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

@article{Benoff2002StructuralBO,
  title={Structural Basis of Transcription Activation: The CAP-$\alpha$CTD-DNA Complex},
  author={Brian Eric Benoff and Huanwang Yang and Catherine L. Lawson and Gary N Parkinson and Jinsong Liu and Erich E. Blatter and Yon W. Ebright and Helen M. Berman and Richard H. Ebright},
  journal={Science},
  year={2002},
  volume={297},
  pages={1562 - 1566}
}
The Escherichia coli catabolite activator protein (CAP) activates transcription at Plac, Pgal, and other promoters through interactions with the RNA polymerase α subunit carboxyl-terminal domain (αCTD). We determined the crystal structure of the CAP-αCTD-DNA complex at a resolution of 3.1 angstroms. CAP makes direct protein-protein interactions with αCTD, and αCTD makes direct protein-DNA interactions with the DNA segment adjacent to the DNA site for CAP. There are no large-scale conformational… 

Catabolite activator protein: DNA binding and transcription activation.

Three-dimensional EM structure of an intact activator-dependent transcription initiation complex

The experimentally determined 3D structure of an intact activator-dependent transcription initiation complex comprising the Escherichia coli catabolite activator protein (CAP), RNA polymerase holoenzyme (RNAP), and a DNA fragment defines the organization of a Class I CAP-RNAP-promoter complex and supports previously proposed interactions.

A regulatory protein that interferes with activator-stimulated transcription in bacteria

The discovery of an “anti-α” factor Spx in Bacillus subtilis that blocks transcriptional activation by binding to the α-C-terminal domain, thereby interfering with the capacity of RNAP to respond to certain activator proteins.

RNA polymerase and an activator form discrete subcomplexes in a transcription initiation complex

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Structure and function of CarD, an essential mycobacterial transcription factor

It is proposed that CarD functions by forming protein/protein and protein/DNA interactions that bridge the RNAP to the promoter DNA, which uses an unusual mechanism for regulating transcription.

Visualization of two architectures in class-II CAP-dependent transcription activation

Cryo-EM structures of an intact E. coli class-II CAP-dependent transcription activation complex (TAC) with and without de novo RNA transcript reveal two distinct architectures of TAC and show that CAP-binding induces substantial conformational changes in all the subunits of RNAP and consequently widens the main cleft ofRNAP considerably to facilitate DNA promoter entering and formation of initiation open complex.

RNA polymerase structure and function at lac operon.

Activation of σ28-dependent transcription in Escherichia coli by the cyclic AMP receptor protein requires an unusual promoter organization

The ternary activator–RNA polymerase–aer promoter open complex is organized differently from complexes at previously characterized promoters, suggesting a common activation mechanism.
...

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