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Expression and Activity of the BioH Esterase of Biotin Synthesis is Independent of Genome Context
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 th...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5438404/ https://www.ncbi.nlm.nih.gov/pubmed/28526858 http://dx.doi.org/10.1038/s41598-017-01490-0 |
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author | Cao, Xinyun Zhu, Lei Hu, Zhe Cronan, John E. |
author_facet | Cao, Xinyun Zhu, Lei Hu, Zhe Cronan, John E. |
author_sort | Cao, Xinyun |
collection | PubMed |
description | 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 | Online Article Text |
id | pubmed-5438404 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-54384042017-05-22 Expression and Activity of the BioH Esterase of Biotin Synthesis is Independent of Genome Context Cao, Xinyun Zhu, Lei Hu, Zhe Cronan, John E. Sci Rep Article 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. Nature Publishing Group UK 2017-05-19 /pmc/articles/PMC5438404/ /pubmed/28526858 http://dx.doi.org/10.1038/s41598-017-01490-0 Text en © The Author(s) 2017 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Cao, Xinyun Zhu, Lei Hu, Zhe Cronan, John E. Expression and Activity of the BioH Esterase of Biotin Synthesis is Independent of Genome Context |
title | 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_short | 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 |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5438404/ https://www.ncbi.nlm.nih.gov/pubmed/28526858 http://dx.doi.org/10.1038/s41598-017-01490-0 |
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