Nα-terminal acetylation of proteins by NatA and NatB serves distinct physiological roles in Saccharomyces cerevisiae

N-terminal (Nt) acetylation is a highly prevalent co-translational protein modification in eukaryotes, catalyzed by at least five Nt acetyltransferases (Nats) with differing specificities. Nt acetylation has been implicated in protein quality control, but its broad biological significance remains el...

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Published in:Cell reports (Cambridge) 2021-02, Vol.34 (5), p.108711-108711, Article 108711
Main Authors: Friedrich, Ulrike Anne, Zedan, Mostafa, Hessling, Bernd, Fenzl, Kai, Gillet, Ludovic, Barry, Joseph, Knop, Michael, Kramer, Günter, Bukau, Bernd
Format: Article
Language:English
Subjects:
Acetylation
Acetyltransferases - metabolism
multi-omics
N-terminal acetylation
NatA
NatB
protein synthesis
ribosome profiling
Saccharomyces cerevisiae - metabolism
Saccharomyces cerevisiae Proteins - metabolism
translation
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Summary:N-terminal (Nt) acetylation is a highly prevalent co-translational protein modification in eukaryotes, catalyzed by at least five Nt acetyltransferases (Nats) with differing specificities. Nt acetylation has been implicated in protein quality control, but its broad biological significance remains elusive. We investigate the roles of the two major Nats of S. cerevisiae, NatA and NatB, by performing transcriptome, translatome, and proteome profiling of natAΔ and natBΔ mutants. Our results reveal a range of NatA- and NatB-specific phenotypes. NatA is implicated in systemic adaptation control, because natAΔ mutants display altered expression of transposons, sub-telomeric genes, pheromone response genes, and nuclear genes encoding mitochondrial ribosomal proteins. NatB predominantly affects protein folding, because natBΔ mutants, to a greater extent than natA mutants, accumulate protein aggregates, induce stress responses, and display reduced fitness in the absence of the ribosome-associated chaperone Ssb. These phenotypic differences indicate that controlling Nat activities may serve to elicit distinct cellular responses. [Display omitted] •Nt acetyltransferases NatA and NatB have distinct roles in cellular processes•NatA is implicated in the maintenance of chromosomal integrity•NatB plays a more important role in cellular proteostasis than NatA Friedrich et al. analyze yeast strains lacking the major N-terminal acetyltransferases NatA or NatB. Observed changes of transcription, translation, cellular physiology, and proteome integrity reveal that NatA and NatB ablation elicits distinct cellular responses. NatA is implicated in chromosomal integrity, while NatB plays more prominent roles in maintaining proteostasis.
ISSN:2211-1247
2211-1247
DOI:10.1016/j.celrep.2021.108711