Related Experiment Video
Updated: Dec 6, 2025

Author Spotlight: Developing Acetyl-Click Assay for HAT1 Inhibitor Screening
Published on: January 26, 2024
Recent insights into Histone Acetyltransferase-1: biological function and involvement in pathogenesis
Angelita Poziello1,2, Angela Nebbioso1, Hendrik G Stunnenberg2,3
1Department of Precision Medicine, University of Campania "Luigi Vanvitelli", Naples, Italy.
Abstract:
Acetylation of histone and non-histone proteins is a post-translational modification mostly associated with activation of gene transcription. The first histone acetyltransferase (HAT) identified as modifying newly synthesized histone H4 in yeast was a type B HAT named HAT1. Although it was the first HAT to be discovered, HAT1 remains one of the most poorly studied enzymes in its class. In addition to its well-established role in the cytoplasm, recent findings have revealed new and intriguing aspects of the function of HAT1 in the nucleus. Several studies have described its involvement in regulating different pathways associated with a wide range of diseases, including cancer. This review focuses on our current understanding of HAT1, highlighting its importance in regulating chromatin replication and gene expression. This previously unknown role for HAT1 opens up novel scenarios in which further studies will be required to better understand its function.
Related Concept Videos
Histone Modification
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone...
Histone Modification
Spreading of Chromatin Modifications
Writers
The writer...
Histone Variants at the Centromere
Chromatin Modification in iPS Cells
Compact chromatin makes reprogramming difficult. Enzymes, such as histone demethylases and acetyltransferases, are often added during reprogramming to loosen the chromatin, making the DNA more accessible to transcription factors. Molecules that inhibit histone...
Covalently Linked Protein Regulators
These groups modify specific amino acids in a protein....

