Comparative analysis of fungal genomes reveals different plant cell wall degrading capacity in fungi

被引:390
作者
Zhao, Zhongtao [1 ,2 ]
Liu, Huiquan [1 ,2 ]
Wang, Chenfang [1 ,2 ]
Xu, Jin-Rong [1 ,2 ,3 ]
机构
[1] Northwest A&F Univ, Coll Plant Protect, NWAFU PU Joint Res Ctr, Yangling 712100, Shaanxi, Peoples R China
[2] Northwest A&F Univ, Coll Plant Protect, State Key Lab Crop Stress Biol Arid Areas, Yangling 712100, Shaanxi, Peoples R China
[3] Purdue Univ, Dept Bot & Plant Pathol, W Lafayette, IN 47907 USA
来源
BMC GENOMICS | 2013年 / 14卷
关键词
Fungi; CAZymes; Glycoside hydrolase; Polysaccharide lyase; Carbohydrate esterase; Pectinase; Cutinase; Lignocellulase; CARBOHYDRATE-ACTIVE ENZYMES; SUBSTRATE-SPECIFICITY; IN-VITRO; DEGRADATION; PATHOGENICITY; DETERMINANTS; INSIGHTS; XYLANASE; CUTINASE;
D O I
10.1186/1471-2164-14-274
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
Background: Fungi produce a variety of carbohydrate activity enzymes (CAZymes) for the degradation of plant polysaccharide materials to facilitate infection and/or gain nutrition. Identifying and comparing CAZymes from fungi with different nutritional modes or infection mechanisms may provide information for better understanding of their life styles and infection models. To date, over hundreds of fungal genomes are publicly available. However, a systematic comparative analysis of fungal CAZymes across the entire fungal kingdom has not been reported. Results: In this study, we systemically identified glycoside hydrolases (GHs), polysaccharide lyases (PLs), carbohydrate esterases (CEs), and glycosyltransferases (GTs) as well as carbohydrate-binding modules (CBMs) in the predicted proteomes of 103 representative fungi from Ascomycota, Basidiomycota, Chytridiomycota, and Zygomycota. Comparative analysis of these CAZymes that play major roles in plant polysaccharide degradation revealed that fungi exhibit tremendous diversity in the number and variety of CAZymes. Among them, some families of GHs and CEs are the most prevalent CAZymes that are distributed in all of the fungi analyzed. Importantly, cellulases of some GH families are present in fungi that are not known to have cellulose-degrading ability. In addition, our results also showed that in general, plant pathogenic fungi have the highest number of CAZymes. Biotrophic fungi tend to have fewer CAZymes than necrotrophic and hemibiotrophic fungi. Pathogens of dicots often contain more pectinases than fungi infecting monocots. Interestingly, besides yeasts, many saprophytic fungi that are highly active in degrading plant biomass contain fewer CAZymes than plant pathogenic fungi. Furthermore, analysis of the gene expression profile of the wheat scab fungus Fusarium graminearum revealed that most of the CAZyme genes related to cell wall degradation were up-regulated during plant infection. Phylogenetic analysis also revealed a complex history of lineage-specific expansions and attritions for the PL1 family. Conclusions: Our study provides insights into the variety and expansion of fungal CAZyme classes and revealed the relationship of CAZyme size and diversity with their nutritional strategy and host specificity.
引用
收藏
页数:15
相关论文
共 56 条
[1]   ProtTest: selection of best-fit models of protein evolution [J].
Abascal, F ;
Zardoya, R ;
Posada, D .
BIOINFORMATICS, 2005, 21 (09) :2104-2105
[2]   PECTIN-DEGRADING ENZYMES AND PLANT-PARASITE INTERACTIONS [J].
ALGHISI, P ;
FAVARON, F .
EUROPEAN JOURNAL OF PLANT PATHOLOGY, 1995, 101 (04) :365-375
[3]   Transcriptional regulation of plant cell wall degradation by filamentous fungi [J].
Aro, N ;
Pakula, T ;
Penttilä, M .
FEMS MICROBIOLOGY REVIEWS, 2005, 29 (04) :719-739
[4]   Evolution, substrate specificity and subfamily classification of glycoside hydrolase family 5 (GH5) [J].
Aspeborg, Henrik ;
Coutinho, Pedro M. ;
Wang, Yang ;
Brumer, Harry, III ;
Henrissat, Bernard .
BMC EVOLUTIONARY BIOLOGY, 2012, 12
[5]   Carbohydrate-active enzymes from the zygomycete fungus Rhizopus oryzae: a highly specialized approach to carbohydrate degradation depicted at genome level [J].
Battaglia, Evy ;
Benoit, Isabelle ;
van den Brink, Joost ;
Wiebenga, Ad ;
Coutinho, Pedro M. ;
Henrissat, Bernard ;
de Vries, Ronald P. .
BMC GENOMICS, 2011, 12
[6]   Mayday - integrative analytics for expression data [J].
Battke, Florian ;
Symons, Stephan ;
Nieselt, Kay .
BMC BIOINFORMATICS, 2010, 11
[7]   Microbial carbohydrate esterases deacetylating plant polysaccharides [J].
Biely, Peter .
BIOTECHNOLOGY ADVANCES, 2012, 30 (06) :1575-1588
[8]   Carbohydrate-binding modules: fine-tuning polysaccharide recognition [J].
Boraston, AB ;
Bolam, DN ;
Gilbert, HJ ;
Davies, GJ .
BIOCHEMICAL JOURNAL, 2004, 382 (03) :769-781
[9]   The Predicted Secretome of the Plant Pathogenic Fungus Fusarium graminearum: A Refined Comparative Analysis [J].
Brown, Neil A. ;
Antoniw, John ;
Hammond-Kosack, Kim E. .
PLOS ONE, 2012, 7 (04)
[10]   Cellulases Dig Deep IN SITU OBSERVATION OF THE MESOSCOPIC STRUCTURAL DYNAMICS OF ENZYMATIC CELLULOSE DEGRADATION [J].
Bubner, Patricia ;
Dohr, Judith ;
Plank, Harald ;
Mayrhofer, Claudia ;
Nidetzky, Bernd .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2012, 287 (04) :2759-2765