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Title: Functional responses of methanogenic archaea to syntrophic growth

Journal Article · · The ISME Journal
 [1];  [2];  [2];  [2];  [3];  [4];  [2];  [5];  [2];  [4];  [3];  [2];  [2];  [5]
  1. Univ. of Washington, Seattle, WA (United States). Dept. of Civil and Environmental Engineering; Geosyntec Consultants, Seattle, WA (United States); DOE/OSTI
  2. Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States). Physical Biosciences Division
  3. Univ. of Oklahoma, Norman, OK (United States). Dept. of Botany and Microbiology
  4. Univ. of Washington, Seattle, WA (United States). Dept. of Microbiology
  5. Univ. of Washington, Seattle, WA (United States). Dept. of Civil and Environmental Engineering

Methanococcus maripaludis grown syntrophically with Desulfovibrio vulgaris was compared with M. maripaludis monocultures grown under hydrogen limitation using transcriptional, proteomic and metabolite analyses. These measurements indicate a decrease in transcript abundance for energyconsuming biosynthetic functions in syntrophically grown M. maripaludis, with an increase in transcript abundance for genes involved in the energy-generating central pathway for methanogenesis. Compared with growth in monoculture under hydrogen limitation, the response of paralogous genes, such as those coding for hydrogenases, often diverged, with transcripts of one variant increasing in relative abundance, whereas the other was little changed or significantly decreased in abundance. A common theme was an apparent increase in transcripts for functions using H2 directly as reductant, versus those using the reduced deazaflavin (coenzyme F420). The greater importance of direct reduction by H2 was supported by improved syntrophic growth of a deletion mutant in an F420-dependent dehydrogenase of M. maripaludis. These data suggest that paralogous genes enable the methanogen to adapt to changing substrate availability, sustaining it under environmental conditions that are often near the thermodynamic threshold for growth. Additionally, the discovery of interspecies alanine transfer adds another metabolic dimension to this environmentally relevant mutualism

Research Organization:
Lawrence Berkeley National Laboratory (LBNL), Berkeley, CA (United States)
Sponsoring Organization:
USDOE Office of Science (SC), Biological and Environmental Research (BER). Biological Systems Science Division
Grant/Contract Number:
AC02-05CH11231
OSTI ID:
1623762
Journal Information:
The ISME Journal, Journal Name: The ISME Journal Journal Issue: 11 Vol. 6; ISSN 1751-7362
Publisher:
Nature Publishing GroupCopyright Statement
Country of Publication:
United States
Language:
English

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