A 10 kDa acyl-CoA binding protein (ACBP) from Brassica napus enhances acyl exchange between acyl-CoA and phosphatidylcholine

• Author(s) / Creator(s)

  • Yurchenko, O. P.
  • Stymne, S.
  • Stahl, U.
  • Moloney, M. M.
  • Nykiforuk, C. L.
  • Weselake, R. J.
  • Banas, A.

• The gene encoding a 10-kDa acyl-CoA-binding protein (ACBP) from Brassica napus wasover-expressed in developing seeds of Arabidopsis thaliana. Biochemical analysis of T2andT3A. thaliana seeds revealed a significant increase in polyunsaturated fatty acids (FAs)(18:2cisD9,12and 18:3cisD9,12,15) at the expense of very long monounsaturated FA(20:1cisD11) and saturated FAs. In vitro assays demonstrated that recombinant B. napusACBP (rBnACBP) strongly increases the formation of phosphatidylcholine (PC) in theabsence of added lysophosphatidylcholine in microsomes from DYOR175c yeast expres-sing A. thaliana lysophosphatidylcholine acyltransferase (AthLPCAT) cDNA or in micro-somes 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 tocatalyse the transfer of acyl group from PC into acyl-CoA in vitro. These data suggest thatthe cytosolic 10-kDa ACBP has an effect on the equilibrium between metabolically activeacyl pools (acyl-CoA and phospholipid pools) involved in FA modifications and triacylgly-cerol bioassembly in plants. Over-expression of ACBP during seed development mayrepresent a useful biotechnological approach for altering the FA composition of seed oil.

• Date created

  2009

• Subjects / Keywords

  • Polyunsaturated Fatty Acid
  • Triacylglycerol
  • Lysophosphatidylcholineacy
  • PhosphatidylCholine
  • Acyl-CoA-Binding Protein
  • Transferase
  • Arabidopsis

• Type of Item

  Article (Published)

• DOI

  https://doi.org/10.7939/R3901ZV76

• License

  Attribution-ShareALike 4.0 International