A nitrile hydratase in the eukaryote Monosiga brevicollis.

Bacterial nitrile hydratase (NHases) are important industrial catalysts and waste water remediation tools. In a global computational screening of conventional and metagenomic sequence data for NHases, we detected the two usually separated NHase subunits fused in one protein of the choanoflagellate M...

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Autores principales: Konrad U Foerstner, Tobias Doerks, Jean Muller, Jeroen Raes, Peer Bork
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Publicado: Public Library of Science (PLoS) 2008
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Acceso en línea:https://doaj.org/article/62b2fe4f090045d2815a4ad93584fd57
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spelling oai:doaj.org-article:62b2fe4f090045d2815a4ad93584fd572021-11-25T06:18:07ZA nitrile hydratase in the eukaryote Monosiga brevicollis.1932-620310.1371/journal.pone.0003976https://doaj.org/article/62b2fe4f090045d2815a4ad93584fd572008-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/19096720/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203Bacterial nitrile hydratase (NHases) are important industrial catalysts and waste water remediation tools. In a global computational screening of conventional and metagenomic sequence data for NHases, we detected the two usually separated NHase subunits fused in one protein of the choanoflagellate Monosiga brevicollis, a recently sequenced unicellular model organism from the closest sister group of Metazoa. This is the first time that an NHase is found in eukaryotes and the first time it is observed as a fusion protein. The presence of an intron, subunit fusion and expressed sequence tags covering parts of the gene exclude contamination and suggest a functional gene. Phylogenetic analyses and genomic context imply a probable ancient horizontal gene transfer (HGT) from proteobacteria. The newly discovered NHase might open biotechnological routes due to its unconventional structure, its new type of host and its apparent integration into eukaryotic protein networks.Konrad U FoerstnerTobias DoerksJean MullerJeroen RaesPeer BorkPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 3, Iss 12, p e3976 (2008)
institution DOAJ
collection DOAJ
language EN
topic Medicine
R
Science
Q
spellingShingle Medicine
R
Science
Q
Konrad U Foerstner
Tobias Doerks
Jean Muller
Jeroen Raes
Peer Bork
A nitrile hydratase in the eukaryote Monosiga brevicollis.
description Bacterial nitrile hydratase (NHases) are important industrial catalysts and waste water remediation tools. In a global computational screening of conventional and metagenomic sequence data for NHases, we detected the two usually separated NHase subunits fused in one protein of the choanoflagellate Monosiga brevicollis, a recently sequenced unicellular model organism from the closest sister group of Metazoa. This is the first time that an NHase is found in eukaryotes and the first time it is observed as a fusion protein. The presence of an intron, subunit fusion and expressed sequence tags covering parts of the gene exclude contamination and suggest a functional gene. Phylogenetic analyses and genomic context imply a probable ancient horizontal gene transfer (HGT) from proteobacteria. The newly discovered NHase might open biotechnological routes due to its unconventional structure, its new type of host and its apparent integration into eukaryotic protein networks.
format article
author Konrad U Foerstner
Tobias Doerks
Jean Muller
Jeroen Raes
Peer Bork
author_facet Konrad U Foerstner
Tobias Doerks
Jean Muller
Jeroen Raes
Peer Bork
author_sort Konrad U Foerstner
title A nitrile hydratase in the eukaryote Monosiga brevicollis.
title_short A nitrile hydratase in the eukaryote Monosiga brevicollis.
title_full A nitrile hydratase in the eukaryote Monosiga brevicollis.
title_fullStr A nitrile hydratase in the eukaryote Monosiga brevicollis.
title_full_unstemmed A nitrile hydratase in the eukaryote Monosiga brevicollis.
title_sort nitrile hydratase in the eukaryote monosiga brevicollis.
publisher Public Library of Science (PLoS)
publishDate 2008
url https://doaj.org/article/62b2fe4f090045d2815a4ad93584fd57
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