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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: Foerstner, Konrad U., Doerks, Tobias, Muller, Jean, Raes, Jeroen, Bork, Peer
Formato: Texto
Lenguaje:English
Publicado: Public Library of Science 2008
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2603476/
https://www.ncbi.nlm.nih.gov/pubmed/19096720
http://dx.doi.org/10.1371/journal.pone.0003976
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author Foerstner, Konrad U.
Doerks, Tobias
Muller, Jean
Raes, Jeroen
Bork, Peer
author_facet Foerstner, Konrad U.
Doerks, Tobias
Muller, Jean
Raes, Jeroen
Bork, Peer
author_sort Foerstner, Konrad U.
collection PubMed
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.
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spelling pubmed-26034762008-12-19 A Nitrile Hydratase in the Eukaryote Monosiga brevicollis Foerstner, Konrad U. Doerks, Tobias Muller, Jean Raes, Jeroen Bork, Peer PLoS One Research Article 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. Public Library of Science 2008-12-19 /pmc/articles/PMC2603476/ /pubmed/19096720 http://dx.doi.org/10.1371/journal.pone.0003976 Text en Foerstner et al. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
spellingShingle Research Article
Foerstner, Konrad U.
Doerks, Tobias
Muller, Jean
Raes, Jeroen
Bork, Peer
A Nitrile Hydratase in the Eukaryote Monosiga brevicollis
title 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_short A Nitrile Hydratase in the Eukaryote Monosiga brevicollis
title_sort nitrile hydratase in the eukaryote monosiga brevicollis
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2603476/
https://www.ncbi.nlm.nih.gov/pubmed/19096720
http://dx.doi.org/10.1371/journal.pone.0003976
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