Nagai A, Saijo M, Kuraoka I, Matsuda T, Kodo N, Nakatsu Y, Mimaki T, Mino M, Biggerstaff M, Wood R D
Institute for Molecular and Cellular Biology, Osaka University, Japan.
Biochem Biophys Res Commun. 1995 Jun 26;211(3):960-6. doi: 10.1006/bbrc.1995.1905.
The human XPA and ERCC1 proteins, which are involved in early steps of nucleotide excision repair of DNA, specifically interacted in an in vitro binding assay and a yeast two-hybrid assay. A stretch of consecutive glutamic acid residues in XPA was needed for binding to ERCC1. Binding of XPA to damaged DNA was markedly increased by the interaction of the XPA and ERCC1 proteins. ERCC1 did not enhance binding to DNA when a truncated XPA protein, MF122, was used in place of the XPA protein. MF122 retains damaged DNA binding activity but lacks the region for protein-protein interaction including the E-cluster region. These results suggest that the XPA/ERCC1 interaction may participate in damage-recognition as well as in incision at the 5' site of damage during nucleotide excision repair.
参与DNA核苷酸切除修复早期步骤的人类XPA和ERCC1蛋白，在体外结合试验和酵母双杂交试验中发生特异性相互作用。XPA中一段连续的谷氨酸残基对于与ERCC1结合是必需的。XPA与ERCC1蛋白的相互作用显著增强了XPA与受损DNA的结合。当使用截短的XPA蛋白MF122代替XPA蛋白时，ERCC1并未增强与DNA的结合。MF122保留了受损DNA结合活性，但缺乏包括E簇区域在内的蛋白质-蛋白质相互作用区域。这些结果表明，XPA/ERCC1相互作用可能参与核苷酸切除修复过程中的损伤识别以及损伤5'位点的切口形成。
