Communication

Conversion of Cysteine into Dehydroalanine Enables Access to Synthetic Histones Bearing Diverse Post-Translational Modifications†

  1. Justin M. Chalker,
  2. Lukas Lercher,
  3. Dr. Nathan R. Rose,
  4. Prof. Christopher J. Schofield,
  5. Prof. Benjamin G. Davis*

Article first published online: 13 JAN 2012

DOI: 10.1002/anie.201106432

Issue

Angewandte Chemie International Edition

Angewandte Chemie International Edition

Volume 51, Issue 8, pages 1835–1839, February 20, 2012

Additional Information

How to Cite

Chalker, J. M., Lercher, L., Rose, N. R., Schofield, C. J. and Davis, B. G. (2012), Conversion of Cysteine into Dehydroalanine Enables Access to Synthetic Histones Bearing Diverse Post-Translational Modifications. Angew. Chem. Int. Ed., 51: 1835–1839. doi: 10.1002/anie.201106432

Author Information

  1. Department of Chemistry, University of Oxford, Chemistry Research Laboratory, Mansfield Road, OX1 3TA (UK)

*Department of Chemistry, University of Oxford, Chemistry Research Laboratory, Mansfield Road, OX1 3TA (UK)

  1. †

    The authors thank the Rhodes Trust, US NSF (J.M.C.); Cancer Research UK, EPSRC (L.L.); the Commonwealth Scholarship Commission, the Wellcome Trust (N.R.R.); Wellcome Trust, EU, BBSRC (C.J.S.); BBSRC, EPSRC (B.G.D.). B.G.D. is a recipient of a Royal Society Wolfson Research Merit Award. We thank Dr. Rob Klose (Biochemistry, Oxford) for H3-encoding plasmids.

Publication History

  1. Issue published online: 14 FEB 2012
  2. Article first published online: 13 JAN 2012
  3. Manuscript Revised: 15 NOV 2011
  4. Manuscript Received: 11 SEP 2011

Funded by

  • Rhodes Trust
  • US NSF
  • Cancer Research UK
  • EPSRC
  • Commonwealth Scholarship Commission
  • Wellcome Trust
  • Wellcome Trust, EU
  • BBSRC

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Keywords:

  • chromatin;
  • enzymes;
  • histone;
  • phosphorylation;
  • protein modifications;
  • synthetic biology
Thumbnail image of graphical abstract

Six for the price of one: From a single precursor, dehydroalanine, six distinct post-translational modifications can be site-selectively installed on histone proteins (see figure), including the first site-selective phosphorylation and glycosylation of histones. Direct observation of histone deacetylase activity on a full-length modified histone as well as its interactions with both chromatin reader and writer/eraser proteins are reported.

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