A genetically encoded 19F NMR probe for lysine acetylation. Issue 31 (29th March 2018)

• Record Type: Journal Article
• Authors: Zhang, Feng; Zhou, Qing; Yang, Guiwen; An, Liguo; Li, Fahui; Wang, Jiangyun
• Is Part Of: Chemical communications. Volume 54:Issue 31(2018)
• Page Start: 3879
• Page End: 3882
• Publication Date: 2018-03-29
• Subjects: Chemistry -- Periodicals; 540
• DOI: 10.1039/c7cc09825a
• Languages: English
• ISSNs: 1359-7345

Abstract

Abstract : An acetyllysine mimic (TFAcK) has been exploited for detecting the conformational changes of acetylated p53–protein/DNA interactions by genetic code expansion and 19 F NMR. Abstract : Advances in acetylated protein–protein/DNA interactions depend on the development of a novel NMR (nuclear magnetic resonance) probe to study the conformational changes of acetylated proteins. However, the method for detecting the acetylated protein conformation is underdeveloped. Herein, an acetyllysine mimic has been exploited for detecting the conformational changes of acetylated p53–protein/DNA interactions by genetic code expansion and 19 F NMR. This 19 F NMR probe shows high structural similarity to acetyllysine and could not be deacetylated by sirtuin deacetylase in vitro / vivo . Moreover, acetylation of p53 K164 is reported to be deacetylated by SIRT2 for the first time.