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Complex pectin metabolism by gut bacteria reveals novel catalytic functions

by Field, Robert A , Architecture et fonction des macromolécules biologiques (AFMB) ; Institut National de la Recherche Agronomique (INRA)-Aix Marseille Université (AMU)-Centre National de la Recherche Scientifique (CNRS) , Ralet-Renard, Marie-Christine , O'Neill, Malcolm A , Centre National de la Recherche Scientifique (CNRS) , Urbanowicz, Breeanna R , Unité de recherche sur les Biopolymères, Interactions Assemblages (BIA) ; Institut National de la Recherche Agronomique (INRA) , Buffetto, Fanny , Labourel, Aurore , Institute for Cell and Molecular Biosciences ; Newcastle University [Newcastle] , Complex Carbohydrate Research Center ; University of Georgia [USA] , Cartmell, Alan , Megazyme International , Nepogodiev, Sergey , Henrissat, Bernard , Department of Chemistry ; RIDER UNIVERSITY , Zhu, Yanping , York, William S , ANR 12-BIME-0006-01/ BB/K020358/1 BB/K001949/1 /Wellcome Trust WT097907MA / DE-FG02-12ER16324 / Marie Sklodowska-Curie 707922/ Beef and Cattle Research Council FDE.15.13 , Briggs, Jonathon , Zhang, Xiaoyang , Department of Microbio

in 631/326 / 631/45/221 / 82 / 82/83 / Acids / Analysis / Bacteroides thetaiotaomicron - enzymology / Bacteroides thetaiotaomicron - growth & development / Bacteroides thetaiotaomicron - metabolism / BASIC BIOLOGICAL SCIENCES / Biocatalysis / Borates - chemistry / Borates - metabolism / Catalysis / Catalytic Domain / Crystal structure / Enzymes / Gastrointestinal Microbiome / Gastrointestinal Tract - microbiology / Glycoside Hydrolases - chemistry / Glycoside Hydrolases - classification / Glycoside Hydrolases - metabolism / Humanities and Social Sciences / Humans / Life Sciences / Microbiota (Symbiotic organisms) / Models, Molecular / multidisciplinary / Mutagenesis / Pectin / Pectins - chemistry / Pectins - metabolism / Physiological aspects / Science / Studies / Substrate Specificity / Vegetal Biology

2017

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2017

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2017

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Journal Article

Complex pectin metabolism by gut bacteria reveals novel catalytic functions

Field, Robert A,

Architecture et fonction des macromolécules biologiques (AFMB) ; Institut National de la Recherche Agronomique (INRA)-Aix Marseille Université (AMU)-Centre National de la Recherche Scientifique (CNRS),

Ralet-Renard, Marie-Christine,

O'Neill, Malcolm A,

Centre National de la Recherche Scientifique (CNRS),

Urbanowicz, Breeanna R,

Unité de recherche sur les Biopolymères, Interactions Assemblages (BIA) ; Institut National de la Recherche Agronomique (INRA),

Buffetto, Fanny,

Labourel, Aurore,

Institute for Cell and Molecular Biosciences ; Newcastle University [Newcastle],

Complex Carbohydrate Research Center ; University of Georgia [USA],

Cartmell, Alan,

Megazyme International,

Nepogodiev, Sergey,

Henrissat, Bernard,

Department of Chemistry ; RIDER UNIVERSITY,

Zhu, Yanping,

York, William S,

ANR 12-BIME-0006-01/ BB/K020358/1 BB/K001949/1 /Wellcome Trust WT097907MA / DE-FG02-12ER16324 / Marie Sklodowska-Curie 707922/ Beef and Cattle Research Council FDE.15.13,

Briggs, Jonathon,

Zhang, Xiaoyang,

Department of Microbio

2017

Overview

The metabolism of carbohydrate polymers drives 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 uses the most structurally complex glycan known: the plant pectic polysaccharide rhamnogalacturonan-II, cleaving all but 1 of its 21 distinct glycosidic linkages. The deconstruction of rhamnogalacturonan-II side chains and backbone are coordinated to overcome steric constraints, and the degradation involves previously undiscovered enzyme families and catalytic activities. The degradation system informs revision of the current structural model of rhamnogalacturonan-II and highlights how individual gut bacteria orchestrate manifold enzymes to metabolize the most challenging glycan in the human diet.

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Publisher

Nature Publishing Group,HAL CCSD,Nature Publishing Group UK

Subject

631/326

/ 631/45/221

/ 82

/ 82/83

/ Acids

/ Analysis

/ Bacteroides thetaiotaomicron - enzymology