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Article

A two-step mechanism for the folding of actin by the yeast cytosolic chaperonin.

The Journal of biological chemistry - 7 Jan 2011

Stuart Sarah F, Leatherbarrow Robin J, Willison Keith R

Abstract excerpt

Actin requires the chaperonin containing TCP1 (CCT), a hexadecameric ATPase essential for cell viability in eukaryotes, to fold to its native state. Following binding of unfolded actin to CCT, the cavity of the chaperone closes and actin is folded and released in an ATP-dependent folding cycle. In yeast, CCT forms a ternary complex with the phosducin-like protein PLP2p to fold actin, and together they can return...

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Identifiers

PMID: 21056978
DOI: 10.1074/jbc.M110.166256
PMCID: PMC3012972

Genes

TCP1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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A two-step mechanism for the folding of actin by the yeast cytosolic chaperonin.PMID 21056978Read ↗

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