ArticleNature communications2024
Mycobacterial biotin synthases require an auxiliary protein to convert dethiobiotin into biotin.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Streptavidins Coordinate Biotin Sequestration and Self-Resistance Within a Biotin-Pathway Antibiotic Network.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Article
- Analysis of Metabolic Differences and Core Regulatory Pathways in Lactic Acid Bacteria-Fermented Broths of DifferentFoods (Basel, Switzerland) · 2026Article
- Balanced Expression of the Diiron Oxygenase BioE Is Essential for Biotin Homeostasis in Elizabethkingia meningoseptica.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Biotin synthesis and assimilation are vital for pathobiology of the insect pathogenic fungusMycology · 2026Article
- A ferritin-like diiron oxygenase BioE initiates bacterial biotin synthesis, a promising antivirulence target.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- RadicalJournal of the American Chemical Society · 2025Article
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Authors and funding
12 authors.
Funding
Abstract
Lipid biosynthesis in the pathogen Mycobacterium tuberculosis depends on biotin for posttranslational modification of key enzymes. However, the mycobacterial biotin synthetic pathway is not fully understood. Here, we show that rv1590, a gene of previously unknown function, is required by M. tuberculosis to synthesize biotin. Chemical-generic interaction experiments mapped the function of rv1590 to the conversion of dethiobiotin to biotin, which is catalyzed by biotin synthases (BioB). Biochemical studies confirmed that in contrast to BioB of Escherichia coli, BioB of M. tuberculosis requires Rv1590 (which we named "biotin synthase auxiliary protein" or BsaP), for activity. We found homologs of bsaP associated with bioB in many actinobacterial genomes, and confirmed that BioB of Mycobacterium smegmatis also requires BsaP. Structural comparisons of BsaP-associated biotin synthases with BsaP-independent biotin synthases suggest that the need for BsaP is determined by the [2Fe-2S] cluster that inserts sulfur into dethiobiotin. Our findings open new opportunities to seek BioB inhibitors to treat infections with M. tuberculosis and other pathogens.
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Registered trials
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