KatNat- Elucidating the multifaceted functions of protein acetyltransferases in plant stress response and regulation of metabolism.


Plants must constantly respond to a wide range of signals, including stresses, in order to coordinate their development and survival within a dynamic environment. One way in which this is achieved is through chemical modifications of proteins, allowing flexible and rapid changes of the proteome to alter cellular and physiological outputs. Protein acetylation is one such modification, which occurs on the N-termini (Nt) and internal lysines (K) of many proteins (Fig. 1).

© ERA-CAPS Project KatNat
Fig. 1: Protein acetylation. Proteins can be acetylated at internal lysine residues as well as at the protein N-terminus. Both reactions are enzyme catalyzed by either lysine acetyltransferases (KAT) or N-terminal acetyltransferases (NAT), respectively. Both enzymes use acetyl-CoA as substrate.

Although, protein acetylation is a prevalent modification, our knowledge of the regulation, specificity and plasticity, and its downstream functional consequences on protein activity and physiology are just emerging, especially in plants.

Aim of Research

The overarching aim of the KatNat project is to provide a mechanistic understanding of protein acetylation in plants, with a particular focus on investigating the enzymes that catalyze this modification (Nt- and K-acetyltransferases) and the resultant effects on proteostasis, photosynthesis, and metabolism.

Who are we?

The KatNat consortium brings together five European groups who all have a significant, demonstrable interest in the study of protein acetylation, and who have the highly complementary expertise in mass spectrometry, protein biochemistry, physiology and molecular plant biology.

© ERA-CAPS Project KatNat