ArticleJournal of bacteriology2013
ClpL is required for folding of CtsR in Streptococcus mutans.
Article in Journal of bacteriology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
14 citing papers in PubMed, 29 citations in OpenAlex.
- Article
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- Persistence ofFoods (Basel, Switzerland) · 2022Article
- Significance of Individual Domains of ClpL: A Novel Chaperone fromBiochemistry · 2020Article
- The pneumococcal two-component system SirRH is linked to enhanced intracellular survival of Streptococcus pneumoniae in influenza-infected pulmonary cells.PLoS pathogens · 2020Article
- CtsR, the Master Regulator of Stress-Response inFrontiers in microbiology · 2018Article
- Engineered botulinum neurotoxin B with improved efficacy for targeting human receptors.Nature communications · 2017Article
- The SAV1322 gene from Staphylococcus aureus: genomic and proteomic approaches to identification and characterization of gene function.BMC microbiology · 2016Article
- Stress Physiology of Lactic Acid Bacteria.Microbiology and molecular biology reviews : MMBR · 2016Review
- Genomes of sequence type 121 Listeria monocytogenes strains harbor highly conserved plasmids and prophages.Frontiers in microbiology · 2015Article
- Regulated proteolysis of the alternative sigma factor SigX in Streptococcus mutans: implication in the escape from competence.BMC microbiology · 2014Article
- SMU.746-SMU.747, a putative membrane permease complex, is involved in aciduricity, acidogenesis, and biofilm formation in Streptococcus mutans.Journal of bacteriology · 2014Article
- Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
ClpL, a member of the HSP100 family, is widely distributed in Gram-positive bacteria but is absent in Gram-negative bacteria. Although ClpL is involved in various cellular processes, such as the stress tolerance response, long-term survival, virulence, and antibiotic resistance, the detailed molecular mechanisms are largely unclear. Here we report that ClpL acts as a chaperone to properly fold CtsR, a stress response repressor, and prevents it from forming protein aggregates in Streptococcus mutans. In vitro, ClpL was able to successfully refold urea-denatured CtsR but not aggregated proteins. We suggest that ClpL recognizes primarily soluble but denatured substrates and prevents the formation of large protein aggregates. We also found that in vivo, the C-terminal D2-small domain of ClpL is essential for the observed chaperone activity. Since ClpL widely contributes to various cellular functions, we speculate that ClpL chaperone activity is necessary to maintain cellular homeostasis.
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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.