The herpes simplex virus type 1 DNA polymerase processivity factor, UL42, does not alter the catalytic activity of the UL9 origin-binding protein but facilitates its loading onto DNA.
The herpes simplex virus type 1 DNA polymerase processivity factor, UL42, does not alter the catalytic activity of the UL9 origin-binding protein but facilitates its loading onto DNA.
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DOI：
10.1093/nar/gki196
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发表时间：
2005
影响因子：
14.9
通讯作者：
Parris DS
中科院分区：
文献类型：
--
作者：
Trego KS;Zhu Y;Parris DS
单纯疱疹病毒1型UL42 DNA聚合酶持续合成因子与UL9物理相互作用，并增强其解链短的部分双链DNA的能力。在本报告中，在存在和不存在UL42的情况下，检查了UL9在单链（ss）或部分双链体DNA上易位期间的ATP水解，以确定UL42对UL9催化功能的影响。我们的研究表明，一个同源二聚体的UL9是足够的DNA易位耦合ATP水解，和稳态ATP酶催化率是大于部分双链体DNA在存在或不存在的UL42的SS DNA。虽然UL42蛋白增加了ATP水解的稳态速率由UL9在易位过程中无论是部分双链体或ss DNA，UL42对固有的ATP酶活性的UL9没有显着的影响。UL42也没有影响ATP水解的催化速率时，UL9是不限制，但增强稳态ATP酶速率仅在亚饱和UL9浓度。在亚饱和UL9与DNA的比例下，化学计量浓度的UL42显示出增加平衡时结合至ss DNA的UL9的量。这些数据支持一种模型，其中UL42增加UL9加载到DNA上的能力，从而增加其组装成能够解旋双链体DNA的功能复合物的能力。
The herpes simplex virus type 1 UL42 DNA polymerase processivity factor interacts physically with UL9 and enhances its ability to unwind short, partially duplex DNA. In this report, ATP hydrolysis during translocation of UL9 on single-stranded (ss) or partially duplex DNA was examined in the presence and absence of UL42 to determine the effect of UL42 on the catalytic function of UL9. Our studies reveal that a homodimer of UL9 is sufficient for DNA translocation coupled to ATP hydrolysis, and the steady-state ATPase catalytic rate was greater on partially duplex DNA than on ss DNA in the presence or absence of UL42. Although UL42 protein increased the steady-state rate for ATP hydrolysis by UL9 during translocation on either partially duplex or ss DNA, UL42 had no significant effect on the intrinsic ATPase activity of UL9. UL42 also had no effect on the catalytic rate of ATP hydrolysis when UL9 was not limiting but enhanced the steady-state ATPase rate at only subsaturating UL9 concentrations. At subsaturating UL9 to DNA ratios, stoichiometric concentrations of UL42 were shown to increase the amount of UL9 bound to ss DNA at equilibrium. These data support a model whereby UL42 increases the ability of UL9 to load onto DNA, thus increasing its ability to assemble into a functional complex capable of unwinding duplex DNA.
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