Description of Research Group
Protein N-terminal acetylation is among the most common types of protein modifications occurring on approximately 50% of all yeast proteins and more than 80 % of all human proteins. Surprisingly, there is yet no clear functional understanding of how N-terminal acetylation affects proteins in general, although recent data indicate roles in protein degradation and targeting. N-terminal acetylation is a co-translational process occurring on the ribosomes and is considered irreversible. An N-terminal acetyltransferase (NAT) transfers an Acetyl group from Acetyl Coenzyme A to the alpha-amino group of the Nterminal
amino acid residue of the protein. During the last decade, the human NATs have been identified and characterized by our group. In humans as in yeast, three NAT complexes NatA, NatB and NatC are believed to perform most N-terminal
acetylations. Each NAT complex is composed of specific subunits and acetylates a specific subset of substrates. Very recently, also human NatD, NatE and NatF were identified. A number of studies have described various aspects of Nterminal
acetylation in humans, such as substrates, NAT knockdown phenotypes, and expression patterns of NAT subunits. Through these studies, a complex and specific system of N-terminal acetylation has been revealed. The importance of Nterminal acetylation in human cell biology and disease has been increasingly recognized.
Technology, expertise and equipment
Detailed knowledge about the catalytic mechanisms underlying the NATs. Long experience with inhibitors, development of new inhibitors.