03-31-2012

Reversible protein phosphorylation is an important and ubiquitous protein modification in all living cells. We report that protein arginine phosphorylation plays a physiological significant role for the regulation of protein activity. We detected 121 arginine phospho-sites for 87 proteins in the Gram-positive model organism Bacillus subtilis in vivo. Moreover, we provide evidences that arginine phosphorylations are involved in the fine-tuned signal transduction of many critical cellular processes, such as protein degradation, motility, competence, stringent and stress response. Our results suggest that in B. subtilis the activity of a protein arginine phosphatase allows a fast regulation of protein activity by protein arginine kinases and that protein arginine phosphorylations play an important role as a reversible post-translational modification in bacteria. Cells were grown under vigorous agitation at 37 °C in a defined medium (Stülke et al., 1993, J Gen Microbiol 139, 2041-2045). Samples were taken at OD500 0.4 and 1h upon entry into stationary phase. Microarray hybridizations were performed with RNA from three biological replicates. The individual samples were labeled with Cy5; a reference pool containing equal amounts of RNA from all 10 samples was labeled with Cy3.

not applicable

instance of dataset

E-GEOD-31249

raw

31249

functional genomics

05-02-2014

available

gene expression

Bacillus subtilis subsp. subtilis str. 168

A-GEOD-10901

B subtilis_Custom_Agilent 44k_v2

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Gene Expression Omnibus

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landing page

true

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EBI

SCR:004727

European Bioinformatics Institute

SCR:002964

ArrayExpress