Site-specific introduction of an acetyl-lysine mimic into peptides and proteins by cysteine alkylation

Rong Huang, Marc A. Holbert, Mary Katherine Tarrant, Sandrine Curtet, David R. Colquhoun, Beverley M. Dancy, Blair C. Dancy, Yousang Hwang, Yong Tang, Katrina Meeth, Ronen Marmorstein, Robert N. Cole, Saadi Khochbin, Philip A. Cole

Research output: Contribution to journalArticlepeer-review

77 Scopus citations


Protein acetylation on Lys residues is recognized as a significant post-translational modification in cells, but it is often difficult to discern the direct structural and functional effects of individual acetylation events. Here we describe a new tool, methylthiocarbonyl-aziridine, to install acetyl-Lys mimics sitespecifically into peptides and proteins by alkylation of Cys residues. We demonstrate that the resultant thiocarbamate modification can be recognized by the Brdt bromodomain and site-specific antiacetyl-Lys antibodies, is resistant to histone deacetylase cleavage, and can confer activation of the histone acetyltransferase Rtt109 by simulating autoacetylation. We also use this approach to obtain functional evidence that acetylation of CK2 protein kinase on Lys102 can stimulate its catalytic activity.

Original languageEnglish (US)
Pages (from-to)9986-9987
Number of pages2
JournalJournal of the American Chemical Society
Issue number29
StatePublished - Jul 28 2010

ASJC Scopus subject areas

  • Catalysis
  • General Chemistry
  • Biochemistry
  • Colloid and Surface Chemistry


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