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06:10
Following Cell-fate in E. coli After Infection by Phage Lambda
Published on: October 14, 2011
Domain structure and DNA binding regions of beta protein from bacteriophage lambda
Zengru Wu1, Xu Xing, Casey E Bohl
1Division of Pharmaceutics, College of Pharmacy, Ohio State University, Columbus, Ohio 43210, USA.
The Journal of Biological Chemistry
|July 6, 2006
Summary
Bacteriophage lambda beta protein
Area of Science:
- Molecular Biology
- Biochemistry
Background:
- Bacteriophage lambda beta protein facilitates single-strand annealing crucial for Red-mediated recombination.
- This protein binds DNA intermediates during annealing.
Purpose of the Study:
- To characterize the domain structure of beta protein.
- To identify DNA binding regions within beta protein.
Main Methods:
- Limited proteolysis to assess domain stability.
- Biotinylation and mass spectrometry to map DNA-binding sites.
Main Results:
- Beta protein has a stable N-terminal core (1-130), a DNA-binding central region (131-177), and a disordered C-terminal tail (178-261).
- DNA binding protects the central region, with key lysine residues involved in binding.
- A fragment of residues 1-177 retains DNA binding and single-strand DNA binding capabilities.
Conclusions:
- A model is proposed where the N-terminal core and central domain bind DNA, while the C-terminal tail remains flexible.
- The N-terminal 177 residues are sufficient for essential DNA binding functions.
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