2. Academic Validation
  3. A novel nucleic acid-binding protein that interacts with human rad51 recombinase

A novel nucleic acid-binding protein that interacts with human rad51 recombinase

  • Nucleic Acids Res. 1997 Dec 15;25(24):4946-53. doi: 10.1093/nar/25.24.4946.
O V Kovalenko 1,  E I Golub,  P Bray-Ward,  D C Ward,  C M Radding
Affiliations

Affiliation

  • 1 Department of Genetics and Department of Molecular Biophysics and Biochemistry, Yale University School of Medicine, 333 Cedar Street, New Haven, CT 06510, USA.
PMID: 9396801 DOI: 10.1093/nar/25.24.4946
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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