Kovalenko O V, Golub E I, Bray-Ward P, Ward D C, Radding C M
Department of Genetics and Department of Molecular Biophysics and Biochemistry, Yale University School of Medicine, 333 Cedar Street, New Haven, CT 06510, USA.
Nucleic Acids Res. 1997 Dec 15;25(24):4946-53. doi: 10.1093/nar/25.24.4946.
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.
利用酵母双杂交系统，我们分离出一个编码新型人类蛋白质的cDNA，该蛋白质名为Pir51，它能与人类Rad51重组酶强烈相互作用。体外分析证实了Rad51与Pir51之间的相互作用。Pir51 mRNA在许多人类器官中表达，最显著的是在睾丸、胸腺、结肠和小肠中。通过荧光原位杂交将Pir51基因座定位到染色体12p13.1 - 13.2。Pir51蛋白在大肠杆菌中表达并纯化至近乎均一。生化分析表明，Pir51蛋白能结合单链和双链DNA，并且能够使DNA聚集。该蛋白也能结合RNA。Pir51蛋白可能代表了推测在哺乳动物细胞中进行同源重组和DNA修复的多蛋白复合物的一个新成员。
