Erratum to: Molecular Characterization of a Lysophosphatidylcholine Acyltransferase Gene Belonging to the MBOAT Family in Ricinus communis L.

Abstract

In the original publication of the article, figure 7 results were incorrectly published. Because of the discrepancies between our results published in Lipids 48(7):663–674, and others in the field with regards to Membrane Bound O-Acyltranferase (MBOAT) activity with 18:2n-6 and 18:3n-3 as substrates, we measured the activity of the castor lysophosphatidylcholine acyltransferase (RcLPCAT) using freshly prepared substrates. The 18:3-CoA and 18:2-CoA were prepared by chemical synthesis [1] and kindly provided by Dr. Stymne (Swedish University of Agricultural Sciences, Alnarp, Sweden). As indicated by our results using the new substrates, LPCAT activity was similar for 18:2 and 18:3 thioesters as it was for 18:1 and 16:1 thioesters, in agreement with the specificity recorded for Brassica LPCAT. These new results do not alter the major conclusion stated in our paper that MBOAT has limited activity with ricinoleoyl-CoA as a substrate, but does indicate it has similar activity with 18:2-CoA and 18:3-CoA as it does with 18:1-CoA and 16:1-CoA. The correct version of figure 7 is given below: RcLPCAT specificity using diverse acyl-CoA donors. LPCAT activity was assayed using 50 μM lysoPtdCho as the acceptor and different acyl-CoA as substrates at two concentrations, 10 μM (grey bars) or 40 μM (black bars) as indicated. The assay was performed as described in “Materials and Methods” of the published paper, in the presence of 30 μg of membrane protein extract prepared from yeast ale1 cells expressing RcLPCAT. Background LPLAT activities were determined from cells transformed with the pYES2 empty vector and the appropriate background rates were subtracted from the measured rate. The specific activity is presented and is expressed as nmol of released CoA min−1 μg−1 of membrane protein