Semisynthesis of Isomerized Histone H4 Reveals Robustness and Vulnerability of Chromatin toward Molecular Aging.

Tianze Zhang, Luis F Guerra, Yana Berlina, Jon R Wilson, Beat Fierz, Manuel M Müller

Department of Chemistry, King's College London, Britannia House, 7 Trinity Street, London SE1 1DB, U.K.Department of Chemistry, King's College London, Britannia House, 7 Trinity Street, London SE1 1DB, U.K. · pubmed

Paper

Abstract

Proteins are subject to aging in the form of spontaneous, nonenzymatic post-translational modifications (PTMs). One such PTM is the formation of the β-linked isomer l-isoaspartic acid (isoAsp) from aspartic acid (Asp) or asparagine residues, which tends to occur in long-lived proteins. Histones can exhibit half-lives on the order of 100 days, and unsurprisingly, isoAsp formation has been observed in nearly every histone family. Delineating the molecular consequences of isoAsp formation in histones is challenging due to the multitude of processes that occur on such time scales. To isolate the effects of a specific isoAsp modification thus necessitates precise

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Research summary

The paper claims that the formation of isoaspartic acid in histones affects chromatin stability and function. This research is relevant as it explores the molecular mechanisms of aging at the protein level, specifically focusing on post-translational modifications that could contribute to the aging process.

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