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Review
. 2025:75:3-24.
doi: 10.1007/978-3-031-91459-1_1.

Histone and Non-histone Reversible Acetylation in Development, Aging, and Disease

Sezgin Gunes  1   2 , Neslihan Hekim  3 , Sercan Ergun  3 , Elzem Nisa Alkan  3 , Cansu Can  3
Affiliations
Review

Histone and Non-histone Reversible Acetylation in Development, Aging, and Disease

Sezgin Gunes et al. Results Probl Cell Differ. 2025.

Abstract

Post-translational modifications (PTM) involve chemical modifications of amino acid residues within histone and non-histone proteins and are chemically diverse. PTM plays a vital role in regulating the chromatin structure in the nucleus, thus gene regulation. Among the various PTM, reversible acetylation of histone non-histone proteins has fundamental functions in various cellular processes. In all organisms, histone acetylation of lysine residues is connected with transcription activation. Acetyltransferases and deacetylases are well-known enzymes in the acetylation of the histone and non-histone proteins. This chapter will review the latest progress in histone and non-histone reversible acetylation epigenetic alterations and mechanisms and summarize how they affect development, aging, and diseases.

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References

    1. Agis-Balboa RC, Pavelka Z, Kerimoglu C, Fischer A (2013) Loss of HDAC5 impairs memory function: implications for Alzheimer’s disease. J Alzheimers Dis 33(1):35–44 - PubMed - DOI
    1. Allfrey VG, Faulkner R, Mirsky AE (1964) Acetylation and methylation of histones and their possible role in the regulation of RNA synthesis. Proc Natl Acad Sci USA 51(5):786–794 - PubMed - PMC - DOI
    1. Aricthota S, Rana PP, Haldar D (2022) Histone acetylation dynamics in repair of DNA double-strand breaks. Front Genet 13:926577 - PubMed - PMC - DOI
    1. Ashton AW, Dhanjal HK, Rossner B, Mahmood H, Patel VI, Nadim M et al (2024) Acetylation of nuclear receptors in health and disease: an update. FEBS J 291(2):217–236 - PubMed - DOI
    1. Batta K, Das C, Gadad S, Shandilya J, Kundu TK (2007) Reversible acetylation of non histone proteins: role in cellular function and disease. Chromatin Dis:193–214

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