ArticleJournal of bacteriology2012
Functional Analysis of Bacillus subtilis Genes Involved in the Biosynthesis of 4-Thiouridine in tRNA.
Article in Journal of bacteriology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 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
27 citing papers in PubMed, 45 citations in OpenAlex.
- Comprehensive post-transcriptional modification profiles in individual Staphylococcus aureus tRNA species.Nucleic acids research · 2026Article
- RudS: bacterial desulfidase responsible for tRNA 4-thiouridine de-modification.Nucleic acids research · 2024Article
- Review
- A subclass of archaeal U8-tRNA sulfurases requires a [4Fe-4S] cluster for catalysis.Nucleic acids research · 2022Article
- Sulfur Availability Impacts Accumulation of the 2-Thiouridine tRNA Modification in Bacillus subtilis.Journal of bacteriology · 2022Article
- The Minimal Translation Machinery: What We Can Learn From Naturally and Experimentally Reduced Genomes.Frontiers in microbiology · 2022Article
- Sulfur modification in natural RNA and therapeutic oligonucleotides.RSC chemical biology · 2021Review
- The Multifaceted Bacterial Cysteine Desulfurases: From Metabolism to Pathogenesis.Antioxidants (Basel, Switzerland) · 2021Review
- Methods to Investigate the Kinetic Profile of Cysteine Desulfurases.Methods in molecular biology (Clifton, N.J.) · 2021Article
- tRNA Modifications as a Readout of S and Fe-S Metabolism.Methods in molecular biology (Clifton, N.J.) · 2021Article
- Naturally occurring modified ribonucleosides.Wiley interdisciplinary reviews. RNA · 2020Review
- Review
- Survey and Validation of tRNA Modifications and Their Corresponding Genes inBiomolecules · 2020Article
- Biosynthesis and Chemical Applications of Thioamides.ACS chemical biology · 2019Review
- A Survey of Pyridoxal 5'-Phosphate-Dependent Proteins in the Gram-Positive Model BacteriumFrontiers in molecular biosciences · 2019Review
- Recent Advances in Our Understanding of the Biosynthesis of Sulfur Modifications in tRNAs.Frontiers in microbiology · 2018Article
- Diverse Mechanisms of Sulfur Decoration in Bacterial tRNA and Their Cellular Functions.Biomolecules · 2017Review
- Biosynthesis of Sulfur-Containing tRNA Modifications: A Comparison of Bacterial, Archaeal, and Eukaryotic Pathways.Biomolecules · 2017Review
- Uncovering Large-Scale Conformational Change in Molecular Dynamics without Prior Knowledge.Journal of chemical theory and computation · 2016Article
- A [3Fe-4S] cluster is required for tRNA thiolation in archaea and eukaryotes.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
ThiI has been identified as an essential enzyme involved in the biosynthesis of thiamine and the tRNA thionucleoside modification, 4-thiouridine. In Escherichia coli and Salmonella enterica, ThiI acts as a sulfurtransferase, receiving the sulfur donated from the cysteine desulfurase IscS and transferring it to the target molecule or additional sulfur carrier proteins. However, in Bacillus subtilis and most species from the Firmicutes phylum, ThiI lacks the rhodanese domain that contains the site responsible for the sulfurtransferase activity. The lack of the gene encoding for a canonical IscS cysteine desulfurase and the presence of a short sequence of ThiI in these bacteria pointed to mechanistic differences involving sulfur trafficking reactions in both biosynthetic pathways. Here, we have carried out functional analysis of B. subtilis thiI and the adjacent gene, nifZ, encoding for a cysteine desulfurase. Gene inactivation experiments in B. subtilis indicate the requirement of ThiI and NifZ for the biosynthesis of 4-thiouridine, but not thiamine. In vitro synthesis of 4-thiouridine by ThiI and NifZ, along with labeling experiments, suggests the occurrence of an alternate transient site for sulfur transfer, thus obviating the need for a rhodanese domain. In vivo complementation studies in E. coli IscS- or ThiI-deficient strains provide further support for specific interactions between NifZ and ThiI. These results are compatible with the proposal that B. subtilis NifZ and ThiI utilize mechanistically distinct and mutually specific sulfur transfer reactions.
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