A mutation at the fab2 locus of Arabidopsis caused increased levels of stearate in leaves. l h e increase in leaf stearate in fab2 varied developmentally, and the largest increase occurred in young leaves, where stearate accounted for almost 20% of total leaf fatty acids. The fatty acid composition of leaf lipids isolated from the fab2 mutant showed increased stearate in all the major glycero-lipids of both the chloroplast and extrachloroplast membranes. Although the stearate content was increased, the fab2 mutant still contained abundant amounts of 18:1, 182, and 1 8 3 fatty acids. lhese results are consistent with the expectations for a mutation partially affeding the action of the stromal stearoyl-acyl carrier protein desaturase. Positional analysis indicated that the extra 18:O is excluded with high specificity from the sn-2 position of both chloroplast and extrachloroplast glycerolipids. Although stearate content was increased in all the major leaf membrane lipids, the amount of increase varied considerably among the different lipids, from a high of 25% of fatty acids in phosphatidylcholine to a low of 2.9% of fatty acids in monogalactosyldiacylglycerol. The membrane lipid composition of plants differs from that of animals and fungi primarily in the composition of the chloroplast membranes and in a higher overall leve1 of un-saturation. The chloroplast membranes are composed almost entirely of the uncharged galactolipids MGD and DGD, which make up about 75% of the total chloroplast thylakoid lipid (Webb and Green, 1991). Depending upon the plant species, trienoic fatty acids (18:3 and 16:3) constitute up to 80% of the fatty acids in this organelle (Murphy, 1986). Although these features are common to a11 higher plants, it remains unclear how these characteristic lipid components are important to the physiology and cell biology of plants. In plants, de novo fatty acid synthesis occurs exclusively in the plastids (Ohlrogge and Kuo, 1985). The plant fatty acid synthase is composed of individual proteins (Shimakata and Stumpf, 1982), and the primary products of this type I1 synthase are 16:O-ACP and 18:O-ACP (Roughan et al., 1979). The 18:O-ACP is normally desaturated with high efficiency '