ArticleBiochemistry2013
Bacterial toxin RelE: a highly efficient ribonuclease with exquisite substrate specificity using atypical catalytic residues.
Article in Biochemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 49 citations in OpenAlex.
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- Influence of Different Transposon Families on Genomic Stability of Shewanella oneidensis MR1.Microbial biotechnology · 2025Article
- Comprehensive mutational analysis of the sequence-function relationship within a viral internal ribosome entry site.Nucleic acids research · 2025Article
- Guided tour through the small protein landscape ofmicroLife · 2025Article
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- Efficient quantitative monitoring of translational initiation by RelE cleavage.Nucleic acids research · 2022Article
- Enzymatic properties of CARF-domain proteins inFrontiers in microbiology · 2022Article
- Significant Loop Motions in the SsoPTP Protein Tyrosine Phosphatase Allow for Dual General Acid Functionality.Biochemistry · 2021Article
- Structure-based design of peptides that trigger Streptococcus pneumoniae cell death.The FEBS journal · 2021Article
- The Cysteine Protease MaOC1, a Prokaryotic Caspase Homolog, Cleaves the Antitoxin of a Type II Toxin-Antitoxin System.Frontiers in microbiology · 2021Article
- Evolutionary and functional classification of the CARF domain superfamily, key sensors in prokaryotic antivirus defense.Nucleic acids research · 2020Article
- Structure of a human 48Science (New York, N.Y.) · 2020Article
- Fuse to defuse: a self-limiting ribonuclease-ring nuclease fusion for type III CRISPR defence.Nucleic acids research · 2020Article
- The Positively Charged Active Site of the Bacterial Toxin RelE Causes a Large Shift in the General Base pBiochemistry · 2020Article
- Convergent Evolution of the Barnase/EndoU/Colicin/RelE (BECR) Fold in Antibacterial tRNase Toxins.Structure (London, England : 1993) · 2019Article
- Whole Genome Sequencing-Based Comparison of Food Isolates ofFrontiers in microbiology · 2019Article
- Systematic approach for dissecting the molecular mechanisms of transcriptional regulation in bacteria.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Miscoding-induced stalling of substrate translocation on the bacterial ribosome.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The toxin RelE is a ribosome-dependent endoribonuclease implicated in diverse cellular processes, including persistence. During amino acid starvation, RelE inhibits translation by cleaving ribosomal A-site mRNA. Although RelE is structurally similar to other microbial endoribonucleases, the active-site amino acid composition differs substantially and lacks obvious candidates for general acid-base functionality. Highly conserved RelE residues (Lys52, Lys54, Arg61, Arg81, and Tyr87) surround the mRNA scissile phosphate, and specific 16S rRNA contacts further contribute to substrate positioning. We used a single-turnover kinetic assay to evaluate the catalytic importance of individual residues in the RelE active site. Within the context of the ribosome, RelE rapidly cleaves A-site mRNA at a rate similar to those of traditional ribonucleases. Single-turnover rate constants decreased between 10(2)- and 10(6)-fold for the RelE active-site mutants of Lys52, Lys54, Arg61, and Arg81. RelE may principally promote catalysis via transition-state charge stabilization and leaving-group protonation, in addition to achieving in-line substrate positioning in cooperation with the ribosome. This kinetic analysis complements structural information to provide a foundation for understanding the molecular mechanism of this atypical endoribonuclease.
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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.