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  1. Artikel: Structural Analysis of a Novel Class of R–M Controller Proteins: C.Csp231I from Citrobacter sp. RFL231

    McGeehan, J.E / Streeter, S.D / Thresh, S.-J / Taylor, J.E.N / Shevtsov, M.B / Kneale, G.G

    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.
    Schlagwörter Citrobacter ; DNA ; binding sites ; gene expression regulation ; genes ; horizontal gene transfer ; protein subunits ; proteins
    Sprache Englisch
    Erscheinungsverlauf 2011-0603
    Umfang p. 177-188.
    Erscheinungsort Elsevier Ltd
    Dokumenttyp Artikel
    ZDB-ID 80229-3
    ISSN 1089-8638 ; 0022-2836
    ISSN (online) 1089-8638
    ISSN 0022-2836
    DOI 10.1016/j.jmb.2011.03.033
    Datenquelle NAL Katalog (AGRICOLA)

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  2. Artikel: Structural Analysis of a Novel Class of R–M Controller Proteins: C.Csp231I from Citrobacter sp. RFL231

    McGeehan, J.E. / Streeter, S.D. / Thresh, S.-J. / Taylor, J.E.N. / Shevtsov, M.B. / Kneale, G.G.

    Journal of molecular biology

    Band v. 409,, Heft no. 2

    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.
    Schlagwörter genes ; binding sites ; Citrobacter ; DNA ; horizontal gene transfer ; proteins ; protein subunits ; gene expression regulation
    Sprache Englisch
    Dokumenttyp Artikel
    ISSN 0022-2836
    Datenquelle AGRIS - International Information System for the Agricultural Sciences and Technology

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    Dieser Service ist kostenpflichtig (siehe Lieferbedingungen von subito). Bestellungen, die einen Artikel nebst Supplementary Material umfassen, werden grundsätzlich wie mehrfache Bestellungen bearbeitet. Gebühren fallen in diesen Fällen für jede einzelne Bestellung an.

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