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SET domain-mediated lysine methylation in lower organisms regulates growth and transcription in hosts

Nwasike, C; Ewert, S; Jovanovic, S; Haider, S; Mujtaba, S; (2016) SET domain-mediated lysine methylation in lower organisms regulates growth and transcription in hosts. Annals of the New York Academy of Sciences: Special Issue - Marrow , 1376 pp. 18-28. 10.1111/nyas.13017. Green open access

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Abstract

Su(var)3-9, Enhancer-of-zeste, Trithorax (SET) domain–mediated lysine methylation, one of the major epigenetic marks, has been found to regulate chromatin-mediated gene transcription. Published studies have established further that methylation is not restricted to nuclear proteins but is involved in many cellular processes, including growth, differentiation, immune regulation, and cancer progression. The biological complexity of lysine methylation emerges from its capacity to cause gene activation or gene repression owing to the specific position of methylated-lysine moieties on the chromatin. Accumulating evidence suggests that despite the absence of chromatin, viruses and prokaryotes also express SET proteins, although their functional roles remain relatively less investigated. One possibility could be that SET proteins in lower organisms have more than one biological function, for example, in regulating growth or in manipulating host transcription machinery in order to establish infection. Thus, elucidating the role of an SET protein in host–pathogen interactions requires a thorough understanding of their functions. This review discusses the biological role of lysine methylation in prokaryotes and lower eukaryotes, as well as the underlying structural complexity and functional diversity of SET proteins.

Type: Article
Title: SET domain-mediated lysine methylation in lower organisms regulates growth and transcription in hosts
Open access status: An open access version is available from UCL Discovery
DOI: 10.1111/nyas.13017
Publisher version: http://doi.org/10.1111/nyas.13017
Language: English
Additional information: © 2016 New York Academy of Sciences. This version is the author accepted manuscript. For information on re-use, please refer to the publisher’s terms and conditions.
Keywords: Science & Technology, Life Sciences & Biomedicine, Cell Biology, epigenetics, SET protein, methyltransferase, chromatin, histone proteins, lysine methylation, HISTONE H3, POSTTRANSLATIONAL MODIFICATIONS, STRUCTURAL BASIS, GENE-EXPRESSION, X-INACTIVATION, PROTEIN, METHYLTRANSFERASE, PROLIFERATION, ACETYLATION, SPECIFICITY
UCL classification: UCL
UCL > Provost and Vice Provost Offices
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > UCL School of Pharmacy
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > UCL School of Pharmacy > Pharma and Bio Chemistry
URI: https://discovery.ucl.ac.uk/id/eprint/1538315
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