Plant protein inhibitors of cell wall degrading enzymes

被引:209
作者
Juge, Nathalie [1 ]
机构
[1] Inst Mediterranen Rech Nutr, Fac Sci St Jerome, F-13397 Marseille 20, France
[2] Inst Food Res, Norwich NR4 7UA, Norfolk, England
基金
英国生物技术与生命科学研究理事会;
关键词
D O I
10.1016/j.tplants.2006.05.006
中图分类号
Q94 [植物学];
学科分类号
071001 ;
摘要
Plant cell walls, which consist mainly of polysaccharides (i.e. cellulose, hemicelluloses and pectins), play an important role in defending plants against pathogens. Most phytopathogenic microorganisms secrete an array of cell wall degrading enzymes (CWDEs) capable of depolymerizing the polysaccharides in the plant host wall. In response, plants have evolved a diverse battery of defence responses including protein inhibitors of these enzymes. These include inhibitors of pectin degrading enzymes such as polygalacturonases, pectin-methyl esterases and pectin lyases, and hemicellulose degrading enzymes such as endoxylanases and xyloglucan endoglucanases. The discovery of these plant inhibitors and the recent resolution of their three-dimensional structures, free or in complex with their target enzymes, provide new lines of evidence regarding their function and evolution in plant-pathogen interactions.
引用
收藏
页码:359 / 367
页数:9
相关论文
共 96 条
[1]   Evaluation of tolerance to Pierce's disease and Botrytis in transgenic plants of Vitis vinifera L. expressing the pear PGIP gene [J].
Agüero, CB ;
Uratsu, SL ;
Greve, C ;
Powell, ALT ;
Labavitch, JM ;
Meredith, CP ;
Dandekar, AM .
MOLECULAR PLANT PATHOLOGY, 2005, 6 (01) :43-51
[2]   Molecular cloning of a BcPGIP cDNA from Brassica campestris and its expression to several stresses [J].
Ahsan, N ;
Yoon, HS ;
Jo, J .
PLANT SCIENCE, 2005, 169 (06) :1081-1089
[3]   Sugars and pH: A clue to the regulation of fungal cell wall-degrading enzymes in plants [J].
Akimitsu, K ;
Isshiki, A ;
Ohtani, K ;
Yammoto, H ;
Eshel, D ;
Prusky, D .
PHYSIOLOGICAL AND MOLECULAR PLANT PATHOLOGY, 2004, 65 (06) :271-275
[4]   LePLDβ1 activation and relocalization in suspension-cultured tomato cells treated with xylanase [J].
Bargmann, BOR ;
Laxalt, AM ;
ter Riet, B ;
Schouten, E ;
van Leeuwen, W ;
Dekker, HL ;
de Koster, CG ;
Haring, MA ;
Munnik, T .
PLANT JOURNAL, 2006, 45 (03) :358-368
[5]   Cloning and characterization of two endoxylanases from the cereal phytopathogen Fusarium graminearum and their inhibition profile against endoxylanase inhibitors from wheat [J].
Beliën, T ;
Van Campenhout, S ;
Van Acker, M ;
Volckaert, G .
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 2005, 327 (02) :407-414
[6]   Potential physiological role of plant glycosidase inhibitors [J].
Bellincampi, D ;
Camardella, L ;
Delcour, JA ;
Desseaux, V ;
D'Ovidio, R ;
Durand, A ;
Elliot, G ;
Gebruers, K ;
Giovane, A ;
Juge, N ;
Sórensen, JF ;
Svensson, B ;
Vairo, D .
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS, 2004, 1696 (02) :265-274
[7]   Evolutionary dynamics of plant R-genes [J].
Bergelson, J ;
Kreitman, M ;
Stahl, EA ;
Tian, DC .
SCIENCE, 2001, 292 (5525) :2281-2285
[8]   Directed mutagenesis confirms the functional importance of positively selected sites in polygalacturonase inhibitor protein [J].
Bishop, JG .
MOLECULAR BIOLOGY AND EVOLUTION, 2005, 22 (07) :1531-1534
[9]   Rapid evolution in plant chitinases: Molecular targets of selection in plant-pathogen coevolution [J].
Bishop, JG ;
Dean, AM ;
Mitchell-Olds, T .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2000, 97 (10) :5322-5327
[10]   Pectin methylesterases and pectin dynamics in pollen tubes [J].
Bosch, M ;
Hepler, PK .
PLANT CELL, 2005, 17 (12) :3219-3226