Please use this identifier to cite or link to this item: http://hdl.handle.net/2381/44531
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dc.contributor.authorBarnes, Claire E.-
dc.contributor.authorEnglish, David M.-
dc.contributor.authorCowley, Shaun M.-
dc.date.accessioned2019-06-20T12:33:03Z-
dc.date.available2019-06-20T12:33:03Z-
dc.date.issued2019-04-02-
dc.identifier.citationEssays in Biochemistry, 2019, 63(1), pp. 97-107en
dc.identifier.urihttp://essays.biochemistry.org/content/63/1/97en
dc.identifier.urihttp://hdl.handle.net/2381/44531-
dc.description.abstractPackaging the long and fragile genomes of eukaryotic species into nucleosomes is all well and good, but how do cells gain access to the DNA again after it has been bundled away? The solution, in every species from yeast to man, is to post-translationally modify histones, altering their chemical properties to either relax the chromatin, label it for remodelling or make it more compact still. Histones are subject to a myriad of modifications: acetylation, methylation, phosphorylation, ubiquitination etc. This review focuses on histone acylations, a diverse group of modifications which occur on the ε-amino group of Lysine residues and includes the well-characterised Lysine acetylation. Over the last 50 years, histone acetylation has been extensively characterised, with the discovery of histone acetyltransferases (HATs) and histone deacetylases (HDACs), and global mapping experiments, revealing an association of hyperacetylated histones with accessible, transcriptionally active chromatin. More recently, there has been an explosion in the number of unique short chain 'acylations' identified by MS, including: propionylation, butyrylation, crotonylation, succinylation, malonylation and 2-hydroxyisobutyrylation. These novel modifications add a range of chemical environments to histones, and similar to acetylation, appear to accumulate at transcriptional start sites and correlate with gene activity.en
dc.description.sponsorshipThis work was supported by Studentships from BBSRC-MIBTP (to C.E.B) and MRC-IMPACT Ph.D. (D.M.E) programmes respectively; a senior non-clinical fellowship from MRC [grant number MR/J009202/1 (to S.M.C.)]; and BBSRC project grants [grant numbers BB/N002954/1, BB/P021689/1 (to S.M.C.)]en
dc.language.isoenen
dc.publisherPortland Press for Biochemical Societyen
dc.relation.urihttps://www.ncbi.nlm.nih.gov/pubmed/30940741-
dc.rightsCopyright © the authors, 2019. This is an open-access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.en
dc.subjectAcetylationen
dc.subjectChromatinen
dc.subjectHistoneen
dc.subjectTranscriptionen
dc.titleAcetylation & Co: an expanding repertoire of histone acylations regulates chromatin and transcription.en
dc.typeJournal Articleen
dc.identifier.doi10.1042/EBC20180061-
dc.identifier.eissn1744-1358-
dc.identifier.piiEBC20180061-
dc.description.statusPeer-revieweden
dc.description.versionPublisher Versionen
dc.type.subtypeJournal Article;Review-
pubs.organisational-group/Organisationen
pubs.organisational-group/Organisation/COLLEGE OF LIFE SCIENCESen
pubs.organisational-group/Organisation/COLLEGE OF LIFE SCIENCES/Biological Sciencesen
pubs.organisational-group/Organisation/COLLEGE OF LIFE SCIENCES/Biological Sciences/Molecular & Cell Biologyen
dc.dateaccepted2019-03-12-
Appears in Collections:Published Articles, Dept. of Molecular and Cell Biology

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