HERPES-SIMPLEX VIRUS HELICASE-PRIMASE - THE UL8 PROTEIN IS NOT REQUIRED FOR DNA-DEPENDENT ATPASE AND DNA HELICASE ACTIVITIES
HERPES-SIMPLEX VIRUS HELICASE-PRIMASE - THE UL8 PROTEIN IS NOT REQUIRED FOR DNA-DEPENDENT ATPASE AND DNA HELICASE ACTIVITIES
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DOI：
10.1093/nar/18.12.3573
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发表时间：
1990-06-25
影响因子：
14.9
通讯作者：
STOW, ND
中科院分区：
文献类型：
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作者：
CALDER, JM;STOW, ND
单纯疱疹病毒1型解旋酶-引物酶复合体由UL5、UL8和UL52基因的产物组成。我们利用杆状病毒载体在昆虫细胞中表达了这些蛋白，并研究了与DNA解绕功能相关的酶活性要求。与最近的一份报告（Dodson, m.s., Crute, j.j., Bruckner， R.C. and Lehman， I.R. 1989， J. Biol）一致。我们发现，在被表达UL5、UL8和UL52蛋白的病毒感染的昆虫细胞中，DNA依赖的atp酶和DNA解旋酶活性在体内组装。此外，在仅表达UL5和UL52产物的细胞中也检测到这些活性，这表明UL8蛋白的存在对atp酶和解旋酶活性都不是必需的。
The herpes simplex virus type 1 helicase-primase complex consists of the products of the UL5, UL8 and UL52 genes. We have expressed these proteins in insect cells using baculovirus vectors and studied the requirements for enzymatic activities associated with the DNA unwinding function of the complex. In agreement with a recent report (Dodson, M.S., Crute, J.J., Bruckner, R.C. and Lehman, I.R. 1989, J. Biol. Chem. 264, 20835-20838) we find that DNA-dependent ATPase and DNA helicase activities are assembled in vivo in insect cells triply infected with viruses expressing the UL5, UL8 and UL52 proteins. Moreover, these activities, were also detected in cells in which only the UL5 and UL52 products were expressed indicating that the presence of the UL8 protein is essential for neither the ATPase nor helicase activity of the complex.