Histone acetylation in gene regulation | Zendy

Loredana Verdone | Zendy

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Histone acetylation in gene regulation

Author(s) -

Loredana Verdone

Publication year - 2006

Publication title -

briefings in functional genomics and proteomics

Language(s) - English

Resource type - Journals

eISSN - 1477-4062

pISSN - 1473-9550

DOI - 10.1093/bfgp/ell028

Subject(s) - biology , acetylation , histone , histone modifying enzymes , histone h2a , histone code , nucleoprotein , chromatin , histone methyltransferase , sap30 , microbiology and biotechnology , computational biology , genetics , biochemistry , gene , nucleosome

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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