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Related Concept Videos

Histone Modification02:32

Histone Modification

15.1K
The histone proteins have a flexible N-terminal tail extending out from the nucleosome. These histone tails are often subjected to post-translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination. Particular combinations of these modifications form “histone codes” that influence the chromatin folding and tissue-specific gene expression.
Acetylation
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Spreading of Chromatin Modifications02:25

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The histone proteins in the nucleosomes are post-translationally modified (PTM) to increase or decrease access to DNA. The commonly observed PTMs are methylation, acetylation, phosphorylation, and ubiquitination of lysine amino acids in the histone H3 tail region. These histone modifications have specific meaning for the cell. Hence, they are called "histone code". The protein complex involved in histone modification is termed as "reader-writer" complex.
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Substrate Scope for Human Histone Lysine Acetyltransferase KAT8.

Giordano Proietti1,2, Yali Wang2,3, Chiara Punzo1

  • 1Department of Physics, Chemistry and Pharmacy, University of Southern Denmark, Campusvej 55, 5230 Odense, Denmark.

International Journal of Molecular Sciences
|January 20, 2021
PubMed
Summary

Histone acetyltransferase KAT8 acetylates lysine on proteins. This study shows human KAT8 can also acetylate lysine analogues, expanding its known substrate scope beyond natural lysine.

Keywords:
acetylationepigeneticshistonelysineposttranslational modifications

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Area of Science:

  • Biochemistry
  • Epigenetics
  • Enzymology

Background:

  • Histone acetylation is a key epigenetic modification regulating gene expression.
  • Histone lysine acetyltransferase KAT8 is a crucial enzyme involved in this process.
  • Understanding KAT8's substrate specificity is vital for its therapeutic targeting.

Purpose of the Study:

  • To investigate the substrate scope of human KAT8 beyond natural lysine.
  • To explore KAT8's ability to acetylate histone H4 peptides with lysine analogues at position 16 (H4K16).

Main Methods:

  • Utilized synthetic and enzymatic studies.
  • Employed chemically and structurally diverse lysine mimics.
  • Tested acetylation of histone H4 peptides with modified lysine residues.

Main Results:

  • Human KAT8 demonstrated the capacity to acetylate selected lysine analogues.
  • Acetylation occurred even with subtle side chain and main chain modifications.
  • KAT8's substrate scope extends beyond natural lysine residues.

Conclusions:

  • KAT8 exhibits a broader substrate specificity than previously known.
  • Findings contribute to the development of novel chemical probes for KAT8 and other KAT enzymes.
  • This research opens avenues for new epigenetic drug discovery.