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Nucleic Acids Research 2006 34(9):2587-2597; doi:10.1093/nar/gkl280
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Published online 17 May 2006

© The Author 2006. Published by Oxford University Press. All rights reserved
The online version of this article has been published under an open access model. Users are entitled to use, reproduce, disseminate, or display the open access version of this article for non-commercial purposes provided that: the original authorship is properly and fully attributed; the Journal and Oxford University Press are attributed as the original place of publication with the correct citation details given; if an article is subsequently reproduced or disseminated not in its entirety but only in part or as a derivative work this must be clearly indicated. For commercial re-use, please contact journals.permissions@oxfordjournals.org

Article

Multiple start codons and phosphorylation result in discrete Rad52 protein species

Adriana Antúnez de Mayolo, Michael Lisby1, Naz Erdeniz2, Tanja Thybo3, Uffe H. Mortensen3 and Rodney Rothstein*

Department of Genetics & Development, Columbia University Medical Center 701 West 168th Street, New York, NY 10032, USA 1 Department of Genetics, Institute of Molecular Biology and Physiology, University of Copenhagen Øster Farimagsgade 2A, DK-1353 Copenhagen K, Denmark 2 Department of Molecular and Medical Genetics, Oregon Health Sciences University 3181 SW Sam Jackson Park Road, Mail Code L103, Portland, OR 97201, USA 3 Center for Microbial Biotechnology, BioCentrum-DTU, Technical University of Denmark Building 223, DK-2800 Lyngby, Denmark

*To whom correspondence should be addressed. Tel: +1 212 305 1733; Fax: +1 212 923 2090; Email: rothstein{at}cancercenter.columbia.edu

Received February 10, 2006. Revised March 8, 2006. Accepted April 4, 2006.

The sequence of the Saccharomyces cerevisiae RAD52 gene contains five potential translation start sites and protein-blot analysis typically detects multiple Rad52 species with different electrophoretic mobilities. Here we define the gene products encoded by RAD52. We show that the multiple Rad52 protein species are due to promiscuous choice of start codons as well as post-translational modification. Specifically, Rad52 is phosphorylated both in a cell cycle-independent and in a cell cycle-dependent manner. Furthermore, phosphorylation is dependent on the presence of the Rad52 C terminus, but not dependent on its interaction with Rad51. We also show that the Rad52 protein can be translated from the last three start sites and expression from any one of them is sufficient for spontaneous recombination and the repair of gamma-ray-induced double-strand breaks.

Present address: Adriana Antúnez de Mayolo, Sylvester Comprehensive Cancer Center, University of Miami Medical Center, 1550 NW 10th Avenue, Miami, FL 33136, USA


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[Abstract] [Full Text] [PDF]


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