Chemical Biology Interrogates Protein Arginine Phosphorylation. Issue 8 (18th August 2016)

• Record Type: Journal Article
• Authors: Suskiewicz, Marcin Józef; Clausen, Tim
• Is Part Of: Cell chemical biology. Volume 23:Issue 8(2016)
• Page Start: 888
• Page End: 890
• Publication Date: 2016-08-18
• Subjects: Biochemistry -- Periodicals; 572.05
• DOI: 10.1016/j.chembiol.2016.08.003
• Languages: English
• ISSNs: 2451-9456

Abstract

Abstract : Protein arginine phosphorylation has emerged as an important regulatory mechanism in Gram-positive bacteria, yet a couple of key mysteries remain. In this issue of Cell Chemical Biology, Fuhrmann et al. (2016) use activity-based probes to demonstrate that the protein arginine phosphatase YwlE is inactivated upon oxidative stress to unleash heat-shock gene expression. Abstract : Protein arginine phosphorylation has emerged as an important regulatory mechanism in Gram-positive bacteria, yet a couple of key mysteries remain. In this issue of Cell Chemical Biology, Fuhrmann et al. (2016) use activity-based probes to demonstrate that the protein arginine phosphatase YwlE is inactivated upon oxidative stress to unleash heat-shock gene expression.