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Complex pectin metabolism by gut bacteria reveals novel catalytic functions
Carbohydrate polymers drive microbial diversity in the human gut microbiota. It is unclear, however, whether bacterial consortia or single organisms are required to depolymerize highly complex glycans. Here we show that the gut bacterium Bacteroides thetaiotaomicron utilizes the most structurally co...
Autores principales: | , , , , , , , , , , , , , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5388186/ https://www.ncbi.nlm.nih.gov/pubmed/28329766 http://dx.doi.org/10.1038/nature21725 |
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author | Ndeh, Didier Rogowski, Artur Cartmell, Alan Luis, Ana S. Baslé, Arnaud Gray, Joseph Venditto, Immacolata Briggs, Jonathon Zhang, Xiaoyang Labourel, Aurore Terrapon, Nicolas Buffetto, Fanny Nepogodiev, Sergey Xiao, Yao Field, Robert A. Zhu, Yanping O’Neil, Malcolm A. Urbanowicz, Breeana R. York, William S. Davies, Gideon J. Abbott, D. Wade Ralet, Marie-Christine Martens, Eric C. Henrissat, Bernard Gilbert, Harry J. |
author_facet | Ndeh, Didier Rogowski, Artur Cartmell, Alan Luis, Ana S. Baslé, Arnaud Gray, Joseph Venditto, Immacolata Briggs, Jonathon Zhang, Xiaoyang Labourel, Aurore Terrapon, Nicolas Buffetto, Fanny Nepogodiev, Sergey Xiao, Yao Field, Robert A. Zhu, Yanping O’Neil, Malcolm A. Urbanowicz, Breeana R. York, William S. Davies, Gideon J. Abbott, D. Wade Ralet, Marie-Christine Martens, Eric C. Henrissat, Bernard Gilbert, Harry J. |
author_sort | Ndeh, Didier |
collection | PubMed |
description | Carbohydrate polymers drive microbial diversity in the human gut microbiota. It is unclear, however, whether bacterial consortia or single organisms are required to depolymerize highly complex glycans. Here we show that the gut bacterium Bacteroides thetaiotaomicron utilizes the most structurally complex glycan known; the plant pectic polysaccharide rhamnogalacturonan-II, cleaving all but one of its 21 distinct glycosidic linkages. We show that rhamnogalacturonan-II side-chain and backbone deconstruction are coordinated, to overcome steric constraints, and that degradation reveals previously undiscovered enzyme families and novel catalytic activities. The degradome informs revision of the current structural model of RG-II and highlights how individual gut bacteria orchestrate manifold enzymes to metabolize the most challenging glycans in the human diet. |
format | Online Article Text |
id | pubmed-5388186 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
record_format | MEDLINE/PubMed |
spelling | pubmed-53881862017-09-22 Complex pectin metabolism by gut bacteria reveals novel catalytic functions Ndeh, Didier Rogowski, Artur Cartmell, Alan Luis, Ana S. Baslé, Arnaud Gray, Joseph Venditto, Immacolata Briggs, Jonathon Zhang, Xiaoyang Labourel, Aurore Terrapon, Nicolas Buffetto, Fanny Nepogodiev, Sergey Xiao, Yao Field, Robert A. Zhu, Yanping O’Neil, Malcolm A. Urbanowicz, Breeana R. York, William S. Davies, Gideon J. Abbott, D. Wade Ralet, Marie-Christine Martens, Eric C. Henrissat, Bernard Gilbert, Harry J. Nature Article Carbohydrate polymers drive microbial diversity in the human gut microbiota. It is unclear, however, whether bacterial consortia or single organisms are required to depolymerize highly complex glycans. Here we show that the gut bacterium Bacteroides thetaiotaomicron utilizes the most structurally complex glycan known; the plant pectic polysaccharide rhamnogalacturonan-II, cleaving all but one of its 21 distinct glycosidic linkages. We show that rhamnogalacturonan-II side-chain and backbone deconstruction are coordinated, to overcome steric constraints, and that degradation reveals previously undiscovered enzyme families and novel catalytic activities. The degradome informs revision of the current structural model of RG-II and highlights how individual gut bacteria orchestrate manifold enzymes to metabolize the most challenging glycans in the human diet. 2017-03-22 2017-04-06 /pmc/articles/PMC5388186/ /pubmed/28329766 http://dx.doi.org/10.1038/nature21725 Text en Users may view, print, copy, and download text and data-mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use:http://www.nature.com/authors/editorial_policies/license.html#terms |
spellingShingle | Article Ndeh, Didier Rogowski, Artur Cartmell, Alan Luis, Ana S. Baslé, Arnaud Gray, Joseph Venditto, Immacolata Briggs, Jonathon Zhang, Xiaoyang Labourel, Aurore Terrapon, Nicolas Buffetto, Fanny Nepogodiev, Sergey Xiao, Yao Field, Robert A. Zhu, Yanping O’Neil, Malcolm A. Urbanowicz, Breeana R. York, William S. Davies, Gideon J. Abbott, D. Wade Ralet, Marie-Christine Martens, Eric C. Henrissat, Bernard Gilbert, Harry J. Complex pectin metabolism by gut bacteria reveals novel catalytic functions |
title | Complex pectin metabolism by gut bacteria reveals novel catalytic
functions |
title_full | Complex pectin metabolism by gut bacteria reveals novel catalytic
functions |
title_fullStr | Complex pectin metabolism by gut bacteria reveals novel catalytic
functions |
title_full_unstemmed | Complex pectin metabolism by gut bacteria reveals novel catalytic
functions |
title_short | Complex pectin metabolism by gut bacteria reveals novel catalytic
functions |
title_sort | complex pectin metabolism by gut bacteria reveals novel catalytic
functions |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5388186/ https://www.ncbi.nlm.nih.gov/pubmed/28329766 http://dx.doi.org/10.1038/nature21725 |
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