Sawadogo M, Sentenac A, Fromageot P
J Biol Chem. 1980 Jan 10;255(1):12-5.
A basic 37,000-dalton protein (P37), purified from yeast cells, interacts with yeast RNA polymerase B and drastically increases its specific activity. A complex of P37 and RNA polymerase can be isolated by sedimentation through a glycerol gradient. The complex is dissociated at the ionic strength of 0.9. The preferential binding of P37 with RNA polymerase form BI (with the unproteolyzed B220 subunit) was visualized by polyacrylamide gel electrophoresis under nondenaturing conditions. Kinetic analysis of the RNA polymerase cofactor interaction indicated that the dissociation constant for the complex is 5 X 10(-8) M.
从酵母细胞中纯化出的一种基本的37000道尔顿蛋白质（P37），可与酵母RNA聚合酶B相互作用，并显著提高其比活性。通过甘油梯度沉降可分离出P37与RNA聚合酶的复合物。该复合物在离子强度为0.9时会解离。在非变性条件下，通过聚丙烯酰胺凝胶电泳观察到P37与BI型RNA聚合酶（带有未被蛋白酶水解的B220亚基）的优先结合。对RNA聚合酶辅因子相互作用的动力学分析表明，该复合物的解离常数为5×10^(-8) M。
