TY - JOUR
T1 - Catabolite activator protein
T2 - DNA binding and transcription activation
AU - Lawson, Catherine L.
AU - Swigon, David
AU - Murakami, Katsuhiko S.
AU - Darst, Seth A.
AU - Berman, Helen M.
AU - Ebright, Richard H.
N1 - Funding Information:
We thank B Benoff, A Kapanidis, A Napoli, N Naryshkin, and W Olson for discussion. Research on CAP in the authors’ laboratories is funded by National Institutes of Health grants GM21589 (HMB and CLL), GM34809 (W Olson and DS), GM41376 (RHE) and GM64375 (R Levy and RHE), and by a Howard Hughes Medical Investigatorship (RHE).
PY - 2004/2
Y1 - 2004/2
N2 - Recently determined structures of the Escherichia coli catabolite activator protein (CAP) in complex with DNA, and in complex with the RNA polymerase α subunit C-terminal domain (αCTD) 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-αCTD-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-αCTD-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.
AB - Recently determined structures of the Escherichia coli catabolite activator protein (CAP) in complex with DNA, and in complex with the RNA polymerase α subunit C-terminal domain (αCTD) 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-αCTD-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-αCTD-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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U2 - 10.1016/j.sbi.2004.01.012
DO - 10.1016/j.sbi.2004.01.012
M3 - Review article
C2 - 15102444
AN - SCOPUS:1342345189
SN - 0959-440X
VL - 14
SP - 10
EP - 20
JO - Current Opinion in Structural Biology
JF - Current Opinion in Structural Biology
IS - 1
ER -