Marsich E, Piccini A, Xodo L E, Manzini G
Department of Biochemistry, Biophysics and Macromolecular Chemistry, University of Trieste, Italy.
Nucleic Acids Res. 1996 Oct 15;24(20):4029-33. doi: 10.1093/nar/24.20.4029.
In recent years several telomere binding proteins from eukaryotic organisms have been identified that are able to recognise specifically the duplex telomeric DNA repeat or the G-rich 3'-ending single strand. In this paper we present experimental evidence that HeLa nuclear extracts contain a protein that binds with high specificity to the single-stranded complementary d(CCCTAA)n repeat. Electrophoretic mobility shift assays show that the oligonucleotide d(CCCTAACCCTAACCCTAACCCT) forms a stable complex with this protein in the presence of up to 1000-fold excesses of single-stranded DNA and RNA competitors, but is prevented from doing so in the presence of its complementary strand. SDS-PAGE experiments after UV cross-linking of the complex provide an estimate of 50 kDa for the molecular weight of this protein.
近年来，已经鉴定出几种来自真核生物的端粒结合蛋白，它们能够特异性识别双链端粒DNA重复序列或富含G的3'末端单链。在本文中，我们提供了实验证据，表明HeLa细胞核提取物中含有一种与单链互补d(CCCTAA)n重复序列具有高度特异性结合的蛋白质。电泳迁移率变动分析表明，在存在高达1000倍过量的单链DNA和RNA竞争物的情况下，寡核苷酸d(CCCTAACCCTAACCCTAACCCT)与该蛋白质形成稳定的复合物，但在其互补链存在时则无法形成。复合物经紫外线交联后的SDS-PAGE实验给出了该蛋白质分子量约为50 kDa的估计值。
