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Methanobactin from methanotrophs: genetics, structure, function and potential applications.
Semrau, Jeremy D; DiSpirito, Alan A; Obulisamy, Parthiba Karthikeyan; Kang-Yun, Christina S.
Afiliação
  • Semrau JD; Department of Civil and Environmental Engineering, University of Michigan, Ann Arbor, MI, USA 48109-2125.
  • DiSpirito AA; Roy J. Carver Department of Biochemistry, Biophysics and Molecular Biology, Iowa State University, Ames, IA, USA 50011.
  • Obulisamy PK; Department of Civil and Environmental Engineering, University of Michigan, Ann Arbor, MI, USA 48109-2125.
  • Kang-Yun CS; Department of Civil and Environmental Engineering, University of Michigan, Ann Arbor, MI, USA 48109-2125.
FEMS Microbiol Lett ; 367(5)2020 03 01.
Article em En | MEDLINE | ID: mdl-32166327
ABSTRACT
Aerobic methane-oxidizing bacteria of the Alphaproteobacteria have been found to express a novel ribosomally synthesized post-translationally modified polypeptide (RiPP) termed methanobactin (MB). The primary function of MB in these microbes appears to be for copper uptake, but MB has been shown to have multiple capabilities, including oxidase, superoxide dismutase and hydrogen peroxide reductase activities, the ability to detoxify mercury species, as well as acting as an antimicrobial agent. Herein, we describe the diversity of known MBs as well as the genetics underlying MB biosynthesis. We further propose based on bioinformatics analyses that some methanotrophs may produce novel forms of MB that have yet to be characterized. We also discuss recent findings documenting that MBs play an important role in controlling copper availability to the broader microbial community, and as a result can strongly affect the activity of microbes that require copper for important enzymatic transformations, e.g. conversion of nitrous oxide to dinitrogen. Finally, we describe procedures for the detection/purification of MB, as well as potential medical and industrial applications of this intriguing RiPP.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Oligopeptídeos / Alphaproteobacteria / Imidazóis / Metano Idioma: En Revista: FEMS Microbiol Lett Ano de publicação: 2020 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Oligopeptídeos / Alphaproteobacteria / Imidazóis / Metano Idioma: En Revista: FEMS Microbiol Lett Ano de publicação: 2020 Tipo de documento: Article