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Nucleic Acids Research Advance Access first published online on September 20, 2006
This version published online on October 6, 2006
Nucleic Acids Research, doi:10.1093/nar/gkl665
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Published by Oxford University Press 2006

Molecular Biology

RAD51AP2, a novel vertebrate- and meiotic-specific protein, shares a conserved RAD51-interacting C-terminal domain with RAD51AP1/PIR51

Oleg V. Kovalenko, Claudia Wiese1 and David Schild1,*

Department of Medical Oncology, Dana-Farber Cancer Institute Boston, MA, 02115, USA 1 Life Sciences Division, Lawrence Berkeley National Laboratory Berkeley, CA 94720, USA

*To whom correspondence should be addressed. Tel: +1 510 486 6013; Fax: +1 510 486 6816; Email: dschild{at}lbl.gov

Received July 25, 2006. Revised August 25, 2006. Accepted August 27, 2006.

Many interacting proteins regulate and/or assist the activities of RAD51, a recombinase which plays a critical role in both DNA repair and meiotic recombination. Yeast two-hybrid screening of a human testis cDNA library revealed a new protein, RAD51AP2 (RAD51 Associated Protein 2), that interacts strongly with RAD51. A full-length cDNA clone predicts a novel vertebrate-specific protein of 1159 residues, and the RAD51AP2 transcript was observed only in meiotic tissue (i.e. adult testis and fetal ovary), suggesting a meiotic-specific function for RAD51AP2. In HEK293 cells the interaction of RAD51 with an ectopically-expressed recombinant large fragment of RAD51AP2 requires the C-terminal 57 residues of RAD51AP2. This RAD51-binding region shows 81% homology to the C-terminus of RAD51AP1/PIR51, an otherwise totally unrelated RAD51-binding partner that is ubiquitously expressed. Analyses using truncations and point mutations in both RAD51AP1 and RAD51AP2 demonstrate that these proteins use the same structural motif for RAD51 binding. RAD54 shares some homology with this RAD51-binding motif, but this homologous region plays only an accessory role to the adjacent main RAD51-interacting region, which has been narrowed here to 40 amino acids. A novel protein, RAD51AP2, has been discovered that interacts with RAD51 through a C-terminal motif also present in RAD51AP1.

The history dates have been corrected.


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