ArticleMicrobiology (Reading, England)2015
Degradation of SsrA-tagged proteins in streptococci.
Article in Microbiology (Reading, England), 2015. 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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Who cites it
14 citing papers in PubMed, 19 citations in OpenAlex.
- MecA: A Multifunctional ClpP-Dependent and Independent Regulator in Gram-Positive Bacteria.Molecular microbiology · 2025Review
- Engineering a New SsrA-Based Degradation Tag (LAA-LAA) and a Bacterial Synthetic Oscillator.ACS synthetic biology · 2025Article
- The final proteolytic step in transmembrane signaling of multiple RsgI anti-σ factors in Clostridium thermocellum.Bioscience reports · 2025Article
- Easy-Curing and pH-Regulated CRISPR-Cas9 Plasmids for Gene Editing and Plasmid Curing in Lactococcus cremoris.Microbial biotechnology · 2024Article
- Diverse nature of ClpX degradation motifs inMicrobiology spectrum · 2024Article
- Clp ATPases differentially affect natural competence development in Streptococcus mutans.MicrobiologyOpen · 2022Article
- ClpX/P-Dependent Degradation of Novel Substrates in Streptococcus mutans.Journal of bacteriology · 2022Article
- The transcription regulator BrsR serves as a network hub of natural competence protein-protein interactions inProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Characterization of FtsH Essentiality inFrontiers in genetics · 2021Article
- Regulatory circuits controlling Spx levels in Streptococcus mutans.Molecular microbiology · 2020Article
- Article
- Deficiency of MecA inFrontiers in microbiology · 2018Article
- Identification of New Degrons inFrontiers in microbiology · 2017Article
- Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
In prokaryotes, a conserved small RNA molecule, called tmRNA, rescues ribosomes from proteins that are abnormally truncated due to the presence of rare codons or degraded mRNA. During the rescue process, a peptide tag (SsrA) encoded by tmRNA is cotranslationally added to the truncated polypeptides, thereby targeting these proteins for proteolytic degradation. In Escherichia coli, ClpXP and ClpAP proteases primarily degrade SsrA-tagged proteins. Other proteases such as Lon and FtsH also participate in the degradation in E. coli. However, in Bacillus subtilis, ClpXP is the major protease that degrades the SsrA-tagged proteins. Degradation of SsrA-tagged protein in streptococci is not well understood except that ClpXP is responsible for the majority of the degradation. Here we show that in Streptococcus mutans, in addition to ClpXP, two other Clp complexes, ClpCP and ClpEP, are also involved in the degradation. We also found that ClpCP- and ClpEP-mediated proteolysis of SsrA-tagged substrates is induced by heat stress. As ClpCP and ClpEP proteins are highly conserved in streptococci, we predicted that ClpEP- and ClpCP-mediated degradation of SsrA-tagged proteins might be operational in other streptococci.
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Registered trials
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