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Title: Complex pectin metabolism by gut bacteria reveals novel catalytic functions

Abstract

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 in this paper 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.

Authors:
 [1];  [1];  [1];  [1];  [1];  [1];  [1];  [1];  [1];  [1];  [2];  [3];  [4];  [5];  [4];  [6];  [6];  [6];  [6];  [7] more »;  [8];  [3];  [5];  [9];  [1] « less
  1. Newcastle Univ., Newcastle upon Tyne (United Kingdom). Inst. for Cell and Molecular Biosciences
  2. Centre National de la Recherche Scientifique (CNRS), Marseille (France). Architecture et Fonction des Macromolécules Biologiques; Aix-Marseille Univ., Marseille (France)
  3. INRA, Nantes (France). Biopolymères Interactions Assemblages
  4. John Innes Centre Norwich Research Park, Norwich (United Kingdom). Dept. of Biological Chemistry
  5. Univ. of Michigan, Ann Arbor, MI (United States). Medical School, Dept. of Microbiology and Immunology
  6. Univ. of Georgia, Athens, GA (United States). Complex Carbohydrate Research Center
  7. Univ. of York (United Kingdom). Dept. of Chemistry
  8. Lethbridge Research Centre, Lethbridge, AB (Canada)
  9. Centre National de la Recherche Scientifique (CNRS), Marseille (France). Architecture et Fonction des Macromolécules Biologiques; Aix-Marseille Univ., Marseille (France); INRA, Marseille (France); King Abdulaziz Univ., Jeddah (Saudi Arabia). Dept. of Biological Sciences
Publication Date:
Research Org.:
Univ. of Georgia, Athens, GA (United States)
Sponsoring Org.:
USDOE Office of Science (SC), Basic Energy Sciences (BES) (SC-22)
OSTI Identifier:
1473846
Grant/Contract Number:  
FG02-12ER16324; SC0008472
Resource Type:
Accepted Manuscript
Journal Name:
Nature (London)
Additional Journal Information:
Journal Name: Nature (London); Journal Volume: 544; Journal Issue: 7648; Journal ID: ISSN 0028-0836
Publisher:
Nature Publishing Group
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES

Citation Formats

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’Neill, Malcolm A., Urbanowicz, Breeanna R., York, William S., Davies, Gideon J., Abbott, D. Wade, Ralet, Marie-Christine, Martens, Eric C., Henrissat, Bernard, and Gilbert, Harry J. Complex pectin metabolism by gut bacteria reveals novel catalytic functions. United States: N. p., 2017. Web. doi:10.1038/nature21725.
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’Neill, Malcolm A., Urbanowicz, Breeanna 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. United States. doi:10.1038/nature21725.
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’Neill, Malcolm A., Urbanowicz, Breeanna R., York, William S., Davies, Gideon J., Abbott, D. Wade, Ralet, Marie-Christine, Martens, Eric C., Henrissat, Bernard, and Gilbert, Harry J. Thu . "Complex pectin metabolism by gut bacteria reveals novel catalytic functions". United States. doi:10.1038/nature21725. https://www.osti.gov/servlets/purl/1473846.
@article{osti_1473846,
title = {Complex pectin metabolism by gut bacteria reveals novel catalytic functions},
author = {Ndeh, Didier and Rogowski, Artur and Cartmell, Alan and Luis, Ana S. and Baslé, Arnaud and Gray, Joseph and Venditto, Immacolata and Briggs, Jonathon and Zhang, Xiaoyang and Labourel, Aurore and Terrapon, Nicolas and Buffetto, Fanny and Nepogodiev, Sergey and Xiao, Yao and Field, Robert A. and Zhu, Yanping and O’Neill, Malcolm A. and Urbanowicz, Breeanna R. and York, William S. and Davies, Gideon J. and Abbott, D. Wade and Ralet, Marie-Christine and Martens, Eric C. and Henrissat, Bernard and Gilbert, Harry J.},
abstractNote = {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 in this paper 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.},
doi = {10.1038/nature21725},
journal = {Nature (London)},
number = 7648,
volume = 544,
place = {United States},
year = {2017},
month = {4}
}

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Works referenced in this record:

Coot model-building tools for molecular graphics
journal, November 2004

  • Emsley, Paul; Cowtan, Kevin
  • Acta Crystallographica Section D Biological Crystallography, Vol. 60, Issue 12, p. 2126-2132
  • DOI: 10.1107/S0907444904019158

MOLREP an Automated Program for Molecular Replacement
journal, December 1997