Loss of N-terminal acetyltransferase A activity induces thermally unstable ribosomal proteins and increases their turnover in Saccharomyces cerevisiae

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Loss of N-terminal acetyltransferase A activity induces thermally unstable ribosomal proteins and increases their turnover in Saccharomyces cerevisiae. / Guzman, Ulises H.; Aksnes, Henriette; Ree, Rasmus; Krogh, Nicolai; Jakobsson, Magnus E.; Jensen, Lars J.; Arnesen, Thomas; Olsen, Jesper V.

In: Nature Communications, Vol. 14, 4517, 2023.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Guzman, UH, Aksnes, H, Ree, R, Krogh, N, Jakobsson, ME, Jensen, LJ, Arnesen, T & Olsen, JV 2023, 'Loss of N-terminal acetyltransferase A activity induces thermally unstable ribosomal proteins and increases their turnover in Saccharomyces cerevisiae', Nature Communications, vol. 14, 4517. https://doi.org/10.1038/s41467-023-40224-x

APA

Guzman, U. H., Aksnes, H., Ree, R., Krogh, N., Jakobsson, M. E., Jensen, L. J., Arnesen, T., & Olsen, J. V. (2023). Loss of N-terminal acetyltransferase A activity induces thermally unstable ribosomal proteins and increases their turnover in Saccharomyces cerevisiae. Nature Communications, 14, [4517]. https://doi.org/10.1038/s41467-023-40224-x

Vancouver

Guzman UH, Aksnes H, Ree R, Krogh N, Jakobsson ME, Jensen LJ et al. Loss of N-terminal acetyltransferase A activity induces thermally unstable ribosomal proteins and increases their turnover in Saccharomyces cerevisiae. Nature Communications. 2023;14. 4517. https://doi.org/10.1038/s41467-023-40224-x

Author

Guzman, Ulises H. ; Aksnes, Henriette ; Ree, Rasmus ; Krogh, Nicolai ; Jakobsson, Magnus E. ; Jensen, Lars J. ; Arnesen, Thomas ; Olsen, Jesper V. / Loss of N-terminal acetyltransferase A activity induces thermally unstable ribosomal proteins and increases their turnover in Saccharomyces cerevisiae. In: Nature Communications. 2023 ; Vol. 14.

Bibtex

@article{40eb21ca9ec74620b42b512944da4c97,
title = "Loss of N-terminal acetyltransferase A activity induces thermally unstable ribosomal proteins and increases their turnover in Saccharomyces cerevisiae",
abstract = "Protein N-terminal (Nt) acetylation is one of the most abundant modifications in eukaryotes, covering ~50-80 % of the proteome, depending on species. Cells with defective Nt-acetylation display a wide array of phenotypes such as impaired growth, mating defects and increased stress sensitivity. However, the pleiotropic nature of these effects has hampered our understanding of the functional impact of protein Nt-acetylation. The main enzyme responsible for Nt-acetylation throughout the eukaryotic kingdom is the N-terminal acetyltransferase NatA. Here we employ a multi-dimensional proteomics approach to analyze Saccharomyces cerevisiae lacking NatA activity, which causes global proteome remodeling. Pulsed-SILAC experiments reveals that NatA-deficient strains consistently increase degradation of ribosomal proteins compared to wild type. Explaining this phenomenon, thermal proteome profiling uncovers decreased thermostability of ribosomes in NatA-knockouts. Our data are in agreement with a role for Nt-acetylation in promoting stability for parts of the proteome by enhancing the avidity of protein-protein interactions and folding.",
author = "Guzman, {Ulises H.} and Henriette Aksnes and Rasmus Ree and Nicolai Krogh and Jakobsson, {Magnus E.} and Jensen, {Lars J.} and Thomas Arnesen and Olsen, {Jesper V.}",
note = "Publisher Copyright: {\textcopyright} 2023, The Author(s).",
year = "2023",
doi = "10.1038/s41467-023-40224-x",
language = "English",
volume = "14",
journal = "Nature Communications",
issn = "2041-1723",
publisher = "nature publishing group",

}

RIS

TY - JOUR

T1 - Loss of N-terminal acetyltransferase A activity induces thermally unstable ribosomal proteins and increases their turnover in Saccharomyces cerevisiae

AU - Guzman, Ulises H.

AU - Aksnes, Henriette

AU - Ree, Rasmus

AU - Krogh, Nicolai

AU - Jakobsson, Magnus E.

AU - Jensen, Lars J.

AU - Arnesen, Thomas

AU - Olsen, Jesper V.

N1 - Publisher Copyright: © 2023, The Author(s).

PY - 2023

Y1 - 2023

N2 - Protein N-terminal (Nt) acetylation is one of the most abundant modifications in eukaryotes, covering ~50-80 % of the proteome, depending on species. Cells with defective Nt-acetylation display a wide array of phenotypes such as impaired growth, mating defects and increased stress sensitivity. However, the pleiotropic nature of these effects has hampered our understanding of the functional impact of protein Nt-acetylation. The main enzyme responsible for Nt-acetylation throughout the eukaryotic kingdom is the N-terminal acetyltransferase NatA. Here we employ a multi-dimensional proteomics approach to analyze Saccharomyces cerevisiae lacking NatA activity, which causes global proteome remodeling. Pulsed-SILAC experiments reveals that NatA-deficient strains consistently increase degradation of ribosomal proteins compared to wild type. Explaining this phenomenon, thermal proteome profiling uncovers decreased thermostability of ribosomes in NatA-knockouts. Our data are in agreement with a role for Nt-acetylation in promoting stability for parts of the proteome by enhancing the avidity of protein-protein interactions and folding.

AB - Protein N-terminal (Nt) acetylation is one of the most abundant modifications in eukaryotes, covering ~50-80 % of the proteome, depending on species. Cells with defective Nt-acetylation display a wide array of phenotypes such as impaired growth, mating defects and increased stress sensitivity. However, the pleiotropic nature of these effects has hampered our understanding of the functional impact of protein Nt-acetylation. The main enzyme responsible for Nt-acetylation throughout the eukaryotic kingdom is the N-terminal acetyltransferase NatA. Here we employ a multi-dimensional proteomics approach to analyze Saccharomyces cerevisiae lacking NatA activity, which causes global proteome remodeling. Pulsed-SILAC experiments reveals that NatA-deficient strains consistently increase degradation of ribosomal proteins compared to wild type. Explaining this phenomenon, thermal proteome profiling uncovers decreased thermostability of ribosomes in NatA-knockouts. Our data are in agreement with a role for Nt-acetylation in promoting stability for parts of the proteome by enhancing the avidity of protein-protein interactions and folding.

U2 - 10.1038/s41467-023-40224-x

DO - 10.1038/s41467-023-40224-x

M3 - Journal article

C2 - 37500638

AN - SCOPUS:85165894108

VL - 14

JO - Nature Communications

JF - Nature Communications

SN - 2041-1723

M1 - 4517

ER -

ID: 362144095