On the mechanism of strand assimilation by the herpes simplex virus type-1 single-strand DNA-binding protein (ICP8).
On the mechanism of strand assimilation by the herpes simplex virus type-1 single-strand DNA-binding protein (ICP8).
复制标题
单纯疱疹病毒1型单链DNA结合蛋白（ICP8）的链同化机制。
DOI：
10.1093/nar/gkg740
复制
发表时间：
2003
影响因子：
14.9
通讯作者：
Boehmer,PaulE
中科院分区：
文献类型：
--
作者：
Nimonkar,AmitabhV;Boehmer,PaulE
单纯疱疹病毒1型编码的单链DNA （ssDNA）结合蛋白ICP8促进单链DNA分子同化到同源双质粒中，从而形成位移环。在这里，我们研究这一过程的机制。与RecA型重组酶通过主动寻找同源性来催化链入侵不同，ICP8通过盐依赖的链退火机制起作用。该反应中的活性物质是一种ssDNA:ICP8核蛋白丝。ICP8似乎不需要与受体DNA相互作用。在较高浓度下，ICP8促进了逆反应，可能是由于它的螺旋不稳定活性。ICP8介导的链同化将单链特征赋予受体DNA，与置换环的形成一致。这些数据表明，ICP8的重组活性与真核Rad52的机制相似。
ICP8, the herpes simplex virus type‐1 encoded single‐strand DNA (ssDNA)‐binding protein, promotes the assimilation of a single‐stranded DNA molecule into a homologous duplex plasmid resulting in the formation of a displacement loop. Here we examine the mechanism of this process. In contrast to the RecA‐type recombinases that catalyze strand invasion via an active search for homology, ICP8 acts by a salt‐dependent strand annealing mechanism. The active species in this reaction is a ssDNA:ICP8 nucleoprotein filament. There appears to be no requirement for ICP8 to interact with the acceptor DNA. At higher concentrations, ICP8 promotes the reverse reaction, presumably owing to its helix destabilizing activity. ICP8‐mediated strand assimilation imparts single‐stranded character onto the acceptor DNA, consistent with the formation of a displacement loop. These data suggest that the recombination activity of ICP8 is similar to the mechanism of eukaryotic Rad52.