Department of Biochemistry and Purdue University Center for Cancer Research, Purdue University, 175 S. University St., West Lafayette, IN 47907, USA.
FEBS Lett. 2011 Sep 16;585(18):2920-8. doi: 10.1016/j.febslet.2011.08.008. Epub 2011 Aug 12.
A vast array of proteins is recruited to the replication fork in a dynamic and coordinated manner through physical interactions with Proliferating Cell Nuclear Antigen, PCNA. How this complex exchange of PCNA binding partners is choreographed to ensure proper replication origin licensing, DNA synthesis during normal replication or repair of DNA damage, chromatin assembly, DNA methylation, histone modification, and sister chromatid cohesion is only beginning to be appreciated. In this review, several roles of ubiquitin-related modifications in the recruitment and turnover of PCNA-interacting proteins at the replication fork are considered.
大量蛋白质通过与增殖细胞核抗原（PCNA）的物理相互作用，以动态和协调的方式被招募到复制叉。这种 PCNA 结合伙伴的复杂交换如何被精心编排，以确保适当的复制起点许可、正常复制期间的 DNA 合成或 DNA 损伤修复、染色质组装、DNA 甲基化、组蛋白修饰和姐妹染色单体凝聚，这仅仅才开始被人们所理解。在这篇综述中，考虑了泛素相关修饰在复制叉处 PCNA 相互作用蛋白的招募和周转中的几个作用。
