Caenorhabditis elegans small heat-shock proteins Hsp12.2 and Hsp12.3 form tetramers and have no chaperone-like activity.

Abstract:

:Four 12.2-12.6 kDa small heat-shock proteins (sHSPs) of Caenorhabditis elegans are the smallest known members of the sHSP family. They essentially comprise the characteristic C-terminal 'alpha-crystallin domain' of the sHSPs, having a very short N-terminal region, and lacking a C-terminal tail. Recombinant Hsp12.2 and 12.3 are characterized here. Far-UV CD spectra reveal, as for other sHSPs, predominantly a beta-sheet structure. By gel permeation and crosslinking, they are the first sHSPs shown to occur as tetramers, rather than forming the usual large multimeric complexes. Exceptionally, too, both appear devoid of in vitro chaperone-like abilities. This supports the notion that tetramers are the building blocks of sHSP complexes, and that higher multimer formation, mediated through the N-terminal domains, is a prerequisite for chaperone-like activity.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Kokke BP,Leroux MR,Candido EP,Boelens WC,de Jong WW

doi

10.1016/s0014-5793(98)00917-x

subject

Has Abstract

pub_date

1998-08-21 00:00:00

pages

228-32

issue

3

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(98)00917-X

journal_volume

433

pub_type

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