Clower Randolph V, Fisk John C, Melendy Thomas
Department of Microbiology & Immunology, The School of Medicine and Biomedical Sciences, University at Buffalo, 213 Biomedical Research Building, 3435 Main Street, Buffalo, NY 14214, USA.
J Virol. 2006 Feb;80(3):1584-7. doi: 10.1128/JVI.80.3.1584-1587.2006.
The papillomavirus (PV) E1 helicase plays a direct role in recruiting cellular DNA replication factors, such as replication protein A or polymerase alpha-primase, to replicate PV genomes. Here, E1 is shown to bind to human topoisomerase I and stimulate its relaxation activity up to sevenfold. The interaction between E1 and topoisomerase I was mapped to the E1 DNA binding domain and C terminus. These findings imply a mechanism for the recruitment of topoisomerase I to PV DNA replication forks and for stimulating topoisomerase I to allow for efficient relaxation of the torsional stress induced by replication fork progression.
乳头瘤病毒(PV)E1解旋酶在募集细胞DNA复制因子(如复制蛋白A或聚合酶α-引发酶)以复制PV基因组方面发挥直接作用。在此,研究表明E1可与人拓扑异构酶I结合,并将其松弛活性提高多达七倍。E1与拓扑异构酶I之间的相互作用定位于E1 DNA结合结构域和C末端。这些发现揭示了一种机制,可将拓扑异构酶I募集到PV DNA复制叉,并刺激拓扑异构酶I,以便有效缓解复制叉前进所诱导的扭转应力。