Abstract 1865 Design of a Novel Bioluminescent Assay for Histone Acetyltransferase Activity and Discovery of the Novel Protein Post-Translational Modification, Lysine Isobutyrylation

Protein acetylation and short chain acylations are critical post-translational modifications (PTMs) widespread across the proteome of eukaryotes and prokaryotes. Histone acetyltransferase (HAT) enzymes are responsible for the catalytic addition of short-chain acyl groups to lysine residues on cellular proteins using several different acyl-coenzyme A molecules as cosubstrates for the reaction. HAT enzymes regulate important DNA-templated processes such as DNA replication, gene transcription, and chromatin assembly by depositing different acyl moieties to specific lysine residues of nucleosomal histones.

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Publication Details

Journal
Journal of Biological Chemistry
Published
2025-05-01
DOI
https://doi.org/10.1016/j.jbc.2025.109266
Primary Topic
Click Chemistry and Applications
Type
article
Field-Weighted Citation Impact
0.00

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Abstract 1865 Design of a Novel Bioluminescent Assay for Histone Acetyltransferase Activity and Discovery of the Novel Protein Post-Translational Modification, Lysine Isobutyrylation

Y. George Zheng, Zhesi Zhu, Nolan D. Swain
Journal of Biological Chemistry
Click Chemistry and Applications
article

Abstract 1865 Design of a Novel Bioluminescent Assay for Histone Acetyltransferase Activity and Discovery of the Novel Protein Post-Translational Modification, Lysine Isobutyrylation

Y. George Zheng, Zhesi Zhu, Nolan D. Swain
article en

Abstract

Protein acetylation and short chain acylations are critical post-translational modifications (PTMs) widespread across the proteome of eukaryotes and prokaryotes. Histone acetyltransferase (HAT) enzymes are responsible for the catalytic addition of short-chain acyl groups to lysine residues on cellular proteins using several different acyl-coenzyme A molecules as cosubstrates for the reaction. HAT enzymes regulate important DNA-templated processes such as DNA replication, gene transcription, and chromatin assembly by depositing different acyl moieties to specific lysine residues of nucleosomal histones.

Journal of Biological ChemistryVol. 301(5)
University of Georgia (US)
University of Pennsylvania, National Institutes of Health
Zero hunger
Openalex Percentile: Top 90%
Click Chemistry and Applications
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