Cargando…

Gene expression and ultrastructure of meso‐ and thermophilic methanotrophic consortia

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 ex...

Descripción completa

Detalles Bibliográficos
Autores principales: Krukenberg, Viola, Riedel, Dietmar, Gruber‐Vodicka, Harald R., Buttigieg, Pier Luigi, Tegetmeyer, Halina E., Boetius, Antje, Wegener, Gunter
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5947290/
https://www.ncbi.nlm.nih.gov/pubmed/29468803
http://dx.doi.org/10.1111/1462-2920.14077
_version_ 1783322341858607104
author Krukenberg, Viola
Riedel, Dietmar
Gruber‐Vodicka, Harald R.
Buttigieg, Pier Luigi
Tegetmeyer, Halina E.
Boetius, Antje
Wegener, Gunter
author_facet Krukenberg, Viola
Riedel, Dietmar
Gruber‐Vodicka, Harald R.
Buttigieg, Pier Luigi
Tegetmeyer, Halina E.
Boetius, Antje
Wegener, Gunter
author_sort Krukenberg, Viola
collection PubMed
description 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.
format Online
Article
Text
id pubmed-5947290
institution National Center for Biotechnology Information
language English
publishDate 2018
publisher John Wiley and Sons Inc.
record_format MEDLINE/PubMed
spelling pubmed-59472902018-05-17 Gene expression and ultrastructure of meso‐ and thermophilic methanotrophic consortia Krukenberg, Viola Riedel, Dietmar Gruber‐Vodicka, Harald R. Buttigieg, Pier Luigi Tegetmeyer, Halina E. Boetius, Antje Wegener, Gunter Environ Microbiol Research Articles 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. John Wiley and Sons Inc. 2018-04-11 2018-05 /pmc/articles/PMC5947290/ /pubmed/29468803 http://dx.doi.org/10.1111/1462-2920.14077 Text en © 2018 The Authors. Environmental Microbiology published by Society for Applied Microbiology and John Wiley & Sons Ltd This is an open access article under the terms of the http://creativecommons.org/licenses/by-nc/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited and is not used for commercial purposes.
spellingShingle Research Articles
Krukenberg, Viola
Riedel, Dietmar
Gruber‐Vodicka, Harald R.
Buttigieg, Pier Luigi
Tegetmeyer, Halina E.
Boetius, Antje
Wegener, Gunter
Gene expression and ultrastructure of meso‐ and thermophilic methanotrophic consortia
title Gene expression and ultrastructure of meso‐ and thermophilic methanotrophic consortia
title_full Gene expression and ultrastructure of meso‐ and thermophilic methanotrophic consortia
title_fullStr Gene expression and ultrastructure of meso‐ and thermophilic methanotrophic consortia
title_full_unstemmed Gene expression and ultrastructure of meso‐ and thermophilic methanotrophic consortia
title_short Gene expression and ultrastructure of meso‐ and thermophilic methanotrophic consortia
title_sort gene expression and ultrastructure of meso‐ and thermophilic methanotrophic consortia
topic Research Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5947290/
https://www.ncbi.nlm.nih.gov/pubmed/29468803
http://dx.doi.org/10.1111/1462-2920.14077
work_keys_str_mv AT krukenbergviola geneexpressionandultrastructureofmesoandthermophilicmethanotrophicconsortia
AT riedeldietmar geneexpressionandultrastructureofmesoandthermophilicmethanotrophicconsortia
AT grubervodickaharaldr geneexpressionandultrastructureofmesoandthermophilicmethanotrophicconsortia
AT buttigiegpierluigi geneexpressionandultrastructureofmesoandthermophilicmethanotrophicconsortia
AT tegetmeyerhalinae geneexpressionandultrastructureofmesoandthermophilicmethanotrophicconsortia
AT boetiusantje geneexpressionandultrastructureofmesoandthermophilicmethanotrophicconsortia
AT wegenergunter geneexpressionandultrastructureofmesoandthermophilicmethanotrophicconsortia