Lysine Acetylation Stoichiometry Analysis at the Proteome Level

Jeovanis Gil, Sergio Encarnación-Guevara

Forskningsoutput: Kapitel i bok/rapport/Conference proceedingKapitel samlingsverkForskningPeer review

Sammanfattning

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.

Originalspråkengelska
Titel på värdpublikationMethods in Molecular Biology
FörlagHumana Press
Sidor73-86
Antal sidor14
DOI
StatusPublished - 2022

Publikationsserier

NamnMethods in Molecular Biology
Volym2420
ISSN (tryckt)1064-3745
ISSN (elektroniskt)1940-6029

Ämnesklassifikation (UKÄ)

  • Biokemi och molekylärbiologi

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