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Structure and function of the Escherichia coli protein YmgB: a protein critical for biofilm formation and acid-resistance.

Structure and function of the Escherichia coli protein YmgB: a protein critical for biofilm formation and acid-resistance. Research Abstract Details 

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  • Structure and function of the Escherichia coli protein YmgB: a protein critical for biofilm formation and acid-resistance. Abstract Text:

    jintae leeJintae Lee,rebecca pageRebecca Page,rodolfo Rodolfo ,jeanne-marie palerminoJeanne-Marie Palermino,xue-song zhangXue-Song Zhang,ojus doshiOjus Doshi,thomas k woodThomas K Wood,wolfgang petiWolfgang Peti,jintae leeJintae Lee,rebecca pageRebecca Page,rodolfo Rodolfo ,jeanne-marie palerminoJeanne-Marie Palermino,xue-song zhangXue-Song Zhang,ojus doshiOjus Doshi,thomas k woodThomas K Wood,wolfgang petiWolfgang Peti,jintae leeJintae Lee,rebecca pageRebecca Page,rodolfo Rodolfo ,jeanne-marie palerminoJeanne-Marie Palermino,xue-song zhangXue-Song Zhang,ojus doshiOjus Doshi,thomas k woodThomas K Wood,wolfgang petiWolfgang Peti,

    The Escherichia coli gene cluster ymgABC was identified in transcriptome studies to have a role in biofilm development and stability. In this study, we showed that YmgB represses biofilm formation in rich medium containing glucose, decreases cellular motility, and protects the cell from acid indicating that YmgB has a major role in acid-resistance in E. coli. Our data show that these phenotypes are potentially mediated through interactions with the important cell signal indole. In addition, gel mobility-shift assays suggest that YmgB may be a non-specific DNA-binding protein. Using nickel-enrichment DNA microarrays, we showed that YmgB binds, either directly or indirectly, via a probable ligand, genes important for biofilm formation. To advance our understanding of the function of YmgB, we used X-ray crystallography to solve the structure of the protein to 1.8 A resolution. YmgB is a biological dimer that is structurally homologous to the E. coli gene regulatory protein Hha, despite having only 5% sequence identity. This supports our DNA microarray data showing that YmgB is a gene regulatory protein. Therefore, this protein, which clearly has a critical role in acid-resistance in E. coli, has been renamed as AriR for regulator of acid resistance influenced by indole.

    Structure and function of the Escherichia coli protein YmgB: a protein critical for biofilm formation and acid-resistance. Publishing Authors By Initials

    j leeJ Lee,r pageR Page,r R ,jm palerminoJM Palermino,xs zhangXS Zhang,o doshiO Doshi,tk woodTK Wood,w petiW Peti,j leeJ Lee,r pageR Page,r R ,jm palerminoJM Palermino,xs zhangXS Zhang,o doshiO Doshi,tk woodTK Wood,w petiW Peti,j leeJ Lee,r pageR Page,r R ,jm palerminoJM Palermino,xs zhangXS Zhang,o doshiO Doshi,tk woodTK Wood,w petiW Peti,

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    Structure and function of the Escherichia coli protein YmgB: a protein critical for biofilm formation and acid-resistance. Journal Published:

    PUBLICATION TYPE: Research Support, N.I.H., Extr

    Journal: Journal of molecular biology

    VOLUME: 373

    Page Numbers: 11-26

    Journal Abbreviation: J. Mol. Biol.

    ISSN: 0022-2836

    DAY: 2

    MONTH: 08

    YEAR: 2007

    Structure and function of the Escherichia coli protein YmgB: a protein critical for biofilm formation and acid-resistance. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 2985088

    Structure and function of the Escherichia coli protein YmgB: a protein critical for biofilm formation and acid-resistance. Keywords Mesh Terms:

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    Chemical & Substance for Abstract: Structure and function of the Escherichia coli protein YmgB: a protein critical for biofilm formation and acid-resistance. Information

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    Grant and Affiliation Information for Structure and function of the Escherichia coli protein YmgB: a protein critical for biofilm formation and acid-resistance.

    AFFILIATION: Artie McFerrin Department of Chemical Engineering, Texas A & M University, College Station, TX 77843-3122, USA.

    Country: England

    England Research PublicationEngland Research Publication

    AGENCY: United States NIBIB

    GRANT: EB 003872-01A1

    ACRONYM: EB

    MEDLINETA: J Mol Biol

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