ArticleJournal of bacteriology2009
ClpXP degrades SsrA-tagged proteins in Streptococcus pneumoniae.
Article in Journal of bacteriology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 17 citations in OpenAlex.
- The ClpA chaperone and the two adaptor proteins modulate the fate of the model substrate tagged with a SsrA-degron of Leptospira.The Biochemical journal · 2025Article
- Recent Advances in the Structural Studies of the Proteolytic ClpP/ClpX Molecular Machine.Biomolecules · 2025Review
- Easy-Curing and pH-Regulated CRISPR-Cas9 Plasmids for Gene Editing and Plasmid Curing in Lactococcus cremoris.Microbial biotechnology · 2024Article
- Bacterial degrons in synthetic circuits.Open biology · 2022Review
- Improving the Robustness of Engineered Bacteria to Nutrient Stress Using Programmed Proteolysis.ACS synthetic biology · 2022Article
- Multiple domains of bacterial and human Lon proteases define substrate selectivity.Emerging microbes & infections · 2018Article
- Identification of New Degrons inFrontiers in microbiology · 2017Article
- Degradation of SsrA-tagged proteins in streptococci.Microbiology (Reading, England) · 2015Article
- Competence in Streptococcus pneumoniae is a response to an increasing mutational burden.PloS one · 2013Article
- Mycobacterium tuberculosis ClpP proteases are co-transcribed but exhibit different substrate specificities.PloS one · 2013Article
- Competence in Streptococcus pneumoniae is regulated by the rate of ribosomal decoding errors.mBio · 2011Article
- ClpP of Streptococcus mutans differentially regulates expression of genomic islands, mutacin production, and antibiotic tolerance.Journal of bacteriology · 2010Article
- spr1630 is responsible for the lethality of clpX mutations in Streptococcus pneumoniae.Journal of bacteriology · 2009Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacterial proteins that are abnormally truncated due to incomplete mRNA or the presence of rare codons are extended by an SsrA tag during ribosome rescue in a trans-translation process important for maintaining protein quality. In Escherichia coli, the SsrA-tagged proteins become the target of the Tsp, Lon, FtsH, ClpXP, and ClpAP proteases. Here we show that degradation of model SsrA-tagged proteins in Streptococcus pneumoniae depends primarily or exclusively on ClpXP in vivo. In addition, we show the E. coli SsrA tag is also a target of S. pneumoniae ClpXP in vivo, even though the N-terminal portions of the tags differ significantly between the two species, suggesting there may be no adaptor protein for SsrA in S. pneumoniae.
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Registered trials
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.