Mahadik S P, Dharmgrongartama B, Srinivasan P R
Proc Natl Acad Sci U S A. 1972 Jan;69(1):162-6. doi: 10.1073/pnas.69.1.162.
A partially purified protein isolated from bacteriophage T3-infected cells of Escherichia coli B markedly inhibits the activity of E. coli RNA polymerase, slightly inhibits the activity of purified T3 polymerase, and does not inhibit the activity of either core polymerase or the ribosome-bound T3 polymerase. The properties of this protein and its mechanism of action have been studied. It appears to antagonize the action of the sigma factor component of RNA polymerase.
从噬菌体T3感染的大肠杆菌B细胞中分离出的一种部分纯化的蛋白质,能显著抑制大肠杆菌RNA聚合酶的活性,轻微抑制纯化的T3聚合酶的活性,而不抑制核心聚合酶或核糖体结合的T3聚合酶的活性。已对该蛋白质的性质及其作用机制进行了研究。它似乎拮抗RNA聚合酶的σ因子成分的作用。