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Originally published In Press as doi:10.1074/jbc.M201083200 on February 26, 2002

J. Biol. Chem., Vol. 277, Issue 19, 16614-16623, May 10, 2002
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Heterogeneous Nuclear Ribonucleoprotein (hnRNP) K Is a Component of an Intronic Splicing Enhancer Complex That Activates the Splicing of the Alternative Exon 6A from Chicken beta -Tropomyosin Pre-mRNA*

Alain Expert-BezançonDagger , Jean Pierre Le Caer§, and Joëlle MarieDagger

From the Dagger  Centre de Génétique Moléculaire, CNRS, F-91190 Gif-sur-Yvette, France and § Ecole Supérieure de physique et de chimie industrielles (ESPCI), 10 rue Vauquelin, 75005 Paris, France

Splicing of the chicken beta -tropomyosin exon 6A is stimulated, both in vivo and in vitro, by an intronic pyrimidine-rich element (S4) located 37 nucleotides downstream of exon 6A. Several pyrimidine-rich sequences are able to substitute for the natural S4 enhancer with various stimulatory effects. We show that the different enhancer sequences recruit U1 small nuclear ribonucleoprotein (SnRNP) to the exon 6A 5' splice site, with an efficiency that correlates with the splicing activation. By using RNA affinity and two-dimensional gel electrophoresis, we characterized several proteins that bind to the different enhancer sequences. Heterogeneous nuclear ribonucleoprotein (hnRNP) K and hnRNP I (polypyrimidine track-binding protein, PTB) exhibit a higher level of interaction with the strong enhancer sequences (S4) than with the weakest enhancers. Functional analysis shows that hnRNP K is a component of the enhancer complex that promotes exon 6A splicing through the wild-type S4 sequence. The addition of recombinant hnRNP K to nuclear extracts preincubated with poly(rC) RNA competitor completely restores splicing efficiency to the original level. hnRNP I (PTB) was also found associated with the strong enhancer sequences. Its function in the splicing of exon 6A is discussed.

* This work was supported by the Center National de la Recherche Sientifique, the Institut National de la Santé et de la Recherche Médicale, l'Association de la Recherche Contre le Cancer Grant 9831, et l'Association Française contre les Myopathies.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.: 0169823800; Fax: 0169823877; E-mail: marie@cgm.cnrs-gif.fr.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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