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Cell Rep

Title:		N(alpha)-terminal acetylation of proteins by NatA and NatB serves distinct physiological roles in Saccharomyces cerevisiae
Author(s):		Friedrich UA; Zedan M; Hessling B; Fenzl K; Gillet L; Barry J; Knop M; Kramer G; Bukau B;
Address:		"Center for Molecular Biology of Heidelberg University (ZMBH) and German Cancer Research Center (DKFZ), DKFZ-ZMBH Alliance, Heidelberg 69120, Germany. Institute of Molecular Systems Biology, ETH Zurich, Zurich 8093, Switzerland. European Molecular Biology Laboratory (EMBL), Heidelberg 69117, Germany. Center for Molecular Biology of Heidelberg University (ZMBH) and German Cancer Research Center (DKFZ), DKFZ-ZMBH Alliance, Heidelberg 69120, Germany. Electronic address: g.kramer@zmbh.uni-heidelberg.de. Center for Molecular Biology of Heidelberg University (ZMBH) and German Cancer Research Center (DKFZ), DKFZ-ZMBH Alliance, Heidelberg 69120, Germany. Electronic address: bukau@zmbh.uni-heidelberg.de"
Journal Title:		Cell Rep
Year:		2021
Volume:		34
Issue:		5
Page Number:		108711 -
DOI:		10.1016/j.celrep.2021.108711
ISSN/ISBN:		2211-1247 (Electronic)
Abstract:		"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 natADelta and natBDelta mutants. Our results reveal a range of NatA- and NatB-specific phenotypes. NatA is implicated in systemic adaptation control, because natADelta 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 natBDelta 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"
Keywords:		Acetylation Acetyltransferases/*metabolism Saccharomyces cerevisiae/*metabolism Saccharomyces cerevisiae Proteins/*metabolism N-terminal acetylation NatA NatB multi-omics protein synthesis ribosome profiling translation;
Notes:		"MedlineFriedrich, Ulrike Anne Zedan, Mostafa Hessling, Bernd Fenzl, Kai Gillet, Ludovic Barry, Joseph Knop, Michael Kramer, Gunter Bukau, Bernd eng Research Support, Non-U.S. Gov't 2021/02/04 Cell Rep. 2021 Feb 2; 34(5):108711. doi: 10.1016/j.celrep.2021.108711"