The Chaperone Activity of the Developmental Small Heat Shock Protein Sip1 Is Regulated by pH-Dependent Conformational Changes.

Abstract:

:Small heat shock proteins (sHsps) are ubiquitous molecular chaperones that prevent the aggregation of unfolding proteins during proteotoxic stress. In Caenorhabditis elegans, Sip1 is the only sHsp exclusively expressed in oocytes and embryos. Here, we demonstrate that Sip1 is essential for heat shock survival of reproducing adults and embryos. X-ray crystallography and electron microscopy revealed that Sip1 exists in a range of well-defined globular assemblies consisting of two half-spheres, each made of dimeric "spokes." Strikingly, the oligomeric distribution of Sip1 as well as its chaperone activity depend on pH, with a trend toward smaller species and higher activity at acidic conditions such as present in nematode eggs. The analysis of the interactome shows that Sip1 has a specific substrate spectrum including proteins that are essential for embryo development.

journal_name

Mol Cell

journal_title

Molecular cell

authors

Fleckenstein T,Kastenmüller A,Stein ML,Peters C,Daake M,Krause M,Weinfurtner D,Haslbeck M,Weinkauf S,Groll M,Buchner J

doi

10.1016/j.molcel.2015.04.019

subject

Has Abstract

pub_date

2015-06-18 00:00:00

pages

1067-78

issue

6

eissn

1097-2765

issn

1097-4164

pii

S1097-2765(15)00301-9

journal_volume

58

pub_type

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