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Reduction in adaptor amounts establishes degradation hierarchy among protease substrates
- Publication Year :
- 2018
- Publisher :
- National Academy of Sciences, 2018.
-
Abstract
- ATP-dependent proteases control critical cellular processes, including development, physiology, and virulence. A given protease may recognize a substrate directly via an unfoldase domain or subunit or indirectly via an adaptor that delivers the substrate to the unfoldase. We now report that cells achieve differential stability among substrates of a given protease by modulating adaptor amounts. We establish that the regulatory protein PhoP represses transcription of the gene specifying the ClpAP protease adaptor ClpS when the bacteria Salmonella enterica and Escherichia coli experience low cytoplasmic Mg2+. The resulting decrease in ClpS amounts diminishes proteolysis of several ClpSAP-dependent substrates, including the putrescine aminotransferase Oat, which heightens the formation of antibiotic persisters, and the transcriptional regulators UvrY and PhoP, which alter the expression of genes controlled by these proteins. By contrast, the decrease in ClpS amounts did not impact the abundance of the ClpSAP substrate FtsA, reflecting that FtsA binds to ClpS more tightly than to UvrY and PhoP. Our findings show how physiological conditions that reduce adaptor amounts modify the abundance of selected substrates of a given protease.
- Subjects :
- 0301 basic medicine
Proteases
Protein subunit
medicine.medical_treatment
Proteolysis
Sequence Homology
medicine.disease_cause
Substrate Specificity
03 medical and health sciences
Bacterial Proteins
Transcription (biology)
Salmonella
medicine
Escherichia coli
Regulation of gene expression
Multidisciplinary
Protease
medicine.diagnostic_test
Base Sequence
Chemistry
Escherichia coli Proteins
Cell biology
030104 developmental biology
PNAS Plus
FtsA
Carrier Proteins
Subjects
Details
- Language :
- English
- Database :
- OpenAIRE
- Accession number :
- edsair.doi.dedup.....ca3263885cbd23771ac33ee6559d3f54