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Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae

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Henriksen, P, Wagner, SA, Weinert, BT, Sharma, S, Bacinskaja, G, Rehman, M, Juffer, AH, Walther, TC, Lisby, M & Choudhary, C 2012, 'Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae' Molecular & cellular proteomics : MCP, vol. 11, no. 11, pp. 1510-22. https://doi.org/10.1074/mcp.M112.017251

APA

CBE

Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C. 2012. Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae. Molecular & cellular proteomics : MCP. 11(11):1510-22. https://doi.org/10.1074/mcp.M112.017251

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Author

Henriksen, Peter ; Wagner, Sebastian A ; Weinert, Brian T ; Sharma, Satyan ; Bacinskaja, Giedre ; Rehman, Michael ; Juffer, André H ; Walther, Tobias C ; Lisby, Michael ; Choudhary, Chunaram. / Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae. In: Molecular & cellular proteomics : MCP. 2012 ; Vol. 11, No. 11. pp. 1510-22.

Bibtex

@article{e0b9302350fc428c95f5ffe54065e610,
title = "Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae",
abstract = "Post-translational modification of proteins by lysine acetylation plays important regulatory roles in living cells. The budding yeast Saccharomyces cerevisiae is a widely used unicellular eukaryotic model organism in biomedical research. S. cerevisiae contains several evolutionary conserved lysine acetyltransferases and deacetylases. However, only a few dozen acetylation sites in S. cerevisiae are known, presenting a major obstacle for further understanding the regulatory roles of acetylation in this organism. Here we use high resolution mass spectrometry to identify about 4000 lysine acetylation sites in S. cerevisiae. Acetylated proteins are implicated in the regulation of diverse cytoplasmic and nuclear processes including chromatin organization, mitochondrial metabolism, and protein synthesis. Bioinformatic analysis of yeast acetylation sites shows that acetylated lysines are significantly more conserved compared with nonacetylated lysines. A large fraction of the conserved acetylation sites are present on proteins involved in cellular metabolism, protein synthesis, and protein folding. Furthermore, quantification of the Rpd3-regulated acetylation sites identified several previously known, as well as new putative substrates of this deacetylase. Rpd3 deficiency increased acetylation of the SAGA (Spt-Ada-Gcn5-Acetyltransferase) complex subunit Sgf73 on K33. This acetylation site is located within a critical regulatory domain in Sgf73 that interacts with Ubp8 and is involved in the activation of the Ubp8-containing histone H2B deubiquitylase complex. Our data provides the first global survey of acetylation in budding yeast, and suggests a wide-ranging regulatory scope of this modification. The provided dataset may serve as an important resource for the functional analysis of lysine acetylation in eukaryotes.",
keywords = "Acetylation, Conserved Sequence, Evolution, Molecular, Ions, Lysine/metabolism, Molecular Sequence Annotation, Nuclear Proteins/metabolism, Protein Transport, Proteome/metabolism, Proteomics/methods, Saccharomyces cerevisiae/enzymology, Saccharomyces cerevisiae Proteins/metabolism",
author = "Peter Henriksen and Wagner, {Sebastian A} and Weinert, {Brian T} and Satyan Sharma and Giedre Bacinskaja and Michael Rehman and Juffer, {Andr{\'e} H} and Walther, {Tobias C} and Michael Lisby and Chunaram Choudhary",
year = "2012",
month = "11",
doi = "10.1074/mcp.M112.017251",
language = "English",
volume = "11",
pages = "1510--22",
journal = "Molecular and Cellular Proteomics",
issn = "1535-9476",
publisher = "American Society for Biochemistry and Molecular Biology, Inc",
number = "11",

}

RIS

TY - JOUR

T1 - Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae

AU - Henriksen, Peter

AU - Wagner, Sebastian A

AU - Weinert, Brian T

AU - Sharma, Satyan

AU - Bacinskaja, Giedre

AU - Rehman, Michael

AU - Juffer, André H

AU - Walther, Tobias C

AU - Lisby, Michael

AU - Choudhary, Chunaram

PY - 2012/11

Y1 - 2012/11

N2 - Post-translational modification of proteins by lysine acetylation plays important regulatory roles in living cells. The budding yeast Saccharomyces cerevisiae is a widely used unicellular eukaryotic model organism in biomedical research. S. cerevisiae contains several evolutionary conserved lysine acetyltransferases and deacetylases. However, only a few dozen acetylation sites in S. cerevisiae are known, presenting a major obstacle for further understanding the regulatory roles of acetylation in this organism. Here we use high resolution mass spectrometry to identify about 4000 lysine acetylation sites in S. cerevisiae. Acetylated proteins are implicated in the regulation of diverse cytoplasmic and nuclear processes including chromatin organization, mitochondrial metabolism, and protein synthesis. Bioinformatic analysis of yeast acetylation sites shows that acetylated lysines are significantly more conserved compared with nonacetylated lysines. A large fraction of the conserved acetylation sites are present on proteins involved in cellular metabolism, protein synthesis, and protein folding. Furthermore, quantification of the Rpd3-regulated acetylation sites identified several previously known, as well as new putative substrates of this deacetylase. Rpd3 deficiency increased acetylation of the SAGA (Spt-Ada-Gcn5-Acetyltransferase) complex subunit Sgf73 on K33. This acetylation site is located within a critical regulatory domain in Sgf73 that interacts with Ubp8 and is involved in the activation of the Ubp8-containing histone H2B deubiquitylase complex. Our data provides the first global survey of acetylation in budding yeast, and suggests a wide-ranging regulatory scope of this modification. The provided dataset may serve as an important resource for the functional analysis of lysine acetylation in eukaryotes.

AB - Post-translational modification of proteins by lysine acetylation plays important regulatory roles in living cells. The budding yeast Saccharomyces cerevisiae is a widely used unicellular eukaryotic model organism in biomedical research. S. cerevisiae contains several evolutionary conserved lysine acetyltransferases and deacetylases. However, only a few dozen acetylation sites in S. cerevisiae are known, presenting a major obstacle for further understanding the regulatory roles of acetylation in this organism. Here we use high resolution mass spectrometry to identify about 4000 lysine acetylation sites in S. cerevisiae. Acetylated proteins are implicated in the regulation of diverse cytoplasmic and nuclear processes including chromatin organization, mitochondrial metabolism, and protein synthesis. Bioinformatic analysis of yeast acetylation sites shows that acetylated lysines are significantly more conserved compared with nonacetylated lysines. A large fraction of the conserved acetylation sites are present on proteins involved in cellular metabolism, protein synthesis, and protein folding. Furthermore, quantification of the Rpd3-regulated acetylation sites identified several previously known, as well as new putative substrates of this deacetylase. Rpd3 deficiency increased acetylation of the SAGA (Spt-Ada-Gcn5-Acetyltransferase) complex subunit Sgf73 on K33. This acetylation site is located within a critical regulatory domain in Sgf73 that interacts with Ubp8 and is involved in the activation of the Ubp8-containing histone H2B deubiquitylase complex. Our data provides the first global survey of acetylation in budding yeast, and suggests a wide-ranging regulatory scope of this modification. The provided dataset may serve as an important resource for the functional analysis of lysine acetylation in eukaryotes.

KW - Acetylation

KW - Conserved Sequence

KW - Evolution, Molecular

KW - Ions

KW - Lysine/metabolism

KW - Molecular Sequence Annotation

KW - Nuclear Proteins/metabolism

KW - Protein Transport

KW - Proteome/metabolism

KW - Proteomics/methods

KW - Saccharomyces cerevisiae/enzymology

KW - Saccharomyces cerevisiae Proteins/metabolism

U2 - 10.1074/mcp.M112.017251

DO - 10.1074/mcp.M112.017251

M3 - Journal article

VL - 11

SP - 1510

EP - 1522

JO - Molecular and Cellular Proteomics

JF - Molecular and Cellular Proteomics

SN - 1535-9476

IS - 11

ER -

ID: 54999626