RpoS proteolysis is controlled directly by ATP levels in Escherichia coli
Name
Baker_Rpos proteolysis.pdf
Size
908.42 KB
Format
Adobe PDF
Checksum (MD5)
74c0909927df8d34dac04452f42cad42
Author(s)
Peterson, Celeste N.
Levchenko, Igor
Baker, Tania
Rabinowitz, Joshua D.
Silhavy, Thomas J.
Date Issued
March 2012
Journal
Genes & Development
Publisher
Cold Spring Harbor Laboratory Press
Citation
Peterson, C. N., I. Levchenko, J. D. Rabinowitz, T. A. Baker, and T. J. Silhavy. “RpoS Proteolysis Is Controlled Directly by ATP Levels in Escherichia Coli.” Genes & Development 26, no. 6 (March 15, 2012): 548–553. Copyright © 2012 by Cold Spring Harbor Laboratory Press
Version
Final published version
Abstract
The master regulator of stationary phase in Escherichia coli, RpoS, responds to carbon availability through changes in stability, but the individual steps in the pathway are unknown. Here we systematically block key steps of glycolysis and the citric acid cycle and monitor the effect on RpoS degradation in vivo. Nutrient upshifts trigger RpoS degradation independently of protein synthesis by activating metabolic pathways that generate small energy molecules. Using metabolic mutants and inhibitors, we show that ATP, but not GTP or NADH, is necessary for RpoS degradation. In vitro reconstitution assays directly demonstrate that ClpXP fails to degrade RpoS, but not other proteins, at low ATP hydrolysis rates. These data suggest that cellular ATP levels directly control RpoS stability.
MIT Department
Massachusetts Institute of Technology. Department of Biology
Massachusetts Institute of Technology. School of Science
Terms of Use
Creative Commons Attribution‐NonCommercial License
Persistent DSpace Link
DOI of Published Version
https://doi.org/10.1101/gad.183517.111
