Author/Authors :
J. Magnus Kjellberg، نويسنده , , Marc Trimborn، نويسنده , , Mats Andersson، نويسنده , , Anna Stina Sandelius، نويسنده ,
DocumentNumber :
1601597
Title Of Article :
Acyl-CoA dependent acylation of phospholipids in the chloroplast envelope
شماره ركورد :
12210
Latin Abstract :
Acyl-CoAs are substrates for acyl lipid synthesis in the endoplasmic reticulum. In addition, they may also be substrates for lipid acylation in other membranes. In order to assess whether lipid acylation may have a role in plastid lipid metabolism, we have studied the incorporation of radiolabelled fatty acids from acyl-CoAs into lipids in isolated, intact pea chloroplasts. The labelled lipids were phosphatidylcholine (PC), phosphatidylglycerol (PG), phosphatidylinositol and free fatty acids. With oleoyl-CoA, the fatty acid was incorporated preferably into the sn-2 position of PC and the acylation activity mainly occurred in fractions enriched in inner chloroplast envelope. Added lysoPC stimulated the activity. With palmitoyl-CoA, the fatty acid was incorporated primarily into the sn-1 position of PG and the reaction occurred at the surface of the chloroplasts. As chloroplast-synthesized PG generally contains 16C fatty acids in the sn-2 position, we propose that the acylation of PG studied represents activities present in a domain of the endoplasmic reticulum or an endoplasmic reticulum-derived fraction that is associated with chloroplasts and maintains this association during isolation. This domain or fraction contains a discreet population of lipid metabolizing activities, different from that of bulk endoplasmic reticulum, as shown by that with isolated endoplasmic reticulum, acyl-CoAs strongly labelled phosphatidic acid and phosphatidylethanolamine, lipids that were never labelled in the isolated chloroplasts.
From Page :
100
NaturalLanguageKeyword :
chloroplast , Acyl transferase , phosphatidylglycerol , Lipid synthesis , Pisum sativum , Phosphatidylcholine
JournalTitle :
Studia Iranica
To Page :
110
To Page :
110
Link To Document :
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