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Catabolite activator protein: DNA binding and transcription activation

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CURRENT OPINION IN STRUCTURAL BIOLOGY
卷 14, 期 1, 页码 10-20

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CURRENT BIOLOGY LTD
DOI: 10.1016/j.sbi.2004.01.012

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资金

  1. NIGMS NIH HHS [R01 GM021589, GM34809, R37 GM041376, R01 GM041376, R01 GM034809, GM41376, GM64375, P20 GM064375, GM21589, R01 GM021589-29] Funding Source: Medline

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Recently determined structures of the Escherichia coli catabolite activator protein (CAP) in complex with DNA, and in complex with the RNA polymerase a 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.

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