An atlas of Arabidopsis protein S-acylation reveals its widespread role in plant cell organization and function.

ABSTRACT: S-acylation is the addition of a fatty acid to a cysteine residue of a protein. While this modification may profoundly alter protein behaviour, its effects on the function of plant proteins remains poorly characterized, largely as a result of the lack of basic information regarding which proteins are S-acylated and where in the proteins the modification occurs. To address this gap in our knowledge, we used an optimized acyl-resin-assisted capture assay to perform a comprehensive analysis of plant protein S-acylation from six separate tissues. In our high- and medium-confidence groups, we identified 1,849 cysteines modified by S-acylation, which were located in 1,640 unique peptides from 1,094 different proteins. This represents around 6% of the detectable Arabidopsis proteome and suggests

SUBMITTER: Kumar M 

PROVIDER: S-EPMC7617270 | biostudies-literature | 2022 Jun

REPOSITORIES: biostudies-literature