Article: Structural Analysis of a Novel Class of R–M Controller Proteins: C.Csp231I from Citrobacter sp. RFL231
Journal of molecular biology. 2011 June 3, v. 409, no. 2
2011
Abstract: Controller proteins play a key role in the temporal regulation of gene expression in bacterial restriction–modification (R–M) systems and are important mediators of horizontal gene transfer. They form the basis of a highly cooperative, concentration- ... ...
Abstract | Controller proteins play a key role in the temporal regulation of gene expression in bacterial restriction–modification (R–M) systems and are important mediators of horizontal gene transfer. They form the basis of a highly cooperative, concentration-dependent genetic switch involved in both activation and repression of R–M genes. Here we present biophysical, biochemical, and high-resolution structural analysis of a novel class of controller proteins, exemplified by C.Csp231I. In contrast to all previously solved C-protein structures, each protein subunit has two extra helices at the C-terminus, which play a large part in maintaining the dimer interface. The DNA binding site of the protein is also novel, having largely AAAA tracts between the palindromic recognition half-sites, suggesting tight bending of the DNA. The protein structure shows an unusual positively charged surface that could form the basis for wrapping the DNA completely around the C-protein dimer. |
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Keywords | Citrobacter ; DNA ; binding sites ; gene expression regulation ; genes ; horizontal gene transfer ; protein subunits ; proteins |
Language | English |
Dates of publication | 2011-0603 |
Size | p. 177-188. |
Publishing place | Elsevier Ltd |
Document type | Article |
ZDB-ID | 80229-3 |
ISSN | 1089-8638 ; 0022-2836 |
ISSN (online) | 1089-8638 |
ISSN | 0022-2836 |
DOI | 10.1016/j.jmb.2011.03.033 |
Database | NAL-Catalogue (AGRICOLA) |
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