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J Am Chem Soc. 2010 Jul 28;132(29):9986-7. doi: 10.1021/ja103954u.

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

Author information

1
Department of Pharmacology and Molecular Sciences, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA.

Abstract

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 site-specifically 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.

PMID:
20608637
PMCID:
PMC2912447
DOI:
10.1021/ja103954u
[Indexed for MEDLINE]
Free PMC Article

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