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Article

Evidence for an essential function of the N terminus of a small heat shock protein in vivo, independent of in vitro chaperone activity.

Proceedings of the National Academy of Sciences of the United States of America - 27 Dec 2005

Giese Kim C, Basha Eman, Catague Belmund Y, Vierling Elizabeth

Abstract excerpt

To investigate the mechanism of small heat shock protein (sHsp) function, unbiased by current models of sHsp chaperone activity, we performed a screen for mutations of Synechocystis Hsp16.6 that reduced the ability of the protein to provide thermotolerance in vivo. Missense mutations at 17 positions throughout the protein and a C-terminal truncation of 5 aa were identified, representing the largest collection of...

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Identifiers

PMID: 16365319
DOI: 10.1073/pnas.0506169103
PMCID: PMC1323161

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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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Evidence for an essential function of the N terminus of a small heat shock protein in vivo, independent of in vitro chaperone activity.PMID 16365319Read ↗

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