Sigurdsson S, Van Komen S, Bussen W, Schild D, Albala J S, Sung P
Department of Molecular Medicine/Institute of Biotechnology, University of Texas Health Science Center at San Antonio, San Antonio, Texas 78245-3207, USA.
Genes Dev. 2001 Dec 15;15(24):3308-18. doi: 10.1101/gad.935501.
Five Rad51-like proteins, referred to as Rad51 paralogs, have been described in vertebrates. We show that two of them, Rad51B and Rad51C, are associated in a stable complex. Rad51B-Rad51C complex has ssDNA binding and ssDNA-stimulated ATPase activities. We also examined the functional interaction of Rad51B-Rad51C with Rad51 and RPA. Even though RPA enhances Rad51-catalyzed DNA joint formation via removal of secondary structure in the ssDNA substrate, it can also compete with Rad51 for binding to the substrate, leading to suppressed reaction efficiency. The competition by RPA for substrate binding can be partially alleviated by Rad51B-Rad51C. This recombination mediator function of Rad51B-Rad51C is likely required for the assembly of the Rad51-ssDNA nucleoprotein filament in vivo.
在脊椎动物中已发现五种类Rad51蛋白,即Rad51旁系同源物。我们发现其中两种,Rad51B和Rad51C,能形成稳定的复合物。Rad51B - Rad51C复合物具有单链DNA结合活性和单链DNA刺激的ATP酶活性。我们还研究了Rad51B - Rad51C与Rad51和RPA的功能相互作用。尽管RPA通过去除单链DNA底物中的二级结构来增强Rad51催化的DNA连接形成,但它也能与Rad51竞争结合底物,从而导致反应效率受到抑制。Rad51B - Rad51C可以部分缓解RPA对底物结合的竞争。Rad51B - Rad51C的这种重组介导功能可能是体内Rad51 - 单链DNA核蛋白丝组装所必需的。