AI Article Synopsis

  • The study examines the sulfate-dependent anaerobic oxidation of methane (AOM) which involves a partnership between archaea and sulfate-reducing bacteria in marine environments.
  • Researchers analyzed the genomes, gene expressions, and structures of three different microbial groups found at varying temperatures: ANME-1a/HotSeep-1 at 60°C, ANME-1a/Seep-SRB2 at 37°C, and ANME-2c/Seep-SRB2 at 20°C.
  • Findings suggest that while all groups express key genes for flagella and cytochromes, ANME-2c shows more complex cytochromes with potential for extracellular functions, indicating that direct electron transfer between species

Article Abstract

The sulfate-dependent, anaerobic oxidation of methane (AOM) is an important sink for methane in marine environments. It is carried out between anaerobic methanotrophic archaea (ANME) and sulfate-reducing bacteria (SRB) living in syntrophic partnership. In this study, we compared the genomes, gene expression patterns and ultrastructures of three phylogenetically different microbial consortia found in hydrocarbon-rich environments under different temperature regimes: ANME-1a/HotSeep-1 (60°C), ANME-1a/Seep-SRB2 (37°C) and ANME-2c/Seep-SRB2 (20°C). All three ANME encode a reverse methanogenesis pathway: ANME-2c encodes all enzymes, while ANME-1a lacks the gene for N5,N10-methylene tetrahydromethanopterin reductase (mer) and encodes a methylenetetrahydrofolate reductase (Met). The bacterial partners contain the genes encoding the canonical dissimilatory sulfate reduction pathway. During AOM, all three consortia types highly expressed genes encoding for the formation of flagella or type IV pili and/or c-type cytochromes, some predicted to be extracellular. ANME-2c expressed potentially extracellular cytochromes with up to 32 hemes, whereas ANME-1a and SRB expressed less complex cytochromes (≤ 8 and ≤ 12 heme respectively). The intercellular space of all consortia showed nanowire-like structures and heme-rich areas. These features are proposed to enable interspecies electron exchange, hence suggesting that direct electron transfer is a common mechanism to sulfate-dependent AOM, and that both partners synthesize molecules to enable it.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5947290PMC
http://dx.doi.org/10.1111/1462-2920.14077DOI Listing

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