Structural Basis of Transcription Activation : The CAP-CTD-DNA Complex

By B. Benoff, Huanwang Yang, Catherine L. Lawson, G. Parkinson, Jinsong Liu, E. Blatter, Y. Ebright, Helen M. Berman, R. Ebright. 2002

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Neglected role of cAMP receptor protein monomer (2011, background): “bound form. The 44 bp oligonucleotide contains CRP binding site [ 18 ].”
Catabolite activator protein: DNA binding and transcription activation. (2004, methodology): “The recently determined crystal structure of a complex containing CAP, aCTD, and DNA has provided the first high-resolution structural description of the interaction between a transcription activator and its functional target within the general transcriptional machinery (Figure 4) [44 ].”
Structural basis for cAMP-mediated allosteric control of the catabolite activator protein (2009, background): “In the cAMP-bound state, CAP binds to DNA sites located in or adjacent to target promoters resulting in modulation of interactions of RNA polymerase with target promoters (1, 3).”
Three-dimensional EM structure of an intact activator-dependent transcription initiation complex (2009, methodology): “At Class I CAP-dependent promoters, CAP activates transcription by making protein-protein interactions with the RNAP subunit C-terminal domain ( CTD), a 9-kDa independently folded domain that is flexibly tethered to the remainder of RNAP (1, 2, 7, 8).”