Reference: Kovalenko OV, et al. (1997) A novel nucleic acid-binding protein that interacts with human rad51 recombinase. Nucleic Acids Res 25(24):4946-53

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Abstract


Using the yeast two-hybrid system, we isolated a cDNA encoding a novel human protein, named Pir51, that strongly interacts with human Rad51 recombinase. Analysis in vitro confirmed the interaction between Rad51 and Pir51. Pir51 mRNA is expressed in a number of human organs, most notably in testis, thymus, colon and small intestine. The Pir51 gene locus was mapped to chromosome 12p13.1-13. 2 by fluorescence in situ hybridization. The Pir51 protein was expressed in Escherichia coli and purified to near homogeneity. Biochemical analysis shows that the Pir51 protein binds both single- and double-stranded DNA, and is capable of aggregating DNA. The protein also binds RNA. The Pir51 protein may represent a new member of the multiprotein complexes postulated to carry out homologous recombination and DNA repair in mammalian cells.

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Journal Article | Research Support, U.S. Gov't, P.H.S.
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Kovalenko OV, Golub EI, Bray-Ward P, Ward DC, Radding CM
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