Pathogen elicitor-induced changes in the maize extracellular matrix proteome

被引:90
作者
Chivasa, S
Simon, WJ
Yu, XL
Yalpani, N
Slabas, AR
机构
[1] Univ Durham, Sch Biol & Biomed Sci, Durham DH1 3LE, England
[2] Pioneer HiBred Int Inc, Johnston, IA USA
关键词
dehydrogenase; extracellular matrix; glyceraldehyde-3-phosphate; heat shock protein-82; maize; phosphotyrosine;
D O I
10.1002/pmic.200500047
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
The extracellular matrix is a vital compartment in plants with a prominent role in defence against pathogen attack. Using a maize cell suspension culture system and pathogen elicitors, responses to pathogen attack that are localised to the extracellular matrix were examined by a proteomic approach. Elicitor treatment of cell cultures induced a rapid change in the phosphorylation status of extracellular peroxidases, the apparent disappearance of a putative extracellular beta-N-acetylglucosamonidase, and accumulation of a secreted putative xylanase inhibitor protein. Onset of the defence response was attended by an accumulation of glyceraldehyde-3-phosphate dehydrogenase and a fragment of a putative heat shock protein. Several distinct spots of both proteins, which preferentially accumulated in cell wall protein fractions, were identified. These three novel observations, viz. (i) secretion of a new class of putative enzyme inhibitor, (ii) the apparent recruitment of classical cytosolic proteins into the cell wall and (ii) the change in phosphorylation status of extracellular matrix proteins, suggest that the extracellular matrix plays a complex role in defence. We discuss the role of the extracellular matrix in signal modulation during pathogen-induced defence responses.
引用
收藏
页码:4894 / 4904
页数:11
相关论文
共 72 条
[51]   Induction of defence responses in cultured tobacco cells by elicitors from Phytophthora nicotianae [J].
Oelofse, D ;
Dubery, IA .
INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY, 1996, 28 (03) :295-301
[52]   MUTANT OF BACILLUS-SUBTILIS LACKING EXO-BETA-N-ACETYLGLUCOSAMINIDASE ACTIVITY [J].
ORTIZ, JM .
JOURNAL OF BACTERIOLOGY, 1974, 117 (02) :909-910
[53]   Characterization and oxidative in vitro cross-linking of an extensin-like protein and a proline-rich protein purified from chickpea cell walls [J].
Otte, O ;
Barz, W .
PHYTOCHEMISTRY, 2000, 53 (01) :1-5
[54]   GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE ON THE SURFACE OF GROUP-A STREPTOCOCCI IS ALSO AN ADP-RIBOSYLATING ENZYME [J].
PANCHOLI, V ;
FISCHETTI, VA .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1993, 90 (17) :8154-8158
[55]   MULTIPLICATION AND VIRULENCE IN PLANT-TISSUES OF ESCHERICHIA-COLI CLONES PRODUCING PECTATE LYASE ISOZYMES PLB AND PLE AT HIGH-LEVELS AND OF AN ERWINIA-CHRYSANTHEMI MUTANT DEFICIENT IN PLE [J].
PAYNE, JH ;
SCHOEDEL, C ;
KEEN, NT ;
COLLMER, A .
APPLIED AND ENVIRONMENTAL MICROBIOLOGY, 1987, 53 (10) :2315-2320
[56]   PEROXIDASE-GENERATED HYDROGEN-PEROXIDE AS A SOURCE OF ANTIFUNGAL ACTIVITY INVITRO AND ON TOBACCO LEAF-DISKS [J].
PENG, M ;
KUC, J .
PHYTOPATHOLOGY, 1992, 82 (06) :696-699
[57]   A 20-BP CIS-ACTING ELEMENT IS BOTH NECESSARY AND SUFFICIENT TO MEDIATE ELICITOR RESPONSE OF A MAIZE PRMS GENE [J].
RAVENTOS, D ;
JENSEN, AB ;
RASK, MB ;
CASACUBERTA, JM ;
MUNDY, J ;
SANSEGUNDO, B .
PLANT JOURNAL, 1995, 7 (01) :147-155
[58]   Transforming growth factor beta (TGF beta)-induced localization of apolipoprotein J/clusterin in epithelial cells [J].
Reddy, KB ;
Jin, G ;
Karode, MC ;
Harmony, JAK ;
Howe, PH .
BIOCHEMISTRY, 1996, 35 (19) :6157-6163
[59]  
RODRIGUEZGALVEZ E, 1995, PLANTA, V197, P535, DOI 10.1007/BF00196676
[60]   Extracellular mannose-6-phosphatase of Phanerochaete chrysosporium:: A lignin peroxidase-modifying enzyme [J].
Rothschild, N ;
Levkowitz, A ;
Hadar, Y ;
Dosoretz, C .
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1999, 372 (01) :107-111