ATP-dependent unwinding of a minimal origin of DNA replication by the origin-binding protein and the single-strand DNA-binding protein ICP8 from Herpes simplex virus type I
ATP-dependent unwinding of a minimal origin of DNA replication by the origin-binding protein and the single-strand DNA-binding protein ICP8 from Herpes simplex virus type I
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DOI：
10.1074/jbc.m208270200
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发表时间：
2002-10-25
影响因子：
4.8
通讯作者：
Elias, P
中科院分区：
文献类型：
--
作者：
Aslani, A;Olsson, M;Elias, P
单纯疱疹病毒I型起源结合蛋白（OBP）由UL 9基因编码。OBP以协同和序列特异性的方式结合DNA复制起点oriS。OBP也是一种ATP依赖性DNA解旋酶。我们最近发现，单链oriS折叠成一个独特的和进化上保守的构象，oriS*，这是稳定结合的OBP。OriS* 含有一个稳定的发夹结构，由oriS中盒I和盒III之间的互补碱基配对形成。在这里，我们表明，OBP，在单链DNA结合蛋白ICP 8的存在下，可以转换一个80碱基对的双链最小的oriS片段oriS*，并形成一个OBP-oriS * 复合物。OBP-oriS * 复合物的形成需要可水解的ATP。我们还表明，在ICP 8和ATP的存在下，OBP促进缓慢，但具体的和完全的双链体最小的oriS解旋。OBP-oriS* 复合物可能作为疱疹病毒复制体的组装位点的可能性进行了讨论。
The Herpes simplex virus type I origin-binding protein, OBP, is encoded by the UL9 gene. OBP binds the origin of DNA replication, oriS, in a cooperative and sequence-specific manner. OBP is also an ATP-dependent DNA helicase. We have recently shown that single-stranded oriS folds into a unique and evolutionarily conserved conformation, oriS*, which is stably bound by OBP. OriS* contains a stable hairpin formed by complementary base pairing between box I and box III in oriS. Here we show that OBP, in the presence of the single-stranded DNA-binding protein ICP8, can convert an 80-base pair double-stranded minimal oriS fragment to oriS* and form an OBP-oriS* complex. The formation of an OBP-oriS* complex requires hydrolysable ATP. We also demonstrate that OBP in the presence of ICP8 and ATP promotes slow but specific and complete unwinding of duplex minimal oriS. The possibility that the OBP-oriS* complex may serve as an assembly site for the herpes virus replisome is discussed.