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

  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},
  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

It is suggested that the architecture of the ternary complex provides a general paradigm for the facilitation of direct, but weak, interactions between polymerase and an activator.

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.



Solution Structure of the Activator Contact Domain of the RNA Polymerase α Subunit

The structure of the carboxyl-terminal domain of the Escherichia coli RNA polymerase α subunit (αCTD), which is regarded as the contact site for transcription activator proteins and for the promoter

Location, structure, and function of the target of a transcriptional activator protein.

The results establish that amino acids 258-265 of alpha constitute an "activation target" essential for CAP-dependent transcription at the lac promoter but not essential forCAP-independent transcription, and amino acid 261 is the most critical amino acid of the activation target.

Activation of prokaryotic transcription through arbitrary protein–protein contacts

It is shown that contact between a DNA-bound protein and a heterologous protein domain fused to RNA polymerase can elicit transcriptional activation; moreover, the strength of this engineered protein–protein interaction determines the amount of gene activation.

Transcription activation by catabolite activator protein (CAP).

Straightforward combination of the mechanisms for transcription activation at class I and class II CAP-dependent promoters permits synergistic transcription activation by multiple molecules of CAP, or by CAP and other activators.

Crystal structure of a CAP-DNA complex: the DNA is bent by 90 degrees

The 3 angstrom resolution crystal structure of the Escherichia coli catabolite gene activator protein (CAP) complexed with a 30-base pair DNA sequence shows that the DNA is bent by 90 degrees. This

An arcane role of DNA in transcription activation.

  • S. RyuS. GargesS. Adhya
  • Biology
    Proceedings of the National Academy of Sciences of the United States of America
  • 1994
The mechanism by which the cAMP receptor protein (CRP) activates transcription has been investigated using the lac promoter of Escherichia coli to find out whether an interaction between DNA-bound CRP and RNA polymerase is not sufficient.

UPs and downs in bacterial transcription initiation: the role of the alpha subunit of RNA polymerase in promoter recognition

The current state of the understanding of the α interaction with DNA during basal transcription initiation and activated transcription initiation is reviewed.

Identification of the activating region of catabolite gene activator protein (CAP): isolation and characterization of mutants of CAP specifically defective in transcription activation.

  • Y. ZhouX. ZhangR. Ebright
  • Biology, Chemistry
    Proceedings of the National Academy of Sciences of the United States of America
  • 1993
It is established that amino acids 156-162 are critical for transcription activation at the lac promoter but not for DNA binding and DNA bending.