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J. Biol. Chem., Vol. 275, Issue 47, 37212-37218, November 24, 2000
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From the Institute of Microbiology, Eidgenössische Technische
Hochschule, Schmelzbergstrasse 7, CH-8092 Zürich,
Switzerland
Rhizobia are the only bacteria known to induce a
multitude of small heat shock proteins (sHsps) upon temperature
upshift. The sHsps of Bradyrhizobium japonicum fall into
two different classes, class A and class B. Here, we studied the
chaperone activity and oligomeric features of two representative
members of each class. The purified sHsps were efficient chaperones, as
demonstrated by their ability to prevent thermally induced aggregation
of citrate synthase in vitro. Homo-oligomer formation of
all four sHsps was demonstrated by gel filtration and by two
independent co-purification approaches. Mixed oligomers were readily
observed between members of the same class, even when these proteins
originated from different species such as Escherichia coli
and B. japonicum. The chaperone activity of purified
hetero-oligomers was indistinguishable from the activity of
homo-oligomers. Heteromeric complexes were never obtained between class
A and class B sHsps, indicating that hetero-oligomer formation is
restricted to sHsps of the same class.
Chaperone Activity and Homo- and Hetero-oligomer Formation of
Bacterial Small Heat Shock Proteins*
*
This study was supported by a grant from the Swiss National
Foundation for Scientific Research.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed. Tel.: 41-1-632-2586;
Fax: 41-1-632-1148; E-mail: fnarber@micro.biol.ethz.ch.
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