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Lysine Acetylation Stoichiometry Analysis at the Proteome Level

Gil, Jeovanis LU and Encarnación-Guevara, Sergio (2022) In Methods in Molecular Biology 2420. p.73-86
Abstract

Lysine acetylation is a widespread posttranslational modification (PTM) in all kingdoms of live. A large number of proteins involved in most of biological pathways are targets of this PTM. The lysine acetylation is a reversible modification controlled by two main groups of enzymes, lysine acetyltransferases responsible for transferring the acetyl group of acetylCoA to the side chain of lysine residues and lysine deacetylases which effectively remove the acetyl tag. Dysregulation of enzymes that control acetylation and/or target proteins have been associated with a growing number of human pathologies. Lysine acetylation is largely a modification that occurs at low stoichiometry at its target sites. Here we describe a method to identify... (More)

Lysine acetylation is a widespread posttranslational modification (PTM) in all kingdoms of live. A large number of proteins involved in most of biological pathways are targets of this PTM. The lysine acetylation is a reversible modification controlled by two main groups of enzymes, lysine acetyltransferases responsible for transferring the acetyl group of acetylCoA to the side chain of lysine residues and lysine deacetylases which effectively remove the acetyl tag. Dysregulation of enzymes that control acetylation and/or target proteins have been associated with a growing number of human pathologies. Lysine acetylation is largely a modification that occurs at low stoichiometry at its target sites. Here we describe a method to identify lysine acetylation sites and estimate their site occupancy at the proteome scale. The method relies on a high-resolution mass spectrometry-based proteomics approach, which includes a specific chemical acetylation reaction on unmodified lysine residues that carry heavy isotopes. The procedures described here have been applied to cell line cultures and to clinically relevant samples stored as both snap-frozen and formalin-fixed paraffin-embedded (FFPE) tissues.

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Please use this url to cite or link to this publication:
author
and
organization
publishing date
type
Chapter in Book/Report/Conference proceeding
publication status
published
subject
keywords
Cell lines, FFPE tissue, Frozen tissue, Lysine acetylation, Mass spectrometry-based proteomics, N-acetoxysuccinimide-d3, Stoichiometry
host publication
Methods in Molecular Biology
series title
Methods in Molecular Biology
volume
2420
pages
14 pages
publisher
Humana Press
external identifiers
  • pmid:34905167
  • scopus:85121709547
ISSN
1064-3745
1940-6029
DOI
10.1007/978-1-0716-1936-0_7
language
English
LU publication?
yes
id
25eaed71-39ec-4d69-be63-403d1212d6e3
date added to LUP
2022-03-04 08:55:44
date last changed
2024-06-16 10:24:06
@inbook{25eaed71-39ec-4d69-be63-403d1212d6e3,
  abstract     = {{<p>Lysine acetylation is a widespread posttranslational modification (PTM) in all kingdoms of live. A large number of proteins involved in most of biological pathways are targets of this PTM. The lysine acetylation is a reversible modification controlled by two main groups of enzymes, lysine acetyltransferases responsible for transferring the acetyl group of acetylCoA to the side chain of lysine residues and lysine deacetylases which effectively remove the acetyl tag. Dysregulation of enzymes that control acetylation and/or target proteins have been associated with a growing number of human pathologies. Lysine acetylation is largely a modification that occurs at low stoichiometry at its target sites. Here we describe a method to identify lysine acetylation sites and estimate their site occupancy at the proteome scale. The method relies on a high-resolution mass spectrometry-based proteomics approach, which includes a specific chemical acetylation reaction on unmodified lysine residues that carry heavy isotopes. The procedures described here have been applied to cell line cultures and to clinically relevant samples stored as both snap-frozen and formalin-fixed paraffin-embedded (FFPE) tissues.</p>}},
  author       = {{Gil, Jeovanis and Encarnación-Guevara, Sergio}},
  booktitle    = {{Methods in Molecular Biology}},
  issn         = {{1064-3745}},
  keywords     = {{Cell lines; FFPE tissue; Frozen tissue; Lysine acetylation; Mass spectrometry-based proteomics; N-acetoxysuccinimide-d3; Stoichiometry}},
  language     = {{eng}},
  pages        = {{73--86}},
  publisher    = {{Humana Press}},
  series       = {{Methods in Molecular Biology}},
  title        = {{Lysine Acetylation Stoichiometry Analysis at the Proteome Level}},
  url          = {{http://dx.doi.org/10.1007/978-1-0716-1936-0_7}},
  doi          = {{10.1007/978-1-0716-1936-0_7}},
  volume       = {{2420}},
  year         = {{2022}},
}