Histone Acetylation in Gene Regulation

Overview

Journal Brief Funct Genomic Proteomic

Publisher Oxford University Press

Date 2006 Aug 1

PMID 16877467

Citations 100

Authors

Loredana Verdone

Eleonora Agricola

Micaela Caserta

Ernesto Di Mauro

Affiliations

Soon will be listed here.

Abstract

Genetic information is packaged in the highly dynamic nucleoprotein structure called chromatin. Many biological processes are regulated via post-translational modifications of key proteins. Acetylation of lysine residues at the N-terminal histone tails is one of the most studied covalent modifications influencing gene regulation in eukaryotic cells. This review focuses on the role of enzymes involved in controlling both histone and non-histone proteins acetylation levels in the cell, with particular emphasis on their effects on cancer.

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