Characterization of elicitin-like phospholipases isolated from Phytophthora capsici culture filtrate

Citation
C. Nespoulous et al., Characterization of elicitin-like phospholipases isolated from Phytophthora capsici culture filtrate, FEBS LETTER, 452(3), 1999, pp. 400-406
Citations number
47
Categorie Soggetti
Biochemistry & Biophysics
Journal title
FEBS LETTERS
ISSN journal
00145793 → ACNP
Volume
452
Issue
3
Year of publication
1999
Pages
400 - 406
Database
ISI
SICI code
0014-5793(19990611)452:3<400:COEPIF>2.0.ZU;2-R
Abstract
The phytopathogenic oomycete Phytophthora capsici secretes in culture a pho spholipase activity, Two enzyme isoforms exhibiting a high phospholipase B activity were isolated by chromatography and electrophoresis, They differ i n their apparent molar masses (22 and 32 kDa), Both proteins are glycosylat ed and share the same N-terminal amino acid sequence up to the 39th residue with a high homology with capsicein, the P. capsici elicitin, Although dev oid of phospholipase activity, capsicein was shown by circular dichroism to specifically interact with negatively charged phospholipids, suggesting th at the membrane lipids could be a potential target for elicitins. (C) 1999 Federation of European Biochemical Societies.