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New protein tricks from an old enzyme

Small chemical groups are commonly attached to proteins in order to control their function. In eukaryotic cells, N-terminal acetyltransferases (NATs) attach acetyl groups to the very first amino acid (the N-terminus) of a majority of proteins. Now, researchers at MBI (UiB) and VIB-Gent have discovered that NATs also carry out other types of protein modifications.

Photo:
Arnt Raae (MBI)

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As presented by the ASBMB, small chemical groups are commonly attached to proteins in order to control their activity, localization, and stability. In eukaryotic cells, most proteins are modified at their N-termini by an acetyl group. N-terminal acetylation involves the transfer of an acetyl moiety from acetyl coenzyme A to the α-amino group of the first amino acid residue of a protein and is catalyzed by N-terminal acetyltransferases (NATs). The NATs have been linked to cancer development and most recently a NAT-mutation was found to cause genetic disease.

Now, researchers from the Department of Molecular Biology (MBI), University of Bergen, and Ghent University (VIB) have revealed that a related protein modification, N-terminal propionylation, is conserved among eukaryotes. Interestingly, the NATs were uncovered to also be responsible for this newly discovered modification by transferring a propionyl-moiety from propionyl coenzyme A to various proteins. Thus, the NATs now emerge as multifunctional enzymes with a broad and diverse impact on the eukaryotic proteomes. These results are published in the current issue of Molecular and Cellular Proteomics.