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      Substrate Scope for Human Histone Lysine Acetyltransferase KAT8

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          Abstract

          Biomedically important histone lysine acetyltransferase KAT8 catalyses the acetyl coenzyme A-dependent acetylation of lysine on histone and other proteins. Here, we explore the ability of human KAT8 to catalyse the acetylation of histone H4 peptides possessing lysine and its analogues at position 16 (H4K16). Our synthetic and enzymatic studies on chemically and structurally diverse lysine mimics demonstrate that KAT8 also has a capacity to acetylate selected lysine analogues that possess subtle changes on the side chain and main chain. Overall, this work highlights that KAT8 has a broader substrate scope beyond natural lysine, and contributes to the design of new chemical probes targeting KAT8 and other members of the histone lysine acetyltransferase (KAT) family.

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          Regulation of chromatin by histone modifications.

          Andrew Bannister, Tony Kouzarides (2011)
          Chromatin is not an inert structure, but rather an instructive DNA scaffold that can respond to external cues to regulate the many uses of DNA. A principle component of chromatin that plays a key role in this regulation is the modification of histones. There is an ever-growing list of these modifications and the complexity of their action is only just beginning to be understood. However, it is clear that histone modifications play fundamental roles in most biological processes that are involved in the manipulation and expression of DNA. Here, we describe the known histone modifications, define where they are found genomically and discuss some of their functional consequences, concentrating mostly on transcription where the majority of characterisation has taken place.
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            The language of covalent histone modifications.

            B. D. Strahl, C Allis (2000)
            Histone proteins and the nucleosomes they form with DNA are the fundamental building blocks of eukaryotic chromatin. A diverse array of post-translational modifications that often occur on tail domains of these proteins has been well documented. Although the function of these highly conserved modifications has remained elusive, converging biochemical and genetic evidence suggests functions in several chromatin-based processes. We propose that distinct histone modifications, on one or more tails, act sequentially or in combination to form a 'histone code' that is, read by other proteins to bring about distinct downstream events.
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              Erasers of histone acetylation: the histone deacetylase enzymes.

              Edward Seto, Minoru Yoshida (2014)
              Histone deacetylases (HDACs) are enzymes that catalyze the removal of acetyl functional groups from the lysine residues of both histone and nonhistone proteins. In humans, there are 18 HDAC enzymes that use either zinc- or NAD(+)-dependent mechanisms to deacetylate acetyl lysine substrates. Although removal of histone acetyl epigenetic modification by HDACs regulates chromatin structure and transcription, deacetylation of nonhistones controls diverse cellular processes. HDAC inhibitors are already known potential anticancer agents and show promise for the treatment of many diseases.
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                Author and article information

                Journal
                Journal ID (nlm-ta): Int J Mol Sci
                Journal ID (iso-abbrev): Int J Mol Sci
                Journal ID (publisher-id): ijms
                Title: International Journal of Molecular Sciences
                Publisher: MDPI
                ISSN (Electronic): 1422-0067
                Publication date (Electronic): 15 January 2021
                Publication date Collection: January 2021
                Volume: 22
                Issue: 2
                Electronic Location Identifier: 846
                Affiliations
                [1 ]Department of Physics, Chemistry and Pharmacy, University of Southern Denmark, Campusvej 55, 5230 Odense, Denmark; proietti@ 123456sdu.dk (G.P.); chiarapunzo.94@ 123456gmail.com (C.P.)
                [2 ]Institute for Molecules and Materials, Radboud University, Heyendaalseweg 135, 6525 AJ Nijmegen, The Netherlands; wangzhang4083@ 123456jlu.edu.cn
                [3 ]Department of Blood Transfusion, Jilin University, 126 Xiantai Street, Changchun 130033, China
                Author notes
                [* ]Correspondence: mecinovic@ 123456sdu.dk
                Author information
                https://orcid.org/0000-0001-7392-4712
                https://orcid.org/0000-0002-5559-3822
                Article
                Publisher ID: ijms-22-00846
                DOI: 10.3390/ijms22020846
                PMC ID: 7830570
                PubMed ID: 33467728
                SO-VID: a592cb72-676f-4cb6-b9bc-5680d10b213d
                Copyright © © 2021 by the authors.
                License:

                Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license ( http://creativecommons.org/licenses/by/4.0/).

                History
                Date received : 28 December 2020
                Date accepted : 13 January 2021
                Categories
                Subject: Article

                ScienceOpen disciplines: Molecular biology
                Keywords: acetylation,epigenetics,histone,lysine,posttranslational modifications
                Data availability:
                ScienceOpen disciplines: Molecular biology
                Keywords: acetylation, epigenetics, histone, lysine, posttranslational modifications

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