Rep provides a second motor at the replisome to promote duplication of protein-bound DNA.
Rep provides a second motor at the replisome to promote duplication of protein-bound DNA.
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DOI：
10.1016/j.molcel.2009.11.009
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发表时间：
2009-11-25
期刊：
影响因子：
16
通讯作者：
McGlynn, Peter
中科院分区：
文献类型：
--
作者：
Guy, Colin P.;Atkinson, John;Gupta, Milind K.;Mahdi, Akeel A.;Gwynn, Emma J.;Rudolph, Christian J.;Moon, Peter B.;van Knippenberg, Ingeborg C.;Cadman, Chris J.;Dillingham, Mark S.;Lloyd, Robert G.;McGlynn, Peter
核蛋白复合物通过充当复制的有效阻断剂而对基因组稳定性提出挑战。如何解决这种冲突的一个有吸引力的模型是通过解旋酶直接靶向阻断的叉，解旋酶具有置换阻断蛋白质-DNA复合物的能力。我们发现Rep和UvrD都能促进E.大肠杆菌复制体在体外被核蛋白复合物阻断，这种活性是体内清除蛋白质块（主要是转录复合物）所必需的，并且与复制解旋酶相反的易位极性对于这种活性是关键的。然而，这两个解旋酶是不等价的。Rep而不是UvrD与复制解旋酶在物理和功能上相互作用。相反，UvrD可能提供了复制、修复和重组过程中蛋白质-DNA复合物周转的一般手段。因此，Rep和UvrD提供了两种关于生物体如何促进蛋白质结合DNA复制的对比解决方案。
Nucleoprotein complexes present challenges to genome stability by acting as potent blocks to replication. One attractive model of how such conflicts are resolved is direct targeting of blocked forks by helicases with the ability to displace the blocking protein-DNA complex. We show that Rep and UvrD each promote movement of E. coli replisomes blocked by nucleoprotein complexes in vitro, that such an activity is required to clear protein blocks (primarily transcription complexes) in vivo, and that a polarity of translocation opposite that of the replicative helicase is critical for this activity. However, these two helicases are not equivalent. Rep but not UvrD interacts physically and functionally with the replicative helicase. In contrast, UvrD likely provides a general means of protein-DNA complex turnover during replication, repair, and recombination. Rep and UvrD therefore provide two contrasting solutions as to how organisms may promote replication of protein-bound DNA.
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