Crute J J, Tsurumi T, Zhu L A, Weller S K, Olivo P D, Challberg M D, Mocarski E S, Lehman I R
Department of Biochemistry, Stanford University School of Medicine, CA 94305.
Proc Natl Acad Sci U S A. 1989 Apr;86(7):2186-9. doi: 10.1073/pnas.86.7.2186.
In an earlier report, we described a DNA helicase that is specifically induced upon infection of Vero cells with herpes simplex virus 1. We have purified this enzyme to near homogeneity and found it to consist of three polypeptides with molecular weights of 120,000, 97,000, and 70,000. Immunochemical analysis has shown these polypeptides to be the products of three of the genes UL52, UL5, and UL8 that are required for replication of a plasmid containing a herpes simplex 1 origin (oriS). In addition to helicase activity, the enzyme contains a tightly associated DNA primase. Thus, the three-subunit enzyme is a helicase-primase complex that may prime lagging-strand synthesis as it unwinds DNA at the viral replication fork.
在早期的一份报告中,我们描述了一种DNA解旋酶,它在单纯疱疹病毒1感染Vero细胞后被特异性诱导。我们已将这种酶纯化至接近均一状态,发现它由分子量分别为120,000、97,000和70,000的三种多肽组成。免疫化学分析表明,这些多肽是包含单纯疱疹1型起源(oriS)的质粒复制所需的三个基因UL52、UL5和UL8的产物。除了解旋酶活性外,该酶还含有紧密结合的DNA引发酶。因此,这种三亚基酶是一种解旋酶 - 引发酶复合物,它在病毒复制叉处解开DNA时可能引发后随链的合成。