removal of all surface exposed cysteine residues for diffracted X-ray tracking experiment, and addition of cysteine residues at the tip of helical protrusions of selected two subunits. Gold nanocrystals are attached onto CtCCTs via gold-thiol bonds and applied for the analysis by diffracted X-ray tracking. Irrespective of the locations of cysteines, ATP binding induces tilting motion followed by rotational motion in the CtCCT molecule, like the archaeal group II chaperonins. When gold nanocrystals are attached onto two subunits in the high ATPase activity hemisphere, the CtCCT complex exhibits a fairly rapid response to the motion. In contrast, the response of CtCCT, which has gold nanocrystals attached to the low-activity hemisphere, is slow. Change from an open to a closed state using caged-ATP, which is a derivative of ATP that is inactive and does not bind to the ATP binding site of the chaperonin
additional information
construction of gene cpkA disruption mutant strains. Gene disruptant strain DA1 (DELTAcpkA) shows decreased cell growth at 60°C as compared to 85°C for the wild-type strain KOD1. The DB2 mutant (DELTAcpkA::cpkB DELTAcpkB), whose cpkB gene is expressed under the control of the cpkA promoter, does not grow at 60°C, and the DB3 mutant (DELTAcpkA(1-524)::cpkB(1-524) DELTAcpkB), whose CpkA amino acid residues 1 to 524 are replaced with corresponding CpkB residues that maintains the C-terminal region intact, grows at 60°C, implying that the CpkA C-terminal region plays a key role in cell growth at 60°C. Proteins coimmunoprecipitated with anti-Cpk from DB1 cells cultivated at 60°C, overview
additional information
construction of gene cpkA disruption mutant strains. Gene disruptant strain DA1 (DELTAcpkA) shows decreased cell growth at 60°C as compared to 85°C for the wild-type strain KOD1. The DB2 mutant (DELTAcpkA::cpkB DELTAcpkB), whose cpkB gene is expressed under the control of the cpkA promoter, does not grow at 60°C, and the DB3 mutant (DELTAcpkA(1-524)::cpkB(1-524) DELTAcpkB), whose CpkA amino acid residues 1 to 524 are replaced with corresponding CpkB residues that maintains the C-terminal region intact, grows at 60°C, implying that the CpkA C-terminal region plays a key role in cell growth at 60°C. Proteins coimmunoprecipitated with anti-Cpk from DB1 cells cultivated at 60°C, overview
additional information
construction of gene cpkB disruption mutant strains. Gene disruptant strain DB1 (DELTAcpkB) shows decreased cell growth at 93°C as compared to 85°C for the wild-type strain KOD1. The DB2 mutant (DELTAcpkA::cpkB DELTAcpkB), whose cpkB gene is expressed under the control of the cpkA promoter, does not grow at 60°C, and the DB3 mutant (DELTAcpkA(1-524)::cpkB(1-524) DELTAcpkB), whose CpkA amino acid residues 1 to 524 are replaced with corresponding CpkB residues that maintains the C-terminal region intact, grows at 60°C, implying that the CpkA C-terminal region plays a key role in cell growth at 60°C. Proteins coimmunoprecipitated with anti-Cpk from DB1 cells cultivated at 60°C, overview
additional information
construction of gene cpkB disruption mutant strains. Gene disruptant strain DB1 (DELTAcpkB) shows decreased cell growth at 93°C as compared to 85°C for the wild-type strain KOD1. The DB2 mutant (DELTAcpkA::cpkB DELTAcpkB), whose cpkB gene is expressed under the control of the cpkA promoter, does not grow at 60°C, and the DB3 mutant (DELTAcpkA(1-524)::cpkB(1-524) DELTAcpkB), whose CpkA amino acid residues 1 to 524 are replaced with corresponding CpkB residues that maintains the C-terminal region intact, grows at 60°C, implying that the CpkA C-terminal region plays a key role in cell growth at 60°C. Proteins coimmunoprecipitated with anti-Cpk from DB1 cells cultivated at 60°C, overview
additional information
construction of the asymmetric ring complex of a group II chaperonin using circular permutated covalent mutants, TKS1-CPNASR. Although one ring of the asymmetric ring complex lacks ATPase or ATP binding activity, the other wild-type ring undergoes an ATP-dependent conformational change and maintains protein-folding activity. It is possible to construct covalent chaperonin complexes by connecting N and C-termini. Circular permutated covalent enzyme TKS1-CPN (CPNCPC) is constructed by applying circular permutation to the covalent TKS1-CPN dimer, the circular permutated covalent TKS1-CPN dimer that has the deletion of 95 amino acids from its N-terminus and the addition of the same 95 amino acids to its C-terminus can assemble into a doublering structure similar to the wild-type. The 95th amino acid residue is located at the loop region between Helix 4 and Helix 5. The complex of the TKS1-CPN variant has ann molecular weight of approximately 120 kDa determined by SDS-PAGE. The ATPase activity of mutant CPNASR is half that of the recombinant His-tagged CPNwild-type homooligomer. Phenotypes, overview
additional information
construction of the asymmetric ring complex of a group II chaperonin using circular permutated covalent mutants, TKS1-CPNASR. Although one ring of the asymmetric ring complex lacks ATPase or ATP binding activity, the other wild-type ring undergoes an ATP-dependent conformational change and maintains protein-folding activity. It is possible to construct covalent chaperonin complexes by connecting N and C-termini. Circular permutated covalent enzyme TKS1-CPN (CPNCPC) is constructed by applying circular permutation to the covalent TKS1-CPN dimer, the circular permutated covalent TKS1-CPN dimer that has the deletion of 95 amino acids from its N-terminus and the addition of the same 95 amino acids to its C-terminus can assemble into a doublering structure similar to the wild-type. The 95th amino acid residue is located at the loop region between Helix 4 and Helix 5. The complex of the TKS1-CPN variant has ann molecular weight of approximately 120 kDa determined by SDS-PAGE. The ATPase activity of mutant CPNASR is half that of the recombinant His-tagged CPNwild-type homooligomer. Phenotypes, overview
additional information
construction of three CPNbeta mutants, with the truncation of 1, 2 and 6 amino acids from the C-terminus, named CPNbetaTc1, CPNbetaTc2 and CPNbetaTc6, respectively. CPNbetaTc2 and CPNbetaTc6 are designed to delete two hydrophobic amino acid residues from the CPNbeta C-terminus (Gly-Ser-Glu-Asp-/Phe-Gly-Ser-Asp-/Leu-Asp, with / indicating Tc6 and Tc2 truncation positions). The mutants form hexadecameric homooligomers, similar to the wild-type CPNbeta (CPNbetaWT). The thermal aggregation of CS is completely suppressed by the presence of an equimolar amount of the CPNbeta mutant variants. The truncation mutants exhibit the same protection abilities as CPNbetaWT. The mutant isoforms CPNbeta and PFDalpha1beta1 from strain KS1 interact with each other at high affinity, interaction analysis using immobilized PFDalpha1beta1, overview
additional information
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construction of the asymmetric ring complex of a group II chaperonin using circular permutated covalent mutants, TKS1-CPNASR. Although one ring of the asymmetric ring complex lacks ATPase or ATP binding activity, the other wild-type ring undergoes an ATP-dependent conformational change and maintains protein-folding activity. It is possible to construct covalent chaperonin complexes by connecting N and C-termini. Circular permutated covalent enzyme TKS1-CPN (CPNCPC) is constructed by applying circular permutation to the covalent TKS1-CPN dimer, the circular permutated covalent TKS1-CPN dimer that has the deletion of 95 amino acids from its N-terminus and the addition of the same 95 amino acids to its C-terminus can assemble into a doublering structure similar to the wild-type. The 95th amino acid residue is located at the loop region between Helix 4 and Helix 5. The complex of the TKS1-CPN variant has ann molecular weight of approximately 120 kDa determined by SDS-PAGE. The ATPase activity of mutant CPNASR is half that of the recombinant His-tagged CPNwild-type homooligomer. Phenotypes, overview
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additional information
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construction of the asymmetric ring complex of a group II chaperonin using circular permutated covalent mutants, TKS1-CPNASR. Although one ring of the asymmetric ring complex lacks ATPase or ATP binding activity, the other wild-type ring undergoes an ATP-dependent conformational change and maintains protein-folding activity. It is possible to construct covalent chaperonin complexes by connecting N and C-termini. Circular permutated covalent enzyme TKS1-CPN (CPNCPC) is constructed by applying circular permutation to the covalent TKS1-CPN dimer, the circular permutated covalent TKS1-CPN dimer that has the deletion of 95 amino acids from its N-terminus and the addition of the same 95 amino acids to its C-terminus can assemble into a doublering structure similar to the wild-type. The 95th amino acid residue is located at the loop region between Helix 4 and Helix 5. The complex of the TKS1-CPN variant has ann molecular weight of approximately 120 kDa determined by SDS-PAGE. The ATPase activity of mutant CPNASR is half that of the recombinant His-tagged CPNwild-type homooligomer. Phenotypes, overview
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