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Purification and antipathogenic activity of lipid transfer proteins (LTPs) from the leaves of Arabidopsis and spinach
Author(s) -
Segura Ana,
Moreno Manuel,
García-Olmedo Francisco
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)80641-7
Subject(s) - spinach , arabidopsis , plant lipid transfer proteins , chemistry , food science , botany , biochemistry , biology , gene , mutant
Two homogeneous proteins active in vitro against the bacterial pathogen Clavibacter michiganensis subsp. sepedonicus were obtained from a crude cell‐wall preparation from the leaves of Columbia wild‐type Arabidopsis . The N‐terminal amino acid sequences of these proteins allowed their identification as lipid transfer proteins (LTP‐a1, LTP‐a2); the LTP1‐a1 sequence was identical to that deduced from a previously described cDNA (EMBL M80566) and LTP‐a2 was quite divergent (44% identical positions). These proteins were not detected in the cytoplasmic fraction by Western‐blot analysis. Proteins LTP‐s1 and LTP‐s2 were similarly obtained from spinach leaves; LTP‐s1 was 91% identical to a previously purified spinach LTP (Swiss Prot P10976), and LTP‐s2 was moderately divergent (71% identical positions). About 1/3 of the total LTPs were detected in the cytoplasmic fraction from spinach by Westem‐blot analysis. Concentrations of these proteins causing 50% inhibition (EC‐50) were in the 0.1–1 μM range for the bacterial pathogens C . michiganensis and Pseudomonas solanacearum and close to 10 μM for the fungal pathogen Fusarium solani .