Stable Histone Adduction by 4-Oxo-2-nonenal: A Potential Link between Oxidative Stress and Epigenetics | Zendy

James J. Galligan | Zendy; Kristie L. Rose | Zendy; William N. Beavers | Zendy; Salisha Hill | Zendy; Keri A. Tallman | Zendy; William P. Tansey | Zendy; Lawrence J. Marnett | Zendy

AI Assistant Blog Pricing

Home ZAIA Blog

Open Access

Stable Histone Adduction by 4-Oxo-2-nonenal: A Potential Link between Oxidative Stress and Epigenetics

Author(s) -

James J. Galligan,

Kristie L. Rose,

William N. Beavers,

Salisha Hill,

Keri A. Tallman,

William P. Tansey,

Lawrence J. Marnett

Publication year - 2014

Publication title -

journal of the american chemical society

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 7.115

H-Index - 612

eISSN - 1520-5126

pISSN - 0002-7863

DOI - 10.1021/ja503604t

Subject(s) - chemistry , histone , adduct , nucleosome , chromatin , epigenetics , electrophile , oxidative stress , stereochemistry , biochemistry , dna , gene , organic chemistry , catalysis

Lipid electrophiles modify cellular targets, altering their function. Here, we describe histones as major targets for modification by 4-oxo-2-nonenal, resulting in a stable Lys modification structurally analogous to other histone Lys acylations. Seven adducts were identified in chromatin isolated from intact cells: four 4-ketoamides to Lys and three Michael adducts to His. A 4-ketoamide adduct residing at H3K27 was identified in stimulated macrophages. Modification of histones H3 and H4 prevented nucleosome assembly.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.

Having issues? You can contact us here

Accelerating Research