大肠杆菌环磷酸腺苷受体蛋白与RNA聚合酶的结合。
Binding of the cyclic AMP receptor protein of Escherichia coli to RNA polymerase.
作者信息
Pinkney M, Hoggett J G
机构信息
Department of Biology, University of York, U.K.
出版信息
Biochem J. 1988 Mar 15;250(3):897-902. doi: 10.1042/bj2500897.
Abstract
Fluorescence polarization studies were used to study the interaction of a fluorescein-labelled conjugate of the Escherichia coli cyclic AMP receptor protein (F-CRP) and RNA polymerase. Under conditions of physiological ionic strength, F-CRP binds to RNA polymerase holoenzyme in a cyclic AMP-dependent manner; the dissociation constant was about 3 microM in the presence of cyclic AMP and about 100 microM in its absence. Binding to core RNA polymerase under the same conditions was weak (Kdiss. approx. 80-100 microM) and independent of cyclic AMP. Competition experiments established that native CRP and F-CRP compete for the same binding site on RNA polymerase holoenzyme and that the native protein binds about 3 times more strongly than does F-CRP. Analytical ultracentrifuge studies showed that CRP binds predominantly to the monomeric rather than the dimeric form of RNA polymerase.
摘要
荧光偏振研究被用于研究大肠杆菌环磷酸腺苷受体蛋白（F-CRP）的荧光素标记共轭物与RNA聚合酶之间的相互作用。在生理离子强度条件下，F-CRP以环磷酸腺苷依赖的方式与RNA聚合酶全酶结合；在存在环磷酸腺苷的情况下，解离常数约为3微摩尔，在不存在环磷酸腺苷的情况下约为100微摩尔。在相同条件下与核心RNA聚合酶的结合较弱（解离常数约为80 - 100微摩尔）且与环磷酸腺苷无关。竞争实验表明，天然CRP和F-CRP竞争RNA聚合酶全酶上的相同结合位点，并且天然蛋白的结合强度比F-CRP强约3倍。分析超速离心研究表明，CRP主要与RNA聚合酶的单体形式而非二聚体形式结合。
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