Analysis of Degradation of Metabolic Proteins during Starvation

Abstract

When E. coli cells become starved for glucose, degradation of the stationary phase master regulator RpoS by the protease ClpXP ceases. However it unknown how other proteins in the cell are also affected by differential degradation by ClpXP. While many studies have examined how gene expression changes during starvation, fewer studies have identified changes in protein degradation in this condition. We used a ClpPtrap, which recognizes and unfolds ClpP substrates but does not release them to monitor substrate selection during starvation conditions. We then further analyzed candidates by Western blot analysis. Numerous differentially regulated substrates were involved in metabolism as well as protein synthesis and other processes such as replication. Many of these substrates had ClpX tags on their N or C termini. Thus changes in protein stability of metabolic and other proteins may be a more general way that cells alter their proteome during starvation.This abstract is from the Experimental Biology 2018 Meeting. There is no full text article associated with this abstract published in The FASEB Journal.