Corrigendum: Complex pectin metabolism by gut bacteria reveals novel catalytic functions (Nature (2017) 544 (65-70) DOI: 10.1038/nature21725);Complex pectin metabolism by gut bacteria reveals novel catalytic functions

Nature

Volumn 544, Issue 7648, 2017, Pages 65-70

  Ndeh, Didier ^a   Rogowski, Artur ^a   Cartmell, Alan ^a   Luis, Ana S ^a   Baslé, Arnaud ^a   Gray, Joseph ^a   Venditto, Immacolata ^a   Briggs, Jonathon ^a   Zhang, Xiaoyang ^a   Labourel, Aurore ^a   Terrapon, Nicolas ^b   Buffetto, Fanny ^c,k   Nepogodiev, Sergey ^d   Xiao, Yao ^e   Field, Robert A ^d   Zhu, Yanping ^f   O'Neill, Malcolm A ^f   Urbanowicz, Breeanna R ^f   York, William S ^f   Davies, Gideon J ^g   Abbott, D Wade ^h   Ralet, Marie Christine ^c   Martens, Eric C ^e   Henrissat, Bernard ^b,i,j,k   Gilbert, Harry J ^a,l   more..

^a NEWCASTLE UNIVERSITY   (United Kingdom)

^b AIX MARSEILLE UNIVERSITY   (France)

^c INRA   (France)

^d JOHN INNES CENTRE   (United Kingdom)

^e UNIVERSITY OF MICHIGAN MEDICAL SCHOOL   (United States)

^f UNIVERSITY OF GEORGIA   (United States)

^g UNIVERSITY OF YORK   (United Kingdom)

^h LETHBRIDGE RESEARCH CENTRE   (Canada)

ⁱ CEMAGREF   (France)

^j KING ABDULAZIZ UNIVERSITY   (Saudi Arabia)

^k Megazyme International Ireland Ltd   (Ireland)

^l STELLENBOSCH UNIVERSITY   (South Africa)

more..

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; GALACTURONIC ACID; GLYCAN; GLYCOSIDASE; OLIGOSACCHARIDE; PECTIN; RHAMNOGALACTURONAN II; UNCLASSIFIED DRUG; BORIC ACID;

BACTERIUM; CARBOHYDRATE; CATALYSIS; CHEMICAL PROPERTY; DIGESTIVE SYSTEM; ENZYME; METABOLISM; MICROBIAL COMMUNITY; POLYMER; POLYSACCHARIDE;

ARTICLE; BACTERIAL GROWTH; BACTEROIDES THETAIOTAOMICRON; CATALYSIS; CONFORMATION; CONTROLLED STUDY; CRYSTAL STRUCTURE; DEPOLYMERIZATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME DEGRADATION; ENZYME SPECIFICITY; ESTERIFICATION; HYDROLYSIS; INTESTINE FLORA; MUTAGENESIS; NONHUMAN; POLYMERIZATION; PRIORITY JOURNAL; STEREOCHEMISTRY; STRUCTURAL MODEL; TRANSCRIPTOMICS; UPREGULATION; BIOCATALYSIS; CHEMISTRY; CLASSIFICATION; ENZYMOLOGY; GASTROINTESTINAL TRACT; GROWTH, DEVELOPMENT AND AGING; HUMAN; METABOLISM; MICROBIOLOGY; MOLECULAR MODEL;

BACTERIA (MICROORGANISMS); BACTEROIDES THETAIOTAOMICRON;

BACTEROIDES THETAIOTAOMICRON; BIOCATALYSIS; BORATES; CATALYTIC DOMAIN; GASTROINTESTINAL MICROBIOME; GASTROINTESTINAL TRACT; GLYCOSIDE HYDROLASES; HUMANS; MODELS, MOLECULAR; PECTINS; SUBSTRATE SPECIFICITY;

EID: 85017104564     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature23659     Document Type: Erratum

References (25)

1. Wißing, C. et al. Isotopic evidence for dietary ecology of late Neandertals in North-Western Europe. Quat. Int. 411, 327-345 (2016).
2. Pellerin, P. et al. Structural characterization of red wine rhamnogalacturonan II. Carbohydr. Res. 290, 183-197 (1996).
3. Apolinar-Valiente, R. et al. Polysaccharide composition of Monastrell red wines from four different Spanish terroirs: effect of wine-making techniques. J. Agric. Food Chem. 61, 2538-2547 (2013).
4. Cuskin, F. et al. Human gut Bacteroidetes can utilize yeast mannan through a selfish mechanism. Nature 517, 165-169 (2015).
5. Larsbrink, J. et al. A discrete genetic locus confers xyloglucan metabolism in select human gut Bacteroidetes. Nature 506, 498-502 (2014).
6. Rogowski, A. et al. Glycan complexity dictates microbial resource allocation in the large intestine. Nat. Commun. 6, 7481 (2015).
7. Koropatkin, N. M., Cameron, E. A. & Martens, E. C. How glycan metabolism shapes the human gut microbiota. Nat. Rev. Microbiol. 10, 323-335 (2012).
8. Martens, E. C. et al. Recognition and degradation of plant cell wall polysaccharides by two human gut symbionts. PLoS Biol. 9, e1001221 (2011).
9. Amaya, M. F. et al. Structural insights into the catalytic mechanism of Trypanosoma cruzi trans-sialidase. Structure 12, 775-784 (2004).
10. Lombard, V., Golaconda Ramulu, H., Drula, E., Coutinho, P. M. & Henrissat, B. The carbohydrate-Active enzymes database (CAZy) in 2013. Nucleic Acids Res. 42, D490-D495 (2014).
11. Davis, B. G. et al. Tetrazoles of manno-And rhamno-pyranoses: Contrasting inhibition of mannosidases by 4.3.0 but of rhamnosidase by 3.3.0 bicyclic tetrazoles. Tetrahedron 55, 4489-4500 (1999).
12. Speciale, G., Thompson, A. J., Davies, G. J. & Williams, S. J. Dissecting conformational contributions to glycosidase catalysis and inhibition. Curr. Opin. Struct. Biol. 28, 1-13 (2014).
13. Fujita, K. et al. Molecular cloning and characterization of a β-l-Arabinobiosidase in Bifidobacterium longum that belongs to a novel glycoside hydrolase family. J. Biol. Chem. 286, 5143-5150 (2011).
14. Spellman, M. W., McNeil, M., Darvill, A. G., Albersheim, P. & Henrick, K. Isolation and characterization of 3-C-carboxy-5-deoxy-l-xylose, a naturally occurring, branched-chain, acidic monosaccharide. Carbohydr. Res. 122, 115-129 (1983).
15. Guérardel, Y. et al. The nematode Caenorhabditis elegans synthesizes unusual O-linked glycans: identification of glucose-substituted mucin-Type O-glycans and short chondroitin-like oligosaccharides. Biochem. J. 357, 167-182 (2001).
16. Russa, R., Urbanik-Sypniewska, T., Choma, A. & Mayer, H. Identification of 3-deoxy-lyxo-2-heptulosaric acid in the core region of lipopolysaccharides from Rhizobiaceae. FEMS Microbiol. Lett. 84, 337-343 (1991).
17. Nagae, M. et al. Structural basis of the catalytic reaction mechanism of novel 1, 2-α-l-fucosidase from Bifidobacterium bifidum. J. Biol. Chem. 282, 18497-18509 (2007).
18. Sulzenbacher, G. et al. Crystal structure of Thermotoga maritima α-l-fucosidase. Insights into the catalytic mechanism and the molecular basis for fucosidosis. J. Biol. Chem. 279, 13119-13128 (2004).
19. ONeill, M. A., Ishii, T., Albersheim, P. & Darvill, A. G. Rhamnogalacturonan II: structure and function of a borate cross-linked cell wall pectic polysaccharide. Annu. Rev. Plant Biol. 55, 109-139 (2004).
20. Pabst, M. et al. Rhamnogalacturonan II structure shows variation in the side chains monosaccharide composition and methylation status within and across different plant species. Plant J. 76, 61-72 (2013).
21. Cartmell, A. et al. The structure and function of an arabinan-specific α-1, 2-Arabinofuranosidase identified from screening the activities of bacterial GH43 glycoside hydrolases. J. Biol. Chem. 286, 15483-15495 (2011).
22. Glenwright, A. J. et al. Structural basis for nutrient acquisition by dominant members of the human gut microbiota. Nature 541, 407-411 (2017).
23. Bourlard, T., Pellerin, P. & Morvan, C. Rhamnogalacturonans I and II are pectic substrates for flax-cell methyltransferases. Plant Physiol. Biochem. 35, 623-629 (1997).
24. Glushka, J. N. et al. Primary structure of the 2-O-methyl-α-l-fucose-containing side chain of the pectic polysaccharide, rhamnogalacturonan II. Carbohydr. Res. 338, 341-352 (2003).
25. Raman, R. et al. Advancing glycomics: implementation strategies at the Consortium for Functional Glycomics. Glycobiology 16, 82R-90R (2006).