Researchers from the University of Bergen (UiB) have uncovered that proteins use a common chemical label as a shield to protect them from degradation, which in turn affects motility and aging.
Proteins are key to all processes in our cells and understanding their functions and regulation is of major importance.
CRISPR-Cas9 technology sheds new light on N-terminal acetylation To address this question, molecular biologist and researcher Sylvia Varland spent two years at the Donnelly Centre for Cellular & Biomolecular Research, University of Toronto, Canada, supported by a FRIPRO mobility grant from the Research Council of Norway.
Related StoriesBack in the Arnesen lab at UiB, Varland explored the molecular implications of her genetic findings with the help from PhD student Ine Kjosås and other lab members. Biochemical, cell biology and proteomics experiments demonstrated that N-terminal acetylation acts as shield to protect many proteins from protein degradation. Proteins lacking N-terminal acetylation were recognized by the cellular degradation machinery .
Postdoctoral researcher Rui Silva and fellow students carried out studies with flies lacking N-terminal acetylation. The two teams decided to merge their efforts and have for the last two years coordinated their experiments. Flies lacking NatC were viable, but these flies displayed decreased longevity and decreased motility with age . These effects could be partially reversed by expressing a protein conserved between fly and human found to be a key target of NatC protection.
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