Life and death of proteins: a case study of glucose-starved Staphylococcus aureus.

Molecular & Cellular Proteomics : MCP
Stephan MichalikMichael Hecker

Abstract

The cellular amount of proteins not only depends on synthesis but also on degradation. Here, we expand the understanding of differential protein levels by complementing synthesis data with a proteome-wide, mass spectrometry-based stable isotope labeling with amino acids in cell culture analysis of protein degradation in the human pathogen Staphylococcus aureus during glucose starvation. Monitoring protein stability profiles in a wild type and an isogenic clpP protease mutant revealed that 1) proteolysis mainly affected proteins with vegetative functions, anabolic and selected catabolic enzymes, whereas the expression of TCA cycle and gluconeogenesis enzymes increased; 2) most proteins were prone to aggregation in the clpP mutant; 3) the absence of ClpP correlated with protein denaturation and oxidative stress responses, deregulation of virulence factors and a CodY repression. We suggest that degradation of redundant, inactive proteins disintegrated from functional complexes and thereby amenable to proteolytic attack is a fundamental cellular process in all organisms to regain nutrients and guarantee protein homeostasis.

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Citations

Jan 21, 2014·International Journal of Medical Microbiology : IJMM·Andreas OttoDörte Becher
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Jun 29, 2021·Frontiers in Molecular Biosciences·Tatjana von RosenEilika Weber-Ban
Feb 12, 2017·Journal of Proteome Research·Joanna KrysiakStephan A Sieber

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