Altering substrate chain length specificity of an acylhomoserine lactone synthase in bacterial communication

Gunter Brader, Solveig Sjöblom, Heidi Hyytiäinen, Karen Sims-Huopaniemi, E. Tapio Palva

    Tutkimustuotos: ArtikkelijulkaisuArtikkeliTieteellinenvertaisarvioitu

    Kuvaus

    "Quorum sensing mediated by specific signal compounds (autoinducers) allows bacteria to monitor their cell density and enables a synchronized regulation of target gene sets. The best studied group of autoinducers are the acylhomoserine lactones (AHSLs), which are central to the regulation of virulence in many plant and animal pathogens. Variation of the acyl side chain of the AHSLs underlies the observed species specificity of this communication system. Here we show that even different strains of the plant pathogen Erwinia carotovora employ different dialects of this language and demonstrate the molecular basis for the acyl chain length specificity of distinct AHSL synthases. Under physiological concentrations, only the cognate AHSL with the ""right"" acyl chain is recognized as a signal that will switch on virulence genes. Mutagenesis of the AHSL synthase gene expI(SCC1) identified the changes M127T and F69L as sufficient to effectively alter ExpI(SCC1) (an N-3-oxohexanoyl-L homoserine lactone producer) substrate specificity to that of an N-3-oxooctanoyl-L-homoserine lactone producer. Our data identify critical residues that define the size of the substrate-binding pocket of the AHSL synthase and will help in understanding and manipulating this bacterial language."
    Alkuperäiskielienglanti
    LehtiJournal of Biological Chemistry
    Vuosikerta280
    Numero11
    Sivut10403-10409
    Sivumäärä7
    ISSN0021-9258
    DOI - pysyväislinkit
    TilaJulkaistu - 2005
    OKM-julkaisutyyppiA1 Alkuperäisartikkeli tieteellisessä aikakauslehdessä, vertaisarvioitu

    Tieteenalat

    • 118 Biotieteet

    Lainaa tätä

    Brader, Gunter ; Sjöblom, Solveig ; Hyytiäinen, Heidi ; Sims-Huopaniemi, Karen ; Palva, E. Tapio. / Altering substrate chain length specificity of an acylhomoserine lactone synthase in bacterial communication. Julkaisussa: Journal of Biological Chemistry. 2005 ; Vuosikerta 280, Nro 11. Sivut 10403-10409.
    @article{69299dbb5c83458cb1ed0f2fe6a9de99,
    title = "Altering substrate chain length specificity of an acylhomoserine lactone synthase in bacterial communication",
    abstract = "{"}Quorum sensing mediated by specific signal compounds (autoinducers) allows bacteria to monitor their cell density and enables a synchronized regulation of target gene sets. The best studied group of autoinducers are the acylhomoserine lactones (AHSLs), which are central to the regulation of virulence in many plant and animal pathogens. Variation of the acyl side chain of the AHSLs underlies the observed species specificity of this communication system. Here we show that even different strains of the plant pathogen Erwinia carotovora employ different dialects of this language and demonstrate the molecular basis for the acyl chain length specificity of distinct AHSL synthases. Under physiological concentrations, only the cognate AHSL with the {"}{"}right{"}{"} acyl chain is recognized as a signal that will switch on virulence genes. Mutagenesis of the AHSL synthase gene expI(SCC1) identified the changes M127T and F69L as sufficient to effectively alter ExpI(SCC1) (an N-3-oxohexanoyl-L homoserine lactone producer) substrate specificity to that of an N-3-oxooctanoyl-L-homoserine lactone producer. Our data identify critical residues that define the size of the substrate-binding pocket of the AHSL synthase and will help in understanding and manipulating this bacterial language.{"}",
    keywords = "118 Biological sciences",
    author = "Gunter Brader and Solveig Sj{\"o}blom and Heidi Hyyti{\"a}inen and Karen Sims-Huopaniemi and Palva, {E. Tapio}",
    year = "2005",
    doi = "10.1074/jbc.M408603200",
    language = "English",
    volume = "280",
    pages = "10403--10409",
    journal = "Journal of Biological Chemistry",
    issn = "0021-9258",
    publisher = "American Society for Biochemistry and Molecular Biology",
    number = "11",

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    Altering substrate chain length specificity of an acylhomoserine lactone synthase in bacterial communication. / Brader, Gunter; Sjöblom, Solveig; Hyytiäinen, Heidi; Sims-Huopaniemi, Karen; Palva, E. Tapio.

    julkaisussa: Journal of Biological Chemistry, Vuosikerta 280, Nro 11, 2005, s. 10403-10409.

    Tutkimustuotos: ArtikkelijulkaisuArtikkeliTieteellinenvertaisarvioitu

    TY - JOUR

    T1 - Altering substrate chain length specificity of an acylhomoserine lactone synthase in bacterial communication

    AU - Brader, Gunter

    AU - Sjöblom, Solveig

    AU - Hyytiäinen, Heidi

    AU - Sims-Huopaniemi, Karen

    AU - Palva, E. Tapio

    PY - 2005

    Y1 - 2005

    N2 - "Quorum sensing mediated by specific signal compounds (autoinducers) allows bacteria to monitor their cell density and enables a synchronized regulation of target gene sets. The best studied group of autoinducers are the acylhomoserine lactones (AHSLs), which are central to the regulation of virulence in many plant and animal pathogens. Variation of the acyl side chain of the AHSLs underlies the observed species specificity of this communication system. Here we show that even different strains of the plant pathogen Erwinia carotovora employ different dialects of this language and demonstrate the molecular basis for the acyl chain length specificity of distinct AHSL synthases. Under physiological concentrations, only the cognate AHSL with the ""right"" acyl chain is recognized as a signal that will switch on virulence genes. Mutagenesis of the AHSL synthase gene expI(SCC1) identified the changes M127T and F69L as sufficient to effectively alter ExpI(SCC1) (an N-3-oxohexanoyl-L homoserine lactone producer) substrate specificity to that of an N-3-oxooctanoyl-L-homoserine lactone producer. Our data identify critical residues that define the size of the substrate-binding pocket of the AHSL synthase and will help in understanding and manipulating this bacterial language."

    AB - "Quorum sensing mediated by specific signal compounds (autoinducers) allows bacteria to monitor their cell density and enables a synchronized regulation of target gene sets. The best studied group of autoinducers are the acylhomoserine lactones (AHSLs), which are central to the regulation of virulence in many plant and animal pathogens. Variation of the acyl side chain of the AHSLs underlies the observed species specificity of this communication system. Here we show that even different strains of the plant pathogen Erwinia carotovora employ different dialects of this language and demonstrate the molecular basis for the acyl chain length specificity of distinct AHSL synthases. Under physiological concentrations, only the cognate AHSL with the ""right"" acyl chain is recognized as a signal that will switch on virulence genes. Mutagenesis of the AHSL synthase gene expI(SCC1) identified the changes M127T and F69L as sufficient to effectively alter ExpI(SCC1) (an N-3-oxohexanoyl-L homoserine lactone producer) substrate specificity to that of an N-3-oxooctanoyl-L-homoserine lactone producer. Our data identify critical residues that define the size of the substrate-binding pocket of the AHSL synthase and will help in understanding and manipulating this bacterial language."

    KW - 118 Biological sciences

    U2 - 10.1074/jbc.M408603200

    DO - 10.1074/jbc.M408603200

    M3 - Article

    VL - 280

    SP - 10403

    EP - 10409

    JO - Journal of Biological Chemistry

    JF - Journal of Biological Chemistry

    SN - 0021-9258

    IS - 11

    ER -