Open AccessA 10‐kDa acyl‐CoA‐binding protein (ACBP) from Brassica napus enhances acyl exchange between acyl‐CoA and phosphatidylcholine
Author(s) -
Yurchenko Olga P.,
Nykiforuk Cory L.,
Moloney Maurice M.,
Ståhl Ulf,
Banaś Antoni,
Stymne Sten,
Weselake Randall J.
Publication year - 2009
Publication title -
plant biotechnology journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.525
H-Index - 115
eISSN - 1467-7652
pISSN - 1467-7644
DOI - 10.1111/j.1467-7652.2009.00427.x
Subject(s) - lysophosphatidylcholine , biology , biochemistry , arabidopsis thaliana , acyltransferase , phosphatidylcholine , brassica , microsome , acyl coa , yeast , enzyme , phospholipid , gene , botany , mutant , membrane
Summary The gene encoding a 10‐kDa acyl‐CoA‐binding protein (ACBP) from Brassica napus was over‐expressed in developing seeds of Arabidopsis thaliana . Biochemical analysis of T 2 and T 3 A. thaliana seeds revealed a significant increase in polyunsaturated fatty acids (FAs) (18:2 cis Δ9,12 and 18:3 cis Δ9,12,15 ) at the expense of very long monounsaturated FA (20:1 cis Δ11 ) and saturated FAs. In vitro assays demonstrated that recombinant B. napus ACBP (rBnACBP) strongly increases the formation of phosphatidylcholine (PC) in the absence of added lysophosphatidylcholine in microsomes from ΔYOR175c yeast expressing A. thaliana lysophosphatidylcholine acyltransferase ( AthLPCAT ) cDNA or in microsomes from microspore‐derived cell suspension cultures of B. napus L. cv. Jet Neuf. rBnACBP or bovine serum albumin (BSA) were also shown to be crucial for AthLPCAT to catalyse the transfer of acyl group from PC into acyl‐CoA in vitro . These data suggest that the cytosolic 10‐kDa ACBP has an effect on the equilibrium between metabolically active acyl pools (acyl‐CoA and phospholipid pools) involved in FA modifications and triacylglycerol bioassembly in plants. Over‐expression of ACBP during seed development may represent a useful biotechnological approach for altering the FA composition of seed oil.