Werstuck G, Capone J P
Department of Biochemistry, McMaster University, Hamilton, Ontario, Canada.
J Virol. 1989 Dec;63(12):5509-13. doi: 10.1128/JVI.63.12.5509-5513.1989.
In order to identify structural domains of the herpes simplex virus trans-activator Vmw65 required for protein-DNA complex formation, subfragments of Vmw65 were expressed in Escherichia coli as fusion polypeptides with protein A of Staphylococcus aureus, and the purified hybrids were used in a band shift assay. The results indicate that a region near the amino terminus of Vmw65 between amino acids 141 and 185 is necessary for complex formation.
为了鉴定单纯疱疹病毒反式激活因子Vmw65形成蛋白质-DNA复合物所需的结构域,Vmw65的亚片段在大肠杆菌中作为与金黄色葡萄球菌蛋白A的融合多肽表达,并且纯化的杂交体用于凝胶迁移试验。结果表明,Vmw65氨基酸141至185之间靠近氨基末端的区域是复合物形成所必需的。