A hydroxylamine probe for profiling S-acylated fatty acids on proteins. Issue 75 (29th August 2019)

• Record Type: Journal Article
• Authors: Schulte-Zweckel, Janine; Dwivedi, Mridula; Brockmeyer, Andreas; Janning, Petra; Winter, Roland; Triola, Gemma
• Is Part Of: Chemical communications. Volume 55:Issue 75(2019)
• Page Start: 11183
• Page End: 11186
• Publication Date: 2019-08-29
• Subjects: Chemistry -- Periodicals; 540
• DOI: 10.1039/c9cc05989j
• Languages: English
• ISSNs: 1359-7345

Abstract

Abstract : An hydroxylamine probe combined with mass spectrometry analysis enable accurate identification of fatty acids in S -acylated proteins. Abstract : Reversible S -palmitoylation is a key regulatory mechanism of protein function and localization. There is increasing evidence that S -acylation is not restricted to palmitate but it includes shorter, longer, and unsaturated fatty acids. However, the diversity of this protein modification has not been fully explored. Herein, we report a chemical probe that combined with MS-based analysis allows the rapid detection and quantification of fatty acids linked to proteins. We have used this approach to profile the S -acylome and to show that the oncogene N-Ras is heterogeneously acylated with palmitate and palmitoleate. Studies on protein distribution in membrane subdomains with semisynthetic proteins revealed that unsaturated N-Ras presents an increased tendency toward clustering and higher insertion kinetic rate constants.