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J. Biol. Chem., Vol. 282, Issue 18, 13617-13626, May 4, 2007

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Members of the Heterogeneous Nuclear Ribonucleoprotein H Family Activate Splicing of an HIV-1 Splicing Substrate by Promoting Formation of ATP-dependent Spliceosomal Complexes^*

From the Department of Biomedical Science, Florida Atlantic University, Boca Raton, Florida 33431

In this study we analyzed members of the heterogeneous nuclear ribonucleoprotein (hnRNP) H protein family to determine their RNA binding specificities and roles in splicing regulation. Our data indicate that hnRNPs H, H', F, 2H9, and GRSF-1 bind the consensus motif DGGGD (where D is U, G, or A) and aggregate in a multimeric complex. We analyzed the role of these proteins in the splicing of a substrate derived from the HIV-1 tat gene and have shown that hnRNP H family members are required for efficient splicing of this substrate. The hnRNP H protein family members activated splicing of the viral substrate by promoting the formation of ATP-dependent spliceosomal complexes. Mutational analysis of six consensus motifs present within the intron of the substrate indicated that only one of these motifs acts as an intronic splicing enhancer.

Received for publication, January 26, 2007 , and in revised form, March 1, 2007.

^* This work was supported by NIAID, National Institutes of Health Grant R01AI052820 (to M. C.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ To whom correspondence should be addressed: Dept. of Biomedical Science, Florida Atlantic University, 777 Glades Rd., Boca Raton, FL 33431. Tel.: 561-297-0627; Fax: 561-297-2221; E-mail: mcaputi{at}fau.edu.

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