ArticleThe Journal of biological chemistry2008
Turnover of endogenous SsrA-tagged proteins mediated by ATP-dependent proteases in Escherichia coli.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed, 99 citations in OpenAlex.
- Targeted Regulation of Protein Expression inBiology · 2026Article
- Approaches to Study Proteins Encoded by Essential Genes.Proteins · 2026Review
- Engineering a New SsrA-Based Degradation Tag (LAA-LAA) and a Bacterial Synthetic Oscillator.ACS synthetic biology · 2025Article
- Toxin-based screening of C-terminal tags inbioRxiv : the preprint server for biology · 2024Article
- Light-inducible protein degradation ineLife · 2024Article
- RNA-seq reveals multifaceted gene expression response to Fab production in Escherichia coli fed-batch processes with particular focus on ribosome stalling.Microbial cell factories · 2024Article
- ClpX/P-Dependent Degradation of Novel Substrates in Streptococcus mutans.Journal of bacteriology · 2022Article
- Protein quality control and regulated proteolysis in the genome-reduced organism Mycoplasma pneumoniae.Molecular systems biology · 2020Article
- Multiple domains of bacterial and human Lon proteases define substrate selectivity.Emerging microbes & infections · 2018Article
- Regulated Proteolysis in Bacteria.Annual review of biochemistry · 2018Review
- Targeting the Proteostasis Network for Mycobacterial Drug Discovery.ACS infectious diseases · 2018Review
- Temporal Proteomics of Inducible RNAi Lines of Clp Protease Subunits Identifies Putative Protease Substrates.Plant physiology · 2018Article
- Role of Heat Shock Proteases in Quorum-Sensing-Mediated Regulation of Biofilm Formation bymBio · 2018Article
- The Proteasomal ATPases Use a Slow but Highly Processive Strategy to Unfold Proteins.Frontiers in molecular biosciences · 2017Article
- Identification of New Degrons inFrontiers in microbiology · 2017Article
- The Potential Link between Thermal Resistance and Virulence inFrontiers in veterinary science · 2017Review
- The AAA+ FtsH Protease Degrades an ssrA-Tagged Model Protein in the Inner Membrane of Escherichia coli.Biochemistry · 2016Article
- ClpXP and ClpAP control the Escherichia coli division protein ZapC by proteolysis.Microbiology (Reading, England) · 2016Article
- The ssrA-Tag Facilitated Degradation of an Integral Membrane Protein.Biochemistry · 2016Article
- Inactivation of Cell Division Protein FtsZ by SulA Makes Lon Indispensable for the Viability of a ppGpp0 Strain of Escherichia coli.Journal of bacteriology · 2015Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Formation and degradation of SsrA-tagged proteins enable ribosome recycling and elimination of defective products of incomplete translation. We produced an antibody against the SsrA peptide and used it to measure the amounts of SsrA-tagged proteins in Escherichia coli cells without interfering with tagging or altering the context of the tag added at the ends of nascent polypeptides. SsrA-tagged proteins were present in very small amounts unless a component of the ClpXP protease was missing. From the levels of tagged proteins in cells in which degradation is essentially blocked, we calculate that > or =1 in 200 translation products receives an SsrA tag. ClpXP is responsible for > or =90% of the degradation of SsrA-tagged proteins. The degradation rate in wild type cells is > or =1.4 min(-1) and decreases to approximately 0.10 min(-1) in a clpX mutant. The rate of degradation by ClpXP is decreased approximately 3-fold in mutants lacking the adaptor SspB, whereas degradation by ClpAP is increased 3-5-fold. However, ClpAP degrades SsrA-tagged proteins slowly even in the absence of SspB, possibly because of interference from ClpA-specific substrates. Lon protease degrades SsrA-tagged proteins at a rate of approximately 0.05 min(-1) in the presence or absence of SspB. We conclude that ClpXP, together with SspB, is uniquely adapted for degradation of SsrA-tagged proteins and is responsible for the major part of their degradation in vivo.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.