Cytochrome c-based domain modularity governs genus-level diversification of electron transfer to dissimilatory nitrite reduction

© 2014 The Authors. Environmental Microbiology published by Society for Applied Microbiology and John Wiley & Sons Ltd. The genus Neisseria contains two pathogenic species (N.meningitidis and N.gonorrhoeae) in addition to a number of commensal species that primarily colonize mucosal surfaces i...

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Main Authors: Finn Erik Aas, Xi Li, James Edwards, Monica Hongrø Solbakken, Manu Deeudom, Åshild Vik, James Moir, Michael Koomey, Marina Aspholm
Format: Journal
Published: 2018
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http://cmuir.cmu.ac.th/jspui/handle/6653943832/54077
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Institution: Chiang Mai University
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spelling th-cmuir.6653943832-540772018-09-04T10:17:13Z Cytochrome c-based domain modularity governs genus-level diversification of electron transfer to dissimilatory nitrite reduction Finn Erik Aas Xi Li James Edwards Monica Hongrø Solbakken Manu Deeudom Åshild Vik James Moir Michael Koomey Marina Aspholm Agricultural and Biological Sciences Immunology and Microbiology © 2014 The Authors. Environmental Microbiology published by Society for Applied Microbiology and John Wiley & Sons Ltd. The genus Neisseria contains two pathogenic species (N.meningitidis and N.gonorrhoeae) in addition to a number of commensal species that primarily colonize mucosal surfaces in man. Within the genus, there is considerable diversity and apparent redundancy in the components involved in respiration. Here, we identify a unique c-type cytochrome (c<inf>N</inf>) that is broadly distributed among commensal Neisseria, but absent in the pathogenic species. Specifically, c<inf>N</inf> supports nitrite reduction in N.gonorrhoeae strains lacking the cytochromes c<inf>5</inf> and CcoP established to be critical to NirK nitrite reductase activity. The c-type cytochrome domain of c<inf>N</inf> shares high sequence identity with those localized c-terminally in c<inf>5</inf> and CcoP and all three domains were shown to donate electrons directly to NirK. Thus, we identify three distinct but paralogous proteins that donate electrons to NirK. We also demonstrate functionality for a N.weaveriiNirK variant with a C-terminal c-type heme extension. Taken together, modular domain distribution and gene rearrangement events related to these respiratory electron carriers within Neisseria are concordant with major transitions in the macroevolutionary history of the genus. This work emphasizes the importance of denitrification as a selectable trait that may influence speciation and adaptive diversification within this largely host-restricted bacterial genus. 2018-09-04T10:07:26Z 2018-09-04T10:07:26Z 2015-01-01 Journal 14622920 14622912 2-s2.0-84931561403 10.1111/1462-2920.12661 https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=84931561403&origin=inward http://cmuir.cmu.ac.th/jspui/handle/6653943832/54077
institution Chiang Mai University
building Chiang Mai University Library
country Thailand
collection CMU Intellectual Repository
topic Agricultural and Biological Sciences
Immunology and Microbiology
spellingShingle Agricultural and Biological Sciences
Immunology and Microbiology
Finn Erik Aas
Xi Li
James Edwards
Monica Hongrø Solbakken
Manu Deeudom
Åshild Vik
James Moir
Michael Koomey
Marina Aspholm
Cytochrome c-based domain modularity governs genus-level diversification of electron transfer to dissimilatory nitrite reduction
description © 2014 The Authors. Environmental Microbiology published by Society for Applied Microbiology and John Wiley & Sons Ltd. The genus Neisseria contains two pathogenic species (N.meningitidis and N.gonorrhoeae) in addition to a number of commensal species that primarily colonize mucosal surfaces in man. Within the genus, there is considerable diversity and apparent redundancy in the components involved in respiration. Here, we identify a unique c-type cytochrome (c<inf>N</inf>) that is broadly distributed among commensal Neisseria, but absent in the pathogenic species. Specifically, c<inf>N</inf> supports nitrite reduction in N.gonorrhoeae strains lacking the cytochromes c<inf>5</inf> and CcoP established to be critical to NirK nitrite reductase activity. The c-type cytochrome domain of c<inf>N</inf> shares high sequence identity with those localized c-terminally in c<inf>5</inf> and CcoP and all three domains were shown to donate electrons directly to NirK. Thus, we identify three distinct but paralogous proteins that donate electrons to NirK. We also demonstrate functionality for a N.weaveriiNirK variant with a C-terminal c-type heme extension. Taken together, modular domain distribution and gene rearrangement events related to these respiratory electron carriers within Neisseria are concordant with major transitions in the macroevolutionary history of the genus. This work emphasizes the importance of denitrification as a selectable trait that may influence speciation and adaptive diversification within this largely host-restricted bacterial genus.
format Journal
author Finn Erik Aas
Xi Li
James Edwards
Monica Hongrø Solbakken
Manu Deeudom
Åshild Vik
James Moir
Michael Koomey
Marina Aspholm
author_facet Finn Erik Aas
Xi Li
James Edwards
Monica Hongrø Solbakken
Manu Deeudom
Åshild Vik
James Moir
Michael Koomey
Marina Aspholm
author_sort Finn Erik Aas
title Cytochrome c-based domain modularity governs genus-level diversification of electron transfer to dissimilatory nitrite reduction
title_short Cytochrome c-based domain modularity governs genus-level diversification of electron transfer to dissimilatory nitrite reduction
title_full Cytochrome c-based domain modularity governs genus-level diversification of electron transfer to dissimilatory nitrite reduction
title_fullStr Cytochrome c-based domain modularity governs genus-level diversification of electron transfer to dissimilatory nitrite reduction
title_full_unstemmed Cytochrome c-based domain modularity governs genus-level diversification of electron transfer to dissimilatory nitrite reduction
title_sort cytochrome c-based domain modularity governs genus-level diversification of electron transfer to dissimilatory nitrite reduction
publishDate 2018
url https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=84931561403&origin=inward
http://cmuir.cmu.ac.th/jspui/handle/6653943832/54077
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