The Atypical Pectin Methylesterase Family Member PME31 Promotes Seedling Lipid Droplet Utilization.

Abstract

In plants, the primary form of energy stored in seed lipid droplets, triacylglycerol (TAG), is catabolized during germination to support pre-photosynthetic growth. Although this process is essential for seedling development, it is incompletely understood. In a screen for Arabidopsis thaliana mutants displaying delayed degradation of the lipid droplet coat protein oleosin, five independent mutations in PECTIN METHYLESTERASE31 (PME31) were recovered. In addition to delayed oleosin degradation, pme31 mutant seedlings exhibited sustained lipid droplets and elevated levels of several TAG and diacylglycerol species. Although structural prediction classified PME31 as a pectinesterase, this structural family also includes a putative E. coli lipase, YbhC. Moreover, PME31 lacks an N-terminal signal peptide that would target it to the cell wall, where pectin resides. We found that a fluorescent PME31 reporter was cytosolic and partially associated with peroxisomes, the site of fatty acid catabolism, during lipid mobilization. Our findings suggest that, in contrast to canonical PMEs, which modify cell wall pectin, PME31 functions at peroxisomes to directly or indirectly promote lipid mobilization.