Lawson Catherine L, Swigon David, Murakami Katsuhiko S, Darst Seth A, Berman Helen M, Ebright Richard H
Department of Chemistry and Chemical Biology, Rutgers University, 610 Taylor Road, Piscataway, NJ 08854, USA.
Curr Opin Struct Biol. 2004 Feb;14(1):10-20. doi: 10.1016/j.sbi.2004.01.012.
Recently determined structures of the Escherichia coli catabolite activator protein (CAP) in complex with DNA, and in complex with the RNA polymerase alpha subunit C-terminal domain (alphaCTD) and DNA, have yielded insights into how CAP binds DNA and activates transcription. Comparison of multiple structures of CAP-DNA complexes has revealed the contributions of direct and indirect readout to DNA binding by CAP. The structure of the CAP-alphaCTD-DNA complex has provided the first structural description of interactions between a transcription activator and its functional target within the general transcription machinery. Using the structure of the CAP-alphaCTD-DNA complex, the structure of an RNA polymerase-DNA complex, and restraints from biophysical, biochemical and genetic experiments, it has been possible to construct detailed three-dimensional models of intact class I and class II transcription activation complexes.
最近确定的大肠杆菌分解代谢物激活蛋白（CAP）与DNA的复合物结构，以及与RNA聚合酶α亚基C末端结构域（αCTD）和DNA的复合物结构，为了解CAP如何结合DNA并激活转录提供了线索。对CAP-DNA复合物多种结构的比较揭示了直接和间接识别对CAP结合DNA的贡献。CAP-αCTD-DNA复合物的结构首次对转录激活因子与其在通用转录机制中的功能靶点之间的相互作用进行了结构描述。利用CAP-αCTD-DNA复合物的结构、RNA聚合酶-DNA复合物的结构以及生物物理、生化和遗传学实验的限制条件，已能够构建完整的I类和II类转录激活复合物的详细三维模型。
