Author:
Zhang Fangrong,Kerbl-Knapp Jakob,Rodriguez Colman Maria J.,Macher Therese,Vujić Nemanja,Fasching Sandra,Jany-Luig Evelyne,Korbelius Melanie,Kuentzel Katharina B.,Mack Maximilian,Akhmetshina Alena,Paar Margret,Rinner Beate,Hörl Gerd,Steyrer Ernst,Stelzl Ulrich,Burgering Boudewijn,Eisenberg Tobias,Pertschy Brigitte,Kratky Dagmar,Madl Tobias
Abstract
SummaryQuantitative information about the levels and dynamics of post-translational modifications (PTMs) is critical for an understanding of cellular functions. Protein arginine methylation (ArgMet) is an important subclass of PTMs and is involved in a plethora of (patho)physiological processes. However, due to the lack of methods for global analysis of ArgMet, the link between ArgMet levels, dynamics and (patho)physiology remains largely unknown. We utilized the high sensitivity and robustness of Nuclear Magnetic Resonance (NMR) spectroscopy to develop a general method for the quantification of global protein ArgMet. Our NMR-based approach enables the detection of protein ArgMet in purified proteins, cells, organoids, and mouse tissues. We demonstrate that the process of ArgMet is a highly prevalent PTM and can be modulated by small-molecule inhibitors and metabolites and changes in cancer and during ageing. Thus, our approach enables to address a wide range of biological questions related to ArgMet in health and disease.Graphical Abstract
Publisher
Cold Spring Harbor Laboratory