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J Biol Chem, Vol. 274, Issue 53, 38163-38170, December 31, 1999

The N-terminal K Homology Domain of the Poly(rC)-binding Protein Is a Major Determinant for Binding to the Poliovirus 5'-Untranslated Region and Acts as an Inhibitor of Viral Translation^*

Deborah Silvera, Andrea V. Gamarnik, and Raul Andino

From the Department of Microbiology and Immunology, University of California, San Francisco, California 94143-0414

The poly(rC)-binding proteins (PCBP1 and PCBP2) are RNA-binding proteins whose RNA recognition motifs are composed of three K homology (KH) domains. These proteins are involved in both the stabilization and translational regulation of several cellular and viral RNAs. PCBP1 and PCBP2 specifically interact with both the 5'-element known as the cloverleaf structure and the large stem-loop IV RNA of the poliovirus 5'-untranslated region. We have found that the first KH domain of PCBP2 (KH1) specifically interacts with the viral RNAs, and together with viral protein 3CD, KH1 forms a high affinity ternary ribonucleoprotein complex with the cloverleaf RNA, resembling the full-length PCBP protein. Furthermore, KH1 acts as a dominant-negative mutant to inhibit translation from a poliovirus reporter gene in both Xenopus laevis oocytes and HeLa cell in vitro translation extracts.

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^* This work was supported by United States Public Health Service Grant AI40085 (to R. A.).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.: 415-502-6358; Fax: 415-476-0939; E-mail: andino@cgl.ucsf.edu.

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Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.

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