Genome analyses highlight the different biological roles of cellulases

被引:171
作者
Medie, Felix Mba [1 ,2 ]
Davies, Gideon J. [3 ]
Drancourt, Michel [2 ]
Henrissat, Bernard [1 ]
机构
[1] Aix Marseille Univ, CNRS, F-13288 Marseille, France
[2] Aix Marseille Univ, Unit Rech Malad Infecti & Trop Emergentes, CNRS, Inst Rech Dev,Fac Med, F-13005 Marseille, France
[3] Univ York, Dept Chem, York Struct Biol Lab, York YO10 5DD, N Yorkshire, England
基金
英国生物技术与生命科学研究理事会;
关键词
HYDROGEN-BONDING SYSTEM; SYNCHROTRON X-RAY; MYCOBACTERIUM-TUBERCULOSIS; CRYSTAL-STRUCTURE; CELLULOSE SYNTHESIS; WALL; ENDO-1,4-BETA-D-GLUCANASE; CLASSIFICATION; DEGRADATION; INSIGHTS;
D O I
10.1038/nrmicro2729
中图分类号
Q93 [微生物学];
学科分类号
071005 [微生物学];
摘要
Cellulolytic enzymes have been the subject of renewed interest owing to their potential role in the conversion of plant lignocellulose to sustainable biofuels. An analysis of similar to 1,500 complete bacterial genomes, presented here, reveals that similar to 40% of the genomes of sequenced bacteria encode at least one cellulase gene. Most of the bacteria that encode cellulases are soil and marine saprophytes, many of which encode a range of enzymes for cellulose hydrolysis and also for the breakdown of the other constituents of plant cell walls (hemicelluloses and pectins). Intriguingly, cellulases are present in organisms that are usually considered as non-saprophytic, such as Mycobacterium tuberculosis, Legionella pneumophila, Yersinia pestis and even Escherichia coli. We also discuss newly emerging roles of cellulases in such non-saprophytic organisms.
引用
收藏
页码:227 / U
页数:8
相关论文
共 47 条
[1]
Vibrio cholerae O139 requires neither capsule nor LPS O side chain to grow inside Acanthamoeba castellanii [J].
Abd, Hadi ;
Saeed, Amir ;
Weintraub, Andrej ;
Sandstrom, Gunnar .
JOURNAL OF MEDICAL MICROBIOLOGY, 2009, 58 (01) :125-131
[2]
Direct photosynthetic recycling of carbon dioxide to isobutyraldehyde [J].
Atsumi, Shota ;
Higashide, Wendy ;
Liao, James C. .
NATURE BIOTECHNOLOGY, 2009, 27 (12) :1177-U142
[3]
The Carbohydrate-Active EnZymes database (CAZy): an expert resource for Glycogenomics [J].
Cantarel, Brandi L. ;
Coutinho, Pedro M. ;
Rancurel, Corinne ;
Bernard, Thomas ;
Lombard, Vincent ;
Henrissat, Bernard .
NUCLEIC ACIDS RESEARCH, 2009, 37 :D233-D238
[4]
Ultrastructure of cyst differentiation in parasitic protozoa [J].
Chavez-Munguia, Bibiana ;
Omana-Molina, Maritza ;
Gonzalez-Lazaro, Monica ;
Gonzalez-Robles, Arturo ;
Cedillo-Rivera, Roberto ;
Bonilla, Patricia ;
Martinez-Palomo, Adolfo .
PARASITOLOGY RESEARCH, 2007, 100 (06) :1169-1175
[5]
Mycobacterium tuberculosis Uses Host Triacylglycerol to Accumulate Lipid Droplets and Acquires a Dormancy-Like Phenotype in Lipid-Loaded Macrophages [J].
Daniel, Jaiyanth ;
Maamar, Hedia ;
Deb, Chirajyoti ;
Sirakova, Tatiana D. ;
Kolattukudy, Pappachan E. .
PLOS PATHOGENS, 2011, 7 (06)
[6]
Structures of oligosaccharide-bound forms of the endoglucanase V from Humicola insolens at 1.9 angstrom resolution [J].
Davies, GJ ;
Tolley, SP ;
Henrissat, B ;
Hjort, C ;
Schulein, M .
BIOCHEMISTRY, 1995, 34 (49) :16210-16220
[7]
Cellulosomes: Plant-cell-wall-degrading enzyme complexes [J].
Doi, RH ;
Kosugi, A .
NATURE REVIEWS MICROBIOLOGY, 2004, 2 (07) :541-551
[8]
Cleavage of cellulose by a CBM33 protein [J].
Forsberg, Zarah ;
Vaaje-Kolstad, Gustav ;
Westereng, Bjorge ;
Bunaes, Anne C. ;
Stenstrom, Yngve ;
MacKenzie, Alasdair ;
Sorlie, Morten ;
Horn, Svein J. ;
Eijsink, Vincent G. H. .
PROTEIN SCIENCE, 2011, 20 (09) :1479-1483
[9]
Regulation of antigen presentation by Mycobacterium tuberculosis: a role for Toll-like receptors [J].
Harding, Clifford V. ;
Boom, W. Henry .
NATURE REVIEWS MICROBIOLOGY, 2010, 8 (04) :296-307
[10]
Stimulation of Lignocellulosic Biomass Hydrolysis by Proteins of Glycoside Hydrolase Family 61: Structure and Function of a Large, Enigmatic Family [J].
Harris, Paul V. ;
Welner, Ditte ;
McFarland, K. C. ;
Re, Edward ;
Poulsen, Jens-Christian Navarro ;
Brown, Kimberly ;
Salbo, Rune ;
Ding, Hanshu ;
Vlasenko, Elena ;
Merino, Sandy ;
Xu, Feng ;
Cherry, Joel ;
Larsen, Sine ;
Lo Leggio, Leila .
BIOCHEMISTRY, 2010, 49 (15) :3305-3316