Xiao P, Capone J P
Department of Biochemistry, McMaster University, Hamilton, Ontario, Canada.
Mol Cell Biol. 1990 Sep;10(9):4974-7. doi: 10.1128/mcb.10.9.4974-4977.1990.
The herpes simplex virus transactivator Vmw65 assembles into a multicomponent protein-DNA complex along with the octamer binding protein Oct-1. Using affinity chromatography on columns conjugated with purified Vmw65 fusion protein expressed in Escherichia coli, we demonstrate that a cellular factor, distinct from Oct-1, binds to Vmw65 in the absence of target DNA and is necessary for Vmw65-mediated complex assembly with Oct-1.
单纯疱疹病毒反式激活因子Vmw65与八聚体结合蛋白Oct-1一起组装成多组分蛋白质-DNA复合物。通过在与大肠杆菌中表达的纯化Vmw65融合蛋白偶联的柱上进行亲和层析,我们证明了一种不同于Oct-1的细胞因子在没有靶DNA的情况下与Vmw65结合,并且是Vmw65介导的与Oct-1的复合物组装所必需的。