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J. Biol. Chem., Vol. 276, Issue 11, 7906-7912, March 16, 2001
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From the DjlA is a 30-kDa type III membrane protein
of Escherichia coli with the majority, including an extreme
C-terminal putative J-domain, oriented toward the cytoplasm. No other
regions of sequence similarity aside from the J-domain exist between
DjlA and the known DnaK (Hsp70) co-chaperones DnaJ (Hsp40) and CbpA. In
this study, we explored whether and to what extent DjlA possesses DnaK co-chaperone activity and under what conditions a DjlA-DnaK interaction could be important to the cell. We found that the DjlA J-domain can
substitute fully for the J-domain of DnaJ using various in vivo functional complementation assays. In addition, the purified cytoplasmic fragment of DjlA was shown to be capable of stimulating DnaK ATPase in a manner indistinguishable from DnaJ, and, furthermore, DjlA could act as a DnaK co-chaperone in the reactivation of chemically denatured luciferase in vitro. DjlA expression in the cell
is tightly controlled, and even its mild overexpression leads to induction of mucoid capsule. Previous analysis showed that
DjlA-mediated induction of the wca capsule operon required
the RcsC/RcsB two-component signaling system and that wca
induction by DjlA was lost when cells contained mutations in either the
dnaK or grpE gene. We now show using
allele-specific genetic suppression analysis that DjlA must interact
with DnaK for DjlA-mediated stimulation of capsule synthesis.
Collectively, these results demonstrate that DjlA is a co-chaperone for
DnaK and that this chaperone
DjlA Is a Third DnaK Co-chaperone of Escherichia
coli, and DjlA-mediated Induction of Colanic Acid Capsule
Requires DjlA-DnaK Interaction*
,,, and¶
Département de Biochimie
Médicale, Centre Médical Universitaire, Université de
Genève, 1, rue Michel-Servet, 1211 Genève 4, Switzerland
and the § Department of Molecular Biology, International
Institute of Molecular and Cell Biology, United Nations Educational,
Scientific and Cultural Organisation-Polish Academy of
Sciences, 4, Trojdena Street, 02-109 Warsaw, Poland
co-chaperone pair is implicated directly,
or indirectly, in the regulation of colanic acid capsule.
*
This work was supported by the Canton of Geneva, Grants
FN-31-47283-96 and 7PLPJ048480 from the Swiss National Science
Foundation (to C. G.), and Grant from the Polish State Committee for
Scientific Research (to M. Z.).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.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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