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Cardiolipin synthase of Arabidopsis thaliana
Author(s) -
Nowicki Marcin,
Müller Frank,
Frentzen Margrit
Publication year - 2005
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.2005.03.007
Subject(s) - cardiolipin , arabidopsis thaliana , arabidopsis , biochemistry , phosphatidylglycerol , diacylglycerol kinase , escherichia coli , chemistry , divalent , phospholipid , signal peptide , biology , gene , enzyme , peptide sequence , membrane , protein kinase c , organic chemistry , phosphatidylcholine , mutant
Functional expression studies in microorganisms showed that the Arabidopsis thaliana gene At4g04870 represents the cardiolipin synthase ( CLS ) gene encoding a hydrophobic preprotein of 38 kDa with a cleavable signal peptide for the import into mitochondria. CLS of Arabidopsis over‐expressed in Escherichia coli has an alkaline pH optimum, a strict requirement for divalent cations and a distinctly lower K m for cytidinediphosphate‐diacylglycerol than for phosphatidylglycerol. It displayed a preference for both its substrates esterified with unsaturated acyl groups. Solubilization and purification experiments revealed that the protein requires a defined phospholipid environment, particularly the presence of cardiolipin, to acquire its catalytically active conformation.