Global Profiling of Sirtuin Deacylase Substrates Using a Chemical Proteomic Strategy and Validation by Fluorescent Labeling. Academic Article uri icon

Overview

abstract

  • Protein fatty-acylation is an important posttranslational modification (PTM) and has been associated with many fundamental biological processes. Sirtuins, the nicotinamide adenine dinucleotide (NAD)-dependent class of histone deacetylases have been reported to possess lysine defatty-acylase activity. Comprehensive substrate profiling of sirtuins will help to establish the function of both protein lysine fatty acylation and its regulation by sirtuins. Here, we describe a chemical proteomic strategy to globally profile sirtuin defatty-acylation substrates and a fluorescent labeling method to validate sirtuin substrates.

publication date

  • January 1, 2019

Research

keywords

  • Fluorescent Dyes
  • Protein Processing, Post-Translational
  • Proteomics
  • Sirtuins
  • Staining and Labeling

Identity

PubMed Central ID

  • PMC6893875

Scopus Document Identifier

  • 85066785353

Digital Object Identifier (DOI)

  • 10.7554/eLife.25158

PubMed ID

  • 31152401

Additional Document Info

volume

  • 2009