Abstract
Protein prenylation is one of the post-translational lipid modifications, which affects protein-membrane interactions, protein-protein interactions, and activities of proteins. Protein prenyltransferases (PPTases) catalyze the transfer of a prenyl moiety derived from farnesyl diphosphate or geranylgeranyl diphosphate to the cysteine residue in recognition motifs at the C-terminus of target proteins. In higher plants, some PPTase mutants show phenotypes including hypersensitivity to ABA and NAA, enlarged meristems, and increase of floral organs, indicating important roles in stress responses and developmental regulations. Despite the importance of this modification, the identification of most putative target proteins is solely based on their C-terminal motifs identified to be prenylated in studies of mammalian PPTases. Therefore, not much is known about actual target proteins and the significance of prenylation in protein function regulation in higher plants.
As a first step to comprehensively identify prenylated proteins, we report the results from a high-throughput proteomics study of prenylated proteins from Arabidopsis suspension culture cells, labeled with azide-substrates.
