Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
Physiological effects of unassembled chaperonin Cct subunits in the yeast Saccharomyces cerevisiae.
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Studied physiological effects of overexpressing individual CCT subunits
"Overexpression of a single CCT gene in Saccharomyces cerevisiae causes an increase of the corresponding Cct subunit, but not of the Cct complex."
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Showed that CCT subunits form a stoichiometric array of eight different subunits in two rings
"Eukaryotic chaperonins, the Cct complexes, are assembled into two rings, each of which is composed of a stoichiometric array of eight different subunits"
Global landscape of protein complexes in the yeast Saccharomyces cerevisiae.
The plasma membrane proteome of Saccharomyces cerevisiae and its response to the antifungal calcofluor.
Quantitative actin folding reactions using yeast CCT purified via an internal tag in the CCT3/gamma subunit.
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Developed efficient purification protocol for yeast CCT
"An efficient purification protocol for CCT from Saccharomyces cerevisiae has been developed."
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Demonstrated quantitative actin folding by purified yeast CCT in vitro
"Yeast CCT catalyses the folding of yeast ACT1p and human beta-actin with nearly identical rate constants and yields."
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CCT catalyses folding via a binding pre-equilibrium followed by ATP-driven processing
"The results from this controlled CCT-actin folding assay are consistent with a model where CCT and Ac(I) are in a binding pre-equilibrium with a rate-limiting binding step, followed by a faster ATP-driven processing to native actin."
An atlas of chaperone-protein interactions in Saccharomyces cerevisiae: implications to protein folding pathways in the cell.
A global protein kinase and phosphatase interaction network in yeast.
The crystal structure of yeast CCT reveals intrinsic asymmetry of eukaryotic cytosolic chaperonins.
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Solved crystal structure of yeast CCT in complex with actin at 3.8 Å
"We have solved the crystal structure of yeast CCT in complex with actin at 3.8 Å resolution, revealing the subunit organisation and the location of discrete patches of co-evolving 'signature residues' that mediate specific interactions between CCT and its substrates."
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Revealed intrinsic asymmetry and subunit individuality in the complex
"The intrinsic asymmetry is revealed by the structural individuality of the CCT subunits, which display unique configurations, substrate binding properties, ATP-binding heterogeneity and subunit-subunit interactions."
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CCT uses a sequential rather than concerted ATP hydrolysis mechanism
"the mechanism by which CCT assists folding is distinct from other chaperonins, with no hydrophobic wall lining a potential Anfinsen cage, and a sequential rather than concerted ATP hydrolysis mechanism."
An inter-species protein-protein interaction network across vast evolutionary distance.
The social and structural architecture of the yeast protein interactome.
Compartmentation of protein folding in vivo: sequestration of non-native polypeptide by the chaperonin-GimC system.
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TRiC and GimC form an integrated folding compartment for newly synthesized actin
"We propose that TRiC and GimC form an integrated 'folding compartment' which functions in cooperation with the translation machinery."
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GimC accelerates actin folding on TRiC at least 5-fold
"GimC accelerates actin folding at least 5-fold and prevents the premature release of non-native protein from TRiC."
UniProtKB entry for Saccharomyces cerevisiae TCP1/CCT1
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TCP1 encodes CCT-alpha, a member of the TCP-1 chaperonin family.
"RecName: Full=T-complex protein 1 subunit alpha; Short=TCP-1-alpha; AltName: Full=CCT-alpha;"
Falcon deep research report for yeast TCP1/CCT1
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TCP1/CCT1 is a TRiC/CCT subunit in the cytosolic ATP-dependent chaperonin complex.
"TCP1/CCT1 encodes CCT1 (TCP-1; CCT-alpha), one of eight paralogous subunits that assemble into the eukaryotic cytosolic chaperonin TRiC/CCT."
PANTHER family PTHR11353 chaperonin metadata