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Published on: December 12, 2017
Structural analysis of a novel class of R-M controller proteins: C.Csp231I from Citrobacter sp. RFL231
J E McGeehan1, S D Streeter, S-J Thresh
1Biophysics Laboratories, Institute of Biomedical and Biomolecular Sciences, School of Biological Sciences, University of Portsmouth, Portsmouth PO1 2DY, UK. john.mcgeehan@port.ac.uk
This study reveals a novel class of bacterial controller proteins, C.Csp231I, with unique structural features. These proteins utilize unusual DNA binding sites and C-terminal helices, impacting gene regulation and horizontal gene transfer.
Area of Science:
- Molecular Biology
- Structural Biology
- Bacteriology
Background:
- Controller proteins regulate gene expression in bacterial restriction-modification (R-M) systems.
- These proteins are crucial for horizontal gene transfer and form cooperative genetic switches.
Purpose of the Study:
- To present a detailed analysis of a novel class of controller proteins, using C.Csp231I as an example.
- To elucidate the unique structural and DNA-binding characteristics of these proteins.
Main Methods:
- Biophysical analysis
- Biochemical assays
- High-resolution structural determination
Main Results:
- Identified a novel class of controller proteins (C.Csp231I) with unique C-terminal helices.
- Discovered an unusual DNA binding site characterized by AAAA tracts, suggesting significant DNA bending.
- Observed a positively charged surface potentially involved in complete DNA wrapping around the protein dimer.
Conclusions:
- The novel structural elements of C.Csp231I contribute to its function in DNA binding and regulation.
- These findings offer new insights into the mechanisms of bacterial gene control and horizontal gene transfer.
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