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J. Biol. Chem., Vol. 277, Issue 21, 18483-18488, May 24, 2002
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From the Department of Molecular and Cellular Biology, Faculty of
Biotechnology, University of Gdansk, 24 Kladki,
80 822 Gdansk, Poland
The Escherichia coli molecular
chaperone protein ClpB is a member of the highly conserved Hsp100/Clp
protein family. Previous studies have shown that the ClpB protein is
needed for bacterial thermotolerance. Purified ClpB protein has been
shown to reactivate chemically and heat-denatured proteins. In this
work we demonstrate that the combined action of ClpB and the DnaK,
DnaJ, and GrpE chaperones leads to the activation of DNA replication of
the broad-host-range plasmid RK2. In contrast, ClpB is not needed for
the activation of the oriC-dependent
replication of E. coli. Using purified protein components
we show that the ClpB/DnaK/DnaJ/GrpE synergistic action activates the
plasmid RK2 replication initiation protein TrfA by converting inactive
dimers to an active monomer form. In contrast, Hsp78/Ssc1/Mdj1/Mge1,
the corresponding protein system from yeast mitochondria, cannot
activate the TrfA replication protein. Our results demonstrate for the
first time that the ClpB/DnaK/DnaJ/GrpE system is involved in protein
monomerization and in the activation of a DNA replication factor.
Cooperative Action of Escherichia coli ClpB Protein
and DnaK Chaperone in the Activation of a Replication Initiation
Protein*
and
*
This work was supported by the Polish State Committee for
Scientific Research Grants 3P04A01422 and 6P04B02317 and
Ministry of National Education National Institutes of Health
Grant 98-349 from the United States-Polish Maria Sklodowska-Curie Fund
II.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.
Recipient of EMBO Young Investigator Program. To whom
correspondence should be addressed. Tel./Fax: 48-58-301-9222; E-mail: igor@biotech.univ.gda.pl.
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