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Published on: August 26, 2012
Structural basis for promoter-10 element recognition by the bacterial RNA polymerase σ subunit
Andrey Feklistov1, Seth A Darst
1The Rockefeller University, 1230 York Avenue, New York, NY 10065, USA. afeklistov@rockefeller.edu
Cell
|December 6, 2011
Summary
Bacterial RNA polymerase sigma subunit recognizes the -10 promoter element, driving DNA opening. Crystal structures reveal key interactions with A(-11) and T(-7) bases, explaining transcription initiation.
Area of Science:
- Molecular Biology
- Structural Biology
- Biochemistry
Background:
- Bacterial transcription initiation is crucial for gene regulation.
- RNA polymerase sigma subunit binding to the -10 promoter element is essential for promoter opening.
- Understanding the structural basis of this interaction is key to deciphering transcription regulation.
Purpose of the Study:
- To determine the crystal structures of the sigma subunit domain 2 bound to -10 promoter DNA.
- To elucidate the molecular interactions driving promoter opening and transcription initiation.
Main Methods:
- X-ray crystallography to obtain high-resolution structures.
- Biochemical assays to validate structural findings.
Main Results:
- Crystal structures reveal extensive interactions between sigma domain 2 and the DNA backbone.
- Specific base interactions with A(-11) and T(-7) were identified, with these bases flipped out and buried in protein pockets.
- A model is proposed where -10 element recognition by sigma directly drives promoter opening.
Conclusions:
- The study provides a detailed structural mechanism for bacterial promoter melting.
- A(-11) and T(-7) play critical roles in sequence recognition and DNA extrusion.
- These findings offer significant insights into the formation of the transcription bubble during initiation.
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