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J. Biol. Chem., Vol. 278, Issue 11, 9107-9115, March 14, 2003
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From the Protein B23 is a multifunctional nucleolar
protein whose molecular chaperone activity is proposed to play role in
ribosome assembly. Previous studies (Szebeni, A., and Olson, M. O. J. (1999) Protein Sci. 8, 905-912) showed that
protein B23 has several characteristics typical of molecular
chaperones, including anti-aggregation activity, promoting the
renaturation of denatured proteins, and preferential binding to
denatured substrates. However, until now there has been no proposed
mechanism for release of a bound substrate. Protein B23 can be
phosphorylated by protein kinase CK2 (CK2) in a segment required for
chaperone activity. The presence of bound substrate enhanced the rate
of CK2 phosphorylation of protein B23 by 2-3-fold, and this
enhancement was dependent on a nonpolar region in its N-terminal end.
Formation of a complex between B23 and chaperone test substrates
(rhodanese or citrate synthase) was inhibited by CK2 phosphorylation.
Furthermore, CK2 phosphorylation of a previously formed B23-substrate
complex promoted its dissociation. The dissociation of complexes
between B23 and the human immunodeficiency virus-Rev protein required
both CK2 phosphorylation and competition with a Rev nuclear
localization signal peptide, suggesting that Rev binds B23 at two
separate sites. These studies suggest that unlike many molecular
chaperones, which directly hydrolyze ATP, substrate release by protein
B23 is dependent on its phosphorylation by CK2.
Role of Protein Kinase CK2 Phosphorylation in the Molecular
Chaperone Activity of Nucleolar Protein B23*
,, and¶
Department of Biochemistry, University of
Mississippi Medical Center, Jackson, Mississippi 39216 and
§ New England Biolabs, Beverly, Massachusetts 01915
*
This work was supported by grants from the National
Institutes of Health, by the Medical Guardian Society of the University of Mississippi, and by funds from the National Science Foundation Experimental Program to Stimulate Competitive Research (EPSCoR) Protein
Structure and Localization Group Project.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.
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