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Site-Specific Introduction of an Acetyl-Lysine Mimic into Peptides and Proteins by Cysteine Alkylation

豆豆添加于 2011-7-5 09:15 | 825 次阅读 | 0 个评论

作者
Huang R, Holbert MA, Tarrant MK, Curtet S, Colquhoun DR, Dancy BM, Dancy BC, Hwang Y, Tang Y, Meeth K, Marmorstein R, Cole RN, Khochbin S, Cole PA
摘要

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.
详细资料
- 文献种类:期刊
- 期刊名称: Journal of the American Chemical Society
- 期刊缩写: J. Am. Chem. Soc.
- 期卷页: 2010年第132卷第29期 9986-9987页
- ISBN: 0002-7863
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附件
Site-Specific Introduction of an Acetyl-Lysine Mimic into Peptides and Proteins
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