RT Journal Article
SR Electronic
T1 N<sup>α</sup>-terminal acetylation of proteins by NatA and NatB serves distinct physiological roles in <em>Saccharomyces cerevisiae</em>
JF bioRxiv
FD Cold Spring Harbor Laboratory
SP 843953
DO 10.1101/843953
A1 Ulrike A. Friedrich
A1 Mostafa Zedan
A1 Bernd Hessling
A1 Kai Fenzl
A1 Ludovic Gillet
A1 Joseph Barry
A1 Michael Knop
A1 Günter Kramer
A1 Bernd Bukau
YR 2019
UL http://biorxiv.org/content/early/2019/11/20/843953.abstract
AB N-terminal (Nt)-acetylation is a highly prevalent co-translational protein modification in eukaryotes, catalyzed by at least five Nt-acetyltransferases (Nat) with differing specificities. Nt-acetylation has been implicated in protein quality control but its broad biological significance remains elusive. We investigated 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 do not support a general role of Nt-acetylation in protein degradation but reveal an unexpected range of Nat-specific phenotypes. NatA is implicated in systemic adaptation control, as 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, as natBΔ mutants accumulate protein aggregates, induce stress responses and display reduced fitness in absence of the ribosome-associated chaperone Ssb. These phenotypic differences indicate that controlling Nat activities may serve to elicit distinct cellular responses.