ArticleThe Journal of biological chemistry2013
Replacement of all arginine residues with canavanine in MazF-bs mRNA interferase changes its specificity.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 16 citations in OpenAlex.
- Residue-Specific Incorporation of Noncanonical Amino Acids in Auxotrophic Hosts:Chemical reviews · 2025Review
- Lipidated variants of the antimicrobial peptide nisin produced via incorporation of methionine analogs for click chemistry show improved bioactivity.The Journal of biological chemistry · 2023Article
- Covalent labeling of a chromatin reader domain using proximity-reactive cyclic peptides.Chemical science · 2022Article
- Conserved Amino Acid Moieties ofFrontiers in microbiology · 2021Article
- Programming mRNA decay to modulate synthetic circuit resource allocation.Nature communications · 2017Article
- Residue-specific Incorporation of Noncanonical Amino Acids into Model Proteins Using an Escherichia coli Cell-free Transcription-translation System.Journal of visualized experiments : JoVE · 2016Article
- Suppression of the toxicity of Bac7 (1-35), a bovine peptide antibiotic, and its production in E. coli.AMB Express · 2016Article
- Structural basis of mRNA recognition and cleavage by toxin MazF and its regulation by antitoxin MazE in Bacillus subtilis.Molecular cell · 2013Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Replacement of a specific amino acid residue in a protein with nonnatural analogues is highly challenging because of their cellular toxicity. We demonstrate for the first time the replacement of all arginine (Arg) residues in a protein with canavanine (Can), a toxic Arg analogue. All Arg residues in the 5-base specific (UACAU) mRNA interferase from Bacillus subtilis (MazF-bs(arg)) were replaced with Can by using the single-protein production system in Escherichia coli. The resulting MazF-bs(can) gained a 6-base recognition sequence, UACAUA, for RNA cleavage instead of the 5-base sequence, UACAU, for MazF-bs(arg). Mass spectrometry analysis confirmed that all Arg residues were replaced with Can. The present system offers a novel approach to create new functional proteins by replacing a specific amino acid in a protein with its analogues.
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Registered trials
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