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Article

The lid domain of Caenorhabditis elegans Hsc70 influences ATP turnover, cofactor binding and protein folding activity.

PloS one - 1 Jan 2012

Sun Li, Edelmann Franziska T, Kaiser Christoph J O, Papsdorf Katharina, Gaiser Andreas M, Richter Klaus

Abstract excerpt

Hsc70 is a conserved ATP-dependent molecular chaperone, which utilizes the energy of ATP hydrolysis to alter the folding state of its client proteins. In contrast to the Hsc70 systems of bacteria, yeast and humans, the Hsc70 system of C. elegans (CeHsc70) has not been studied to date.We find that CeHsc70 is characterized by a high ATP turnover rate and limited by post-hydrolysis nucleotide exchange. This...

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Identifiers

PMID: 22479492
DOI: 10.1371/journal.pone.0033980
PMCID: PMC3315512

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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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