Expression and Activity of the BioH Esterase of Biotin Synthesis is Independent of Genome Context

Abstract BioH is an α/β-hydrolase required for synthesis of the pimelate moiety of biotin in diverse bacteria. The bioH gene is found in different genomic contexts. In some cases (e.g., Escherichia coli) the gene is not located within a biotin synthetic operon and its transcription is not coregulate...

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Autores principales:	Xinyun Cao, Lei Zhu, Zhe Hu, John E. Cronan
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/f5ef9fa935814307babedf8dbcec1b9b
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spelling	oai:doaj.org-article:f5ef9fa935814307babedf8dbcec1b9b2021-12-02T11:40:13ZExpression and Activity of the BioH Esterase of Biotin Synthesis is Independent of Genome Context10.1038/s41598-017-01490-02045-2322https://doaj.org/article/f5ef9fa935814307babedf8dbcec1b9b2017-05-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-01490-0https://doaj.org/toc/2045-2322Abstract BioH is an α/β-hydrolase required for synthesis of the pimelate moiety of biotin in diverse bacteria. The bioH gene is found in different genomic contexts. In some cases (e.g., Escherichia coli) the gene is not located within a biotin synthetic operon and its transcription is not coregulated with the other biotin synthesis genes. In other genomes such as Pseudomonas aeruginosa the bioH gene is within a biotin synthesis operon and its transcription is coregulated with the other biotin operon genes. The esterases of pimelate moiety synthesis show remarkable genomic plasticity in that in some biotin operons bioH is replaced by other α/ß hydrolases of diverse sequence. The “wild card” nature of these enzymes led us to compare the paradigm “freestanding” E. coli BioH with the operon-encoded P. aeruginosa BioH. We hypothesized that the operon-encoded BioH might differ in its expression level and/or activity from the freestanding BioH gene. We report this is not the case. The two BioH proteins show remarkably similar hydrolase activities and substrate specificity. Moreover, Pseudomonas aeruginosa BioH is more highly expressed than E. coli BioH. Despite the enzymatic similarities of the two BioH proteins, bioinformatics analysis places the freestanding and operon-encoded BioH proteins into distinct clades.Xinyun CaoLei ZhuZhe HuJohn E. CronanNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-12 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Xinyun Cao Lei Zhu Zhe Hu John E. Cronan Expression and Activity of the BioH Esterase of Biotin Synthesis is Independent of Genome Context
description	Abstract BioH is an α/β-hydrolase required for synthesis of the pimelate moiety of biotin in diverse bacteria. The bioH gene is found in different genomic contexts. In some cases (e.g., Escherichia coli) the gene is not located within a biotin synthetic operon and its transcription is not coregulated with the other biotin synthesis genes. In other genomes such as Pseudomonas aeruginosa the bioH gene is within a biotin synthesis operon and its transcription is coregulated with the other biotin operon genes. The esterases of pimelate moiety synthesis show remarkable genomic plasticity in that in some biotin operons bioH is replaced by other α/ß hydrolases of diverse sequence. The “wild card” nature of these enzymes led us to compare the paradigm “freestanding” E. coli BioH with the operon-encoded P. aeruginosa BioH. We hypothesized that the operon-encoded BioH might differ in its expression level and/or activity from the freestanding BioH gene. We report this is not the case. The two BioH proteins show remarkably similar hydrolase activities and substrate specificity. Moreover, Pseudomonas aeruginosa BioH is more highly expressed than E. coli BioH. Despite the enzymatic similarities of the two BioH proteins, bioinformatics analysis places the freestanding and operon-encoded BioH proteins into distinct clades.
format	article
author	Xinyun Cao Lei Zhu Zhe Hu John E. Cronan
author_facet	Xinyun Cao Lei Zhu Zhe Hu John E. Cronan
author_sort	Xinyun Cao
title	Expression and Activity of the BioH Esterase of Biotin Synthesis is Independent of Genome Context
title_short	Expression and Activity of the BioH Esterase of Biotin Synthesis is Independent of Genome Context
title_full	Expression and Activity of the BioH Esterase of Biotin Synthesis is Independent of Genome Context
title_fullStr	Expression and Activity of the BioH Esterase of Biotin Synthesis is Independent of Genome Context
title_full_unstemmed	Expression and Activity of the BioH Esterase of Biotin Synthesis is Independent of Genome Context
title_sort	expression and activity of the bioh esterase of biotin synthesis is independent of genome context
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/f5ef9fa935814307babedf8dbcec1b9b
work_keys_str_mv	AT xinyuncao expressionandactivityofthebiohesteraseofbiotinsynthesisisindependentofgenomecontext AT leizhu expressionandactivityofthebiohesteraseofbiotinsynthesisisindependentofgenomecontext AT zhehu expressionandactivityofthebiohesteraseofbiotinsynthesisisindependentofgenomecontext AT johnecronan expressionandactivityofthebiohesteraseofbiotinsynthesisisindependentofgenomecontext
_version_	1718395739029110784

Expression and Activity of the BioH Esterase of Biotin Synthesis is Independent of Genome Context

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