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Investigating d-lysine stereochemistry for epigenetic methylation, demethylation and recognition.

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journal contribution
posted on 2019-06-14, 11:42 authored by R Belle, AHK Al Temimi, K Kumar, BJGE Pieters, A Tumber, JE Dunford, C Johansson, U Oppermann, T Brown, CJ Schofield, RJ Hopkinson, RS Paton, A Kawamura, J Mecinović
Histone lysine methylation is regulated by Nε-methyltransferases, demethylases, and Nε-methyl lysine binding proteins. Thermodynamic, catalytic and computational studies were carried out to investigate the interaction of three epigenetic protein classes with synthetic histone substrates containing l- and d-lysine residues. The results reveal that out of the three classes, Nε-methyl lysine binding proteins are superior in accepting lysines with the d-configuration.

Funding

This work was supported by the ERC Starting Grant to J. M. (ChemEpigen-715691) and to A. K. (EPITOOLS-679479), the Netherlands Organization for Scientific Research (NCI-TA 731.015.202), Royal Society Dorothy Hodgkin Fellowship (A. K.), the Wellcome Trust, Cancer Research UK, the Engineering & Physical Sciences Research Council UK, the John Fell Oxford University Press (OUP) Research Fund, and the NIHR Oxford Biomedical Research Unit. We gratefully acknowledge Dr D. McClymont for his support in developing the Matlab script.

History

Citation

Chemical Communications, 2017, 53 (99), pp. 13264-13267

Author affiliation

/Organisation/COLLEGE OF SCIENCE AND ENGINEERING/Department of Chemistry

Version

  • AM (Accepted Manuscript)

Published in

Chemical Communications

Publisher

Royal Society of Chemistry

eissn

1364-548X

Acceptance date

2017-11-23

Copyright date

2017

Available date

2019-06-14

Publisher version

https://pubs.rsc.org/en/content/articlelanding/2017/CC/C7CC08028J#!divAbstract

Notes

Electronic supplementary information (ESI) available: Supporting figures, enzyme assays, peptide synthesis, protein production, synthesis, NMR data. See DOI: 10.1039/c7cc08028j

Language

en