
Functional analysis of cysteine residues of ECP elicitor proteins of the fungal tomato pathogen Cladosporium fulvum
Author(s) -
Luderer Rianne,
De Kock Maarten J. D.,
Dees Robert H. L.,
De Wit Pierre J. G. M.,
Joosten Matthieu H. A. J.
Publication year - 2002
Publication title -
molecular plant pathology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.945
H-Index - 103
eISSN - 1364-3703
pISSN - 1464-6722
DOI - 10.1046/j.1464-6722.2001.00095.x
Subject(s) - cysteine , elicitor , cladosporium , hypersensitive response , biology , biochemistry , cysteine protease , microbiology and biotechnology , enzyme , gene , plant disease resistance , aspergillus
summary A striking feature of all elicitor proteins of Cladosporium fulvum that are specifically recognized by tomato is that they contain an even number of cysteine residues. These cysteine residues are thought to be involved in disulphide bridges. In this study, a mutational analysis of the cysteine residues of ECP1, ECP2 and ECP5 was performed, to examine their role in stability and hypersensitive response‐inducing activity of the proteins. We show that not all cysteine residues of the ECPs are critical for the hypersensitive response‐inducing activity of the proteins, and we propose that the role of cysteine residues in the ECPs is more complex than anticipated.