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Originally published In Press as doi:10.1074/jbc.M107581200 on October 3, 2001

J. Biol. Chem., Vol. 276, Issue 48, 44841-44847, November 30, 2001
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The Major Messenger Ribonucleoprotein Particle Protein p50 (YB-1) Promotes Nucleic Acid Strand Annealing*

Maxim A. SkabkinDagger , Valentina EvdokimovaDagger §, Adri A. M. Thomas, and Lev P. OvchinnikovDagger ||

From the Dagger  Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region 142290, Russia and the  Department of Developmental Biology, Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands

p50, a member of the Y-box binding transcription factor family, is tightly associated with eukaryotic mRNAs and is responsible for general translational regulation. Here we show that p50, in addition to its previously described ability to melt mRNA secondary structure, is capable of promoting rapid annealing of complementary nucleic acid strands. p50 accelerates annealing of RNA and DNA duplexes up to 1500-fold within a wide range of salt concentrations and temperatures. Phosphorylation of p50 selectively inhibits DNA annealing. Moreover, p50 catalyzes strand exchange between double-stranded and single-stranded RNAs yielding a product bearing a more extended double-stranded structure. Strikingly, p50 displays both RNA-melting and -annealing activities in a dose-dependent manner; a relatively low amount of p50 promotes formation of RNA duplexes, whereas an excess of p50 causes unwinding of double-stranded forms. Our results suggest that the alteration of nucleic acid conformation is a basic mechanism of the p50-dependent regulation of gene expression.

* This work was supported by the Russian Academy of Sciences and Grants N 97-open-501 (to A. A. M. T. and L. P. O.) from INTAS (International Association for the promotion of co-operation with scientists from the New Independent States of the former Soviet Union) and N 00-15-9790 (to L. P. O.) from the Russian Foundation for Basic 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.

§ Recipient of a Human Frontier Science Program Organization long-term fellowship. Present address: Dept. of Biochemistry and McGill Cancer Center, McGill University, 3655 Promenade Sir William Osler, Montreal, Quebec  H3G 1Y6, Canada.

|| To whom correspondence should be addressed. Tel./Fax: 7-095-924-04-93; E-mail: ovchinn@vega.protres.ru.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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