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Updated: Jun 30, 2026

A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli
11:08

A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli

Published on: December 9, 2017

Acetylation of non-histone proteins modulates cellular signalling at multiple levels

Stephanie Spange1, Tobias Wagner, Thorsten Heinzel

  • 1Leibniz Institute for Age Research - Fritz Lipmann Institute, Beutenbergstrasse 11, 07745 Jena, Germany. spange@fli-leibniz.de

The International Journal of Biochemistry & Cell Biology
|September 23, 2008
PubMed

Insights

Posttranslational acetylation of non-histone proteins regulates gene expression, protein function, and cellular processes. This dynamic modification is crucial in cancer and immune responses, highlighting histone deacetylase inhibitors as potential cancer therapies.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Epigenetics

Background:

  • Posttranslational acetylation of non-histone proteins is a vital regulatory mechanism.
  • Histone acetyltransferases and deacetylases dynamically regulate genes controlling cell proliferation and differentiation.
  • Reversible lysine acetylation impacts mRNA stability, protein localization, interaction, degradation, and function.

Purpose of the Study:

  • To review the complex effects of dynamic alterations in the cellular acetylome on physiologically relevant pathways.
  • To highlight the role of non-histone protein acetylation in tumorigenesis, cancer cell proliferation, and immune functions.
  • To discuss the therapeutic potential of histone deacetylase inhibitors in cancer treatment.

Main Methods:

  • Literature review focusing on posttranslational acetylation of non-histone proteins.
  • Analysis of identified acetylated non-histone proteins and their functions.
  • Examination of the role of histone deacetylase inhibitors in modulating gene expression and protein acetylation.

Main Results:

  • A growing number of non-histone proteins are identified as targets of acetylation.
  • Acetylation significantly affects protein stability, localization, and function.
  • Non-histone protein acetylation is implicated in cancer development and immune responses.

Conclusions:

  • Dynamic alterations in the cellular acetylome play critical roles in various physiological pathways.
  • Histone deacetylase inhibitors show promise as anti-cancer agents by modulating both histone and non-histone protein acetylation.
  • Further research into the non-histone acetylome is essential for understanding disease mechanisms and developing novel therapies.

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