Phosphorylation And Acetylation In Action

Protein posttranslational modifications switch essential biological processes on and off, but tracking them in real time is a challenge. Now, researchers led by Philipp Selenko of the Leibniz Institute of Molecular Pharmacology, in Berlin, have developed a way to concurrently watch phosphorylations and acetylations take place (J. Am. Chem. Soc., DOI: 10.1021/ja106764y). The technique involves standard two-dimensional nuclear magnetic resonance spectroscopy and can be used for isotope-labeled proteins in solutions, as well as for cellular extracts. The reason both phosphorylation and acetylation can be observed simultaneously is that backbone amide group NMR signals shift when the posttranslational modification occurs. “This is an advance over mass spectrometry, the standard technique for studying posttranslational modifications, because modifications can be observed in real time, at atomic resolution, without having to purify the end mixture,” Selenko explains. MS can only detect the modifications after they have taken place.