4.6 Article

The dddP gene, encoding a novel enzyme that converts dimethylsulfoniopropionate into dimethyl sulfide, is widespread in ocean metagenomes and marine bacteria and also occurs in some Ascomycete fungi

Journal

ENVIRONMENTAL MICROBIOLOGY
Volume 11, Issue 6, Pages 1376-1385

Publisher

WILEY
DOI: 10.1111/j.1462-2920.2009.01864.x

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Funding

  1. BBSRC
  2. NERC
  3. Biotechnology and Biological Sciences Research Council [BBS/E/J/00000606] Funding Source: researchfish
  4. Natural Environment Research Council [NE/E018033/1] Funding Source: researchfish
  5. NERC [NE/E018033/1] Funding Source: UKRI

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The marine alphaproteobacterium Roseovarius nubinhibens ISM can produce the gas dimethyl sulfide (DMS) from dimethylsulfoniopropionate (DMSP), a widespread secondary metabolite that occurs in many phytoplankton. Roseovarius possesses a novel gene, termed dddP, which when cloned, confers on Escherichia coli the ability to produce DMS. The DddP polypeptide is in the large family of M24 metallopeptidases and is wholly different from two other enzymes, DddD and DddL, which were previously shown to generate DMS from dimethylsulfoniopropionate. Close homologues of DddP occur in other alphaproteobacteria and more surprisingly, in some Ascomycete fungi. These were the biotechnologically important Aspergillus oryzae and the plant pathogen, Fusarium graminearum. The dddP gene is abundant in the bacterial metagenomic sequences in the Global Ocean Sampling Expedition. Thus, dddP has several novel features and is widely dispersed, both taxonomically and geographically.

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