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J. Biol. Chem., Vol. 280, Issue 7, 5205-5210, February 18, 2005

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Identification of the Polypyrimidine Tract Binding Protein-associated Splicing Factor·p54(nrb) Complex as a Candidate DNA Double-strand Break Rejoining Factor^*

Catherine L. Bladen, Durga Udayakumar, Yoshihiko Takeda, and William S. Dynan

From the Program in Gene Regulation and Cancer Biology, Institute of Molecular Medicine and Genetics, Medical College of Georgia, Augusta, Georgia 30912

The biological effects of ionizing radiation are attributable, in large part, to induction of DNA double-strand breaks. We report here the identification of a new protein factor that reconstitutes efficient double-strand break rejoining when it is added to a reaction containing the five other polypeptides known to participate in the human nonhomologous end-joining pathway. The factor is a stable heteromeric complex of polypyrimidine tract-binding protein-associated splicing factor (PSF) and a 54-kDa nuclear RNA-binding protein (p54(nrb)). These polypeptides, to which a variety of functions have previously been attributed, share extensive homology, including tandem RNA recognition motif domains. The PSF·p54(nrb) complex cooperates with Ku protein to form a functional preligation complex with substrate DNA. Based on structural comparison with related proteins, we propose a model where the four RNA recognition motif domains in the heteromeric PSF·p54(nrb) complex cooperate to align separate DNA molecules.

Received for publication, November 11, 2004 , and in revised form, December 3, 2004.

^* This work was supported by United States Public Health Service Grants GM 35866 and CA 98239 and United States National Science Foundation Grant MCB-9906440 (to W. S. D.). 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.

These authors contributed equally to this work.

An Eminent Scholar of the Georgia Research Alliance. To whom correspondence should be addressed: Institute of Molecular Medicine and Genetics, Rm. CB-2803, Medical College of Georgia, Augusta, GA 30912. Tel.: 706-721-8756; Fax: 706-721-8752; E-mail: wdynan{at}mail.mcg.edu.

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