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Related Experiment Videos

Acetylation: a regulatory modification to rival phosphorylation?

T Kouzarides1

  • 1Wellcome/CRC Institute, Department of Pathology, Cambridge University, Tennis Court Road, Cambridge CB2 1QR, UK. tk106@mole.bio.cam.ac.uk

The EMBO Journal
|March 16, 2000
PubMed
Summary

Histone acetylation, a modification known for decades, is now understood to regulate diverse protein functions. This review compares acetylation with phosphorylation, exploring their similarities and differences.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Epigenetics

Background:

  • Histone acetylation has been known for nearly 30 years.
  • Recent discoveries reveal enzymes regulating histone acetylation impact broader cellular functions.
  • Acetylases modify various proteins beyond histones, including transcription factors and alpha-tubulin.

Purpose of the Study:

  • To review the broader substrate specificity and regulation of acetylases.
  • To compare histone acetylation with phosphorylation, exploring analogies and differences.
  • To highlight the signaling role of acetylation through structures like bromodomains.

Main Methods:

  • Literature review of histone acetylation and acetylase function.
  • Comparative analysis of acetylation and phosphorylation mechanisms.

Related Experiment Videos

  • Discussion of conserved domains involved in recognizing acetylated residues.

    • Main Results:

    • Acetylases target a wider range of proteins, influencing DNA recognition, protein interactions, and stability.
    • Bromodomains act as conserved signaling modules recognizing acetylated residues.
    • Acetylation shares functional and regulatory parallels with phosphorylation.

    Conclusions:

    • Histone acetylation is a dynamic regulatory mechanism with broad implications.
    • Acetylation represents a modification analogous to phosphorylation in many aspects.
    • Understanding acetylation is crucial for deciphering complex cellular signaling pathways.