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Updated: Jun 17, 2026

A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli
Published on: December 9, 2017
The emerging role of lysine acetylation of non-nuclear proteins
Pierre Close1, Catherine Creppe, Magali Gillard
1Interdisciplinary Cluster for Applied Genoproteomics (GIGA-R), University of Liège, CHU Sart-Tilman, Liège, Belgium.
Abstract:
Lysine acetylation is a post-translational modification that critically regulates gene transcription by targeting histones as well as a variety of transcription factors in the nucleus. More recent reports have also demonstrated that numerous proteins located outside the nucleus are also acetylated and that this modification has profound consequences on their functions. This review describes the latest findings on the substrates acetylated outside the nucleus and on the acetylases and deacetylates that catalyse these modifications. Protein acetylation is emerging as a major mechanism by which key proteins are regulated in many physiological processes such as migration, metabolism and aging as well as in pathological circumstances such as cancer and neurodegenerative disorders.
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