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

View ORCID ProfileUlrike A. Friedrich, Mostafa Zedan, Bernd Hessling, Kai Fenzl, Ludovic Gillet, Joseph Barry, Michael Knop, Günter Kramer, Bernd Bukau
doi: https://doi.org/10.1101/843953
Ulrike A. Friedrich
1Center for Molecular Biology of Heidelberg University (ZMBH) and German Cancer Research Center (DKFZ), DKFZ-ZMBH Alliance, Im Neuenheimer Feld 282, Heidelberg D-69120, Germany
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  • ORCID record for Ulrike A. Friedrich
Mostafa Zedan
1Center for Molecular Biology of Heidelberg University (ZMBH) and German Cancer Research Center (DKFZ), DKFZ-ZMBH Alliance, Im Neuenheimer Feld 282, Heidelberg D-69120, Germany
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Bernd Hessling
1Center for Molecular Biology of Heidelberg University (ZMBH) and German Cancer Research Center (DKFZ), DKFZ-ZMBH Alliance, Im Neuenheimer Feld 282, Heidelberg D-69120, Germany
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Kai Fenzl
1Center for Molecular Biology of Heidelberg University (ZMBH) and German Cancer Research Center (DKFZ), DKFZ-ZMBH Alliance, Im Neuenheimer Feld 282, Heidelberg D-69120, Germany
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Ludovic Gillet
2Institute of Molecular Systems Biology, ETH Zurich CH-8093, Switzerland
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Joseph Barry
3European Molecular Biology Laboratory (EMBL), Heidelberg, Germany
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Michael Knop
1Center for Molecular Biology of Heidelberg University (ZMBH) and German Cancer Research Center (DKFZ), DKFZ-ZMBH Alliance, Im Neuenheimer Feld 282, Heidelberg D-69120, Germany
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Günter Kramer
1Center for Molecular Biology of Heidelberg University (ZMBH) and German Cancer Research Center (DKFZ), DKFZ-ZMBH Alliance, Im Neuenheimer Feld 282, Heidelberg D-69120, Germany
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  • For correspondence: g.kramer@zmbh.uni-heidelberg.de bukau@zmbh.uni-heidelberg.de
Bernd Bukau
1Center for Molecular Biology of Heidelberg University (ZMBH) and German Cancer Research Center (DKFZ), DKFZ-ZMBH Alliance, Im Neuenheimer Feld 282, Heidelberg D-69120, Germany
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  • For correspondence: g.kramer@zmbh.uni-heidelberg.de bukau@zmbh.uni-heidelberg.de
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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 (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.

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Posted November 20, 2019.
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Nα-terminal acetylation of proteins by NatA and NatB serves distinct physiological roles in Saccharomyces cerevisiae
Ulrike A. Friedrich, Mostafa Zedan, Bernd Hessling, Kai Fenzl, Ludovic Gillet, Joseph Barry, Michael Knop, Günter Kramer, Bernd Bukau
bioRxiv 843953; doi: https://doi.org/10.1101/843953
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Nα-terminal acetylation of proteins by NatA and NatB serves distinct physiological roles in Saccharomyces cerevisiae
Ulrike A. Friedrich, Mostafa Zedan, Bernd Hessling, Kai Fenzl, Ludovic Gillet, Joseph Barry, Michael Knop, Günter Kramer, Bernd Bukau
bioRxiv 843953; doi: https://doi.org/10.1101/843953

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