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The eukaryotic NAT-machinery

Protein N-terminal acetylation

From molecular mechanisms to human disease

Most proteins are chemically modified in the cell and such modifications are often crucial for the protein’s ability to carry out a function. N-terminal acetylation one of the most common modifications in eukaryotes. It is catalyzed by N-terminal acetyltransferases (NATs) which are linked to cancer, genetic syndromes, and regulation of human metabolism.

The Arnesen lab is part of the Translational Cell Signaling and Metabolism research group at the Department of biomedicine.

New research
melissa-labellarte unsplash

New gene variants linked to congenital heart disease

Around 600 children are born with congenital heart disease in Norway each year. Little is known about the causes of congenital heart defects. A new international study involving researchers from University of Bergen and Haukeland University Hospital shows that the NAA15 protein can play an important...

New research
Structure of actin, profilin and NAA80

Mechanism of a cell motility regulator

Actin is the most abundant protein in human cells and is involved in numerous functions including steering cellular architecture, cell motility and cell division. Recently, UiB researchers identified NAA80 as a long-sought actin regulator. Now, the structure of NAA80 bound to actin and profilin...

News
PFN2 co-operates with NAA80 to acetylate actin

The cell motility regulator NAA80 is assisted by Profilin 2

Actin is modified by N-terminal acetylation which regulates its role in steering cellular architecture and cell motility. Now the machinery performing this acetylation is uncovered.

New research
Ine Kjosås (venstre) og Emilie Seljesth (høyre) under MOL231 posterpresentasjon, våren 2019.

From MOL231 Project to Published Article

Ine and Emilie were attending a project course priming them for lab work. They ended up co-developing a method to quality control a cell model which is used by thousands of researchers worldwide.

Cell biology
Cryo-EM structures of the NatE complex with/without HYPK bound

The structure of an enzyme complex upregulated in cancer

In human cells, N-terminal acetylation is among the most common protein modifications. Now, researchers at the University of Pennsylvania and the University of Bergen have revealed the structural and biochemical properties of the major molecular machine involved in this process. Cancer cells require...