10:17pm Tuesday 12 December 2017

New protein tricks from an old enzyme

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.

Naa10 catalyzes N-terminal acetylation and N-terminal propionylation (Arnt Raae, MBI)

Identification of N-terminal acetyltransferases (NATs) as N-terminal propionyltransferases (NPTs) in yeast and humans. Naa10 (light blue) and other NATs/NPTs catalyze the transfer of an Acetyl (red) moiety or Propionyl (purple) moiety from Ac-CoA (red) or Prop-CoA (purple), respectively, to the N-terminal amino acid residue of a polypeptide. This process may occur both co-translationally while the polypeptide emerges from the ribosome (green) and post-translationally. A major fraction of the eukaryotic proteomes is N-terminally acetylated while a minor fraction is N-terminally propionylated. Arnt Raae, MBI, UiB.

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