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Structural basis of transcription activation
Yu Feng1, Yu Zhang1, Richard H Ebright2
1Waksman Institute and Department of Chemistry and Chemical Biology, Rutgers University, Piscataway, NJ 08854, USA.
Science (New York, N.Y.)
|June 11, 2016
Summary
Class II transcription activators, like TTHB099 (TAP), enhance gene transcription by stabilizing RNA polymerase (RNAP) interactions. This structural study reveals how TAP activates transcription initiation via protein-DNA and protein-protein interactions.
Area of Science:
- Molecular Biology
- Structural Biology
- Biochemistry
Background:
- Class II transcription activators bind DNA near promoters to initiate transcription.
- They stimulate the conversion of closed RNA polymerase (RNAP)-promoter complexes to open, active complexes.
Purpose of the Study:
- To determine the high-resolution crystal structure of a bacterial class II transcription activation complex.
- To elucidate the molecular mechanisms of transcription activation by TTHB099 (TAP) and its interactions with RNAP.
Main Methods:
- X-ray crystallography at 4.4 angstrom resolution.
- Structural analysis of an intact bacterial transcription activation complex.
Main Results:
- The crystal structure reveals interactions between RNAP holoenzyme and DNA during transcription initiation.
- Detailed interactions between TTHB099 (TAP) and RNAP holoenzyme responsible for transcription activation were identified.
- TAP stabilizes RNAP holoenzyme through direct protein-protein interactions, promoting promoter isomerization.
Conclusions:
- The structure provides a molecular basis for understanding class II transcription activation.
- TTHB099 (TAP) activates transcription by stabilizing the RNAP holoenzyme, facilitating promoter opening.
- This study highlights the role of protein-protein interactions in regulating transcription initiation.
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