Analysis of lacking Na-terminal acetylation of proteins by NatA and NatB in Saccharomyces cerevisiae on mRNA levels and protein synthesis

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 and translatome profiling by using mRNA sequencing and ribosome profiling. The results are combined with global proteome, aggregome and stabilome datasets. To analyze previously proposed physiolocal roles of NatA and NatB in yeast cells on protein stability and interaction specific growth conditions such as different growth media and heat stress are used in addition to physiological growth. Overall design: mRNA sequencing and ribosome profiling of generated yeast strains lacking the N-terminal acetyltransferase complex catalytic subunit Naa10 (for NatA) or Naa20 (for NatB) in wild-type background or hml? background under different growth conditions (as indicated), each sample is prepared in replicates and wild-type yeast strain is used as reference (also in replicates)