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Originally published In Press as doi:10.1074/jbc.M105453200 on September 5, 2001

J. Biol. Chem., Vol. 276, Issue 45, 42370-42381, November 9, 2001
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A Direct Interaction between the Carboxyl-terminal Region of CDC5L and the WD40 Domain of PLRG1 Is Essential for Pre-mRNA Splicing*

Paul Ajuh, Judith Sleeman, Janet Chusainow, and Angus I. LamondDagger

From the School of Life Sciences, the University of Dundee, Dow Street, Dundee DD1 5EH, Scotland, United Kingdom

The human proteins CDC5L (hCDC5) and PLRG1 are both highly conserved components of a multiprotein complex that is a subunit of the spliceosome. The respective homologues in yeast of both proteins are also associated with a sub-spliceosomal multiprotein complex that has been shown to be important for pre-mRNA splicing. We show that these two human proteins are associated in vivo and will interact directly in vitro. The regions containing the interacting domains in both proteins have been identified. Our results indicate that the carboxyl-terminal region of CDC5L and the WD40 domain of PLRG1 are essential for direct interaction between both proteins. By using a bacterially expressed mutant protein, containing the PLRG1 interacting domain in CDC5L, we show that the CDC5L-PLRG1 interaction in HeLa nuclear extract can be disrupted causing pre-mRNA splicing to be inhibited. Thus, a direct interaction between the CDC5L protein and PLRG1 in the CDC5L complex is essential for pre-mRNA splicing progression.

* 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.

Dagger Principal Research Fellow of the Wellcome Trust. To whom correspondence should be addressed. Tel.: 44 1382 345473; Fax: 44 1382 345695; E-mail: a.i.lamond@dundee.ac.uk.

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