Mechanisms and functions of protein S-acylation modifications at the plant vacuolar membrane

• Applicant: Dr. Oliver Batistic
• Subject Area: Plant Biochemistry and Biophysics
• Term: from 2012 to 2020
• Project identifier: Deutsche Forschungsgemeinschaft (DFG) - Project number 221273105

Protein S-acylation is an important secondary modification and regulates protein membrane association, targeting and function. However, detailed biochemical and genetic analyses of the modifying protein S-acyltransferases (PATs) and of modified target proteins have been hampered by the functional redundancy of modifying enzymes towards targets. In plants, the mechanisms, functions and requirements for protein S-acylation are not well understood. Therefore, we employed a functional screen and identified a specific enzyme-substrate pair (PAT10-CBL2) from Arabidopsis thaliana, which now allows addressing the mechanism of lipid modification at the plant tonoplast directly. Consequently, this project aims to elucidate the functional properties of the PAT proteins 10 and 11 from Arabidopsis, representing tonoplast localized enzymes. In addition we will analyze the mechanistic principles required for the targeting of enzymes (PAT) as well as their substrates, and especially the specific modification of substrates like the tonoplast bound calcineurin B-like (CBL) proteins by the vacuolar PAT enzymes.

• DFG Programme: Research Grants