Joung J K, Koepp D M, Hochschild A
Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, MA 02115.
Science. 1994 Sep 23;265(5180):1863-6. doi: 10.1126/science.8091212.
Two heterologous prokaryotic activators, the bacteriophage lambda cI protein (lambda cI) and the Escherichia coli cyclic AMP receptor protein (CRP), were shown to activate transcription synergistically from an artificial promoter bearing binding sites for both proteins. The synergy depends on a functional activation (positive control) surface on each activator. These results imply that both proteins interact directly with RNA polymerase and thus suggest a precise mechanism for transcriptional synergy: the interaction of two activators with two distinct surfaces of RNA polymerase.
两种异源原核激活因子，即噬菌体λ cI蛋白（λ cI）和大肠杆菌环磷酸腺苷受体蛋白（CRP），已被证明可从一个带有这两种蛋白结合位点的人工启动子协同激活转录。这种协同作用取决于每个激活因子上的功能性激活（正调控）表面。这些结果表明这两种蛋白都直接与RNA聚合酶相互作用，因此提示了一种转录协同作用的精确机制：两种激活因子与RNA聚合酶的两个不同表面相互作用。
