Loss of N-terminal acetyltransferase A activity induces thermally unstable ribosomal proteins and increases their turnover in Saccharomyces cerevisiae

Ulises H. Guzman, Henriette Aksnes, Rasmus Ree, Nicolai Krogh, Magnus E. Jakobsson, Lars J. Jensen, Thomas Arnesen () and Jesper V. Olsen ()
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Ulises H. Guzman: University of Copenhagen
Henriette Aksnes: University of Bergen
Rasmus Ree: University of Bergen
Nicolai Krogh: University of Copenhagen
Magnus E. Jakobsson: University of Copenhagen
Lars J. Jensen: University of Copenhagen
Thomas Arnesen: University of Bergen
Jesper V. Olsen: University of Copenhagen

Nature Communications, 2023, vol. 14, issue 1, 1-16

Abstract: Abstract Protein N-terminal (Nt) acetylation is one of the most abundant modifications in eukaryotes, covering ~50-80 % of the proteome, depending on species. Cells with defective Nt-acetylation display a wide array of phenotypes such as impaired growth, mating defects and increased stress sensitivity. However, the pleiotropic nature of these effects has hampered our understanding of the functional impact of protein Nt-acetylation. The main enzyme responsible for Nt-acetylation throughout the eukaryotic kingdom is the N-terminal acetyltransferase NatA. Here we employ a multi-dimensional proteomics approach to analyze Saccharomyces cerevisiae lacking NatA activity, which causes global proteome remodeling. Pulsed-SILAC experiments reveals that NatA-deficient strains consistently increase degradation of ribosomal proteins compared to wild type. Explaining this phenomenon, thermal proteome profiling uncovers decreased thermostability of ribosomes in NatA-knockouts. Our data are in agreement with a role for Nt-acetylation in promoting stability for parts of the proteome by enhancing the avidity of protein-protein interactions and folding.

Date: 2023
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DOI: 10.1038/s41467-023-40224-x

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