Elucidating the functions of RPD3/HDA1-like lysine deacetylases in Arabidopsis thaliana

Basic data for this project

Description

Reversible acetylation of the ε-amino group of lysine has recently emerged as an ubiquitous post-translational modification controlling many important cellular functions beyond transcription. It is a conserved modification occurring on proteins of both, prokaryotes and eukaryotes, indicating its universal importance for life. The identification of lysine acetylation sites on many metabolic enzymes was a first step to uncover its physiological role in metabolism. Lysine acetylation is catalysed by the antagonistic action of lysine acetyltransferases and lysine deacetylases. Lysine deacetylases (KDACs) have central functions in regulating stress defenses and development in plants, but their action was mainly investigated in the context of histones thus far, and their versatility in molecular activities is still largely unexplored. This project aims at a comprehensive investigation on the molecular functions of Arabidopsis RPD3/HDA1-like KDACs to uncover new functions and target proteins connected to plant stress physiology and development. This project will employ a sophisticated biochemical toolbox for dissecting novel KDAC functions in plants. The toolbox will include activity-based probes for the pull-down of active KDACs from tissues and analysed by quantitative mass spectrometry, large-scale acetylome profiling of KDAC mutants, and testing new peptide-based acyl-lysine substrates to determine their enzymatic properties. Taken together these approaches shall uncover novel KDAC functions important for the integration of stress responses and development in plants.