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Article

Control of Hsp90 chaperone and its clients by N-terminal acetylation and the N-end rule pathway.

Proceedings of the National Academy of Sciences of the United States of America - 30 May 2017

Oh Jang-Hyun, Hyun Ju-Yeon, Varshavsky Alexander

Abstract excerpt

We found that the heat shock protein 90 (Hsp90) chaperone system of the yeast Saccharomyces cerevisiae is greatly impaired in naa10Δ cells, which lack the NatA Nα-terminal acetylase (Nt-acetylase) and therefore cannot N-terminally acetylate a majority of normally N-terminally acetylated proteins, including Hsp90 and most of its cochaperones. Chk1, a mitotic checkpoint kinase and a client of Hsp90, was degraded...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 28515311
DOI: 10.1073/pnas.1705898114
PMCID: PMC5465900

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

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