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Catabolite activator protein: DNA binding and transcription activation Export

Current Opinion in Structural Biology, Vol. 14, No. 1. (February 2004), pp. 10-20.

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allostery cap cap_dna protein review

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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 [alpha] subunit C-terminal domain ([alpha]CTD) 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-[alpha]CTD-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-[alpha]CTD-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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