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Related Concept Videos

Histone Modification02:32

Histone Modification

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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
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone...
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Chemical tools for probing histidine modifications.

Nurgül Bilgin1, Jordi C J Hintzen2, Jasmin Mecinović1

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

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Summary

This review explores chemical tools for studying histidine, a vital amino acid in proteins. It highlights histidine analogues and bioconjugation methods for understanding its modifications and functions.

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Area of Science:

  • Biochemistry
  • Chemical Biology
  • Proteomics

Background:

  • Histidine is a crucial amino acid involved in protein structure, metal ion binding, and enzyme catalysis.
  • Histidine residues undergo various posttranslational modifications (PTMs) like methylation, phosphorylation, and hydroxylation, mediated by newly identified enzymes.

Purpose of the Study:

  • To review the development of chemical tools for investigating histidine's roles in biological systems.
  • To spotlight the use of histidine analogues in studying PTMs of histidine residues.
  • To highlight novel bioconjugation techniques for selective modification of histidine in peptides and proteins.

Main Methods:

  • Development and application of chemical tools and histidine analogues.
  • Utilizing bioconjugation strategies for chemoselective protein modification.
  • Reviewing recent literature on histidine modification enzymes and their characterization.

Main Results:

  • Chemical tools and analogues provide insights into histidine's function and PTMs.
  • Bioconjugation methods enable precise modification of histidine residues in complex biological settings.
  • Recent advances have led to the identification and characterization of novel histidine-modifying enzymes.

Conclusions:

  • Chemical approaches are essential for elucidating the complex roles of histidine and its modifications in proteins.
  • Histidine analogues and advanced bioconjugation techniques offer powerful strategies for future research in chemical biology and proteomics.
  • Continued development of chemical tools will advance our understanding of histidine-mediated biological processes.