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Identification and characterization of an LCAT‐like Arabidopsis thaliana gene encoding a novel phospholipase A
Author(s) -
Chen Guanqun,
Greer Michael S.,
Lager Ida,
Lindberg Yilmaz Jenny,
Mietkiewska Elzbieta,
Carlsson Anders S.,
Stymne Sten,
Weselake Randall J.
Publication year - 2012
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/j.febslet.2011.12.034
Subject(s) - phosphatidylethanolamine , phosphatidic acid , biochemistry , arabidopsis , acyltransferase , arabidopsis thaliana , silique , phosphatidylserine , biology , phosphatidylcholine , phospholipase d , phospholipase a1 , phospholipase , gene , phospholipid , enzyme , chemistry , mutant , membrane
A previously uncharacterized Arabidopsis lecithin:cholesterol acyltransferase (LCAT) family gene ( At4g19860 ) was functionally expressed in yeast, where it was demonstrated to encode a novel cytosolic and calcium‐independent phospholipase A with preferences for the sn‐2 position. This enzyme shows optimal activity at pH 5.0, exhibits a headgroup specificity for phosphatidylcholine > phosphatidic acid > phosphatidylethanolamine > phosphatidylglycerol > phosphatidylserine and has an acyl chain specificity for oleoyl > linoleoyl > ricinoleoyl. The expression of AtLCAT‐PLA inhibited yeast cell growth and fatty acid accumulation. AtLCAT‐PLA transcript in Arabidopsis was detected at high levels in roots and siliques.