ArticleJournal of bacteriology2011
Functional analysis of molybdopterin biosynthesis in mycobacteria identifies a fused molybdopterin synthase in Mycobacterium tuberculosis.
Article in Journal of bacteriology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 52 citations in OpenAlex.
- MoaB2, a newly identified transcription factor, binds to σJournal of bacteriology · 2024Article
- The risk of pulmonary NTM infections and water-quality constituents among persons with cystic fibrosis in the United States, 2010-2019.Environmental epidemiology (Philadelphia, Pa.) · 2023Article
- Deciphering the biosynthesis of a novel lipid in Mycobacterium tuberculosis expands the known roles of the nitroreductase superfamily.The Journal of biological chemistry · 2023Article
- DosR's multifaceted role onFrontiers in cellular and infection microbiology · 2023Article
- Nontuberculous Mycobacteria Infection Risk and Trace Metals in Surface Water: A Population-based Ecologic Epidemiologic Study in Oregon.Annals of the American Thoracic Society · 2022Article
- Genomic Insights Into the Interspecific Diversity and Evolution ofFrontiers in microbiology · 2022Article
- Aptamer-Based Diagnostic Systems for the Rapid Screening of TB at the Point-of-Care.Diagnostics (Basel, Switzerland) · 2021Review
- Analysis of Mycobacterium africanum in the last 17 years in Aragon identifies a specific location of IS6110 in Lineage 6.Scientific reports · 2021Article
- Mycobacterium smegmatis does not display functional redundancy in nitrate reductase enzymes.PloS one · 2021Article
- The ATP-Binding Cassette (ABC) Transport Systems inBiology · 2020Review
- Nontuberculous Mycobacterial Disease and Molybdenum in Colorado Watersheds.International journal of environmental research and public health · 2020Article
- ATP-binding cassette (ABC) import systems ofEmerging microbes & infections · 2020Review
- Genome-wide mutational biases fuel transcriptional diversity in the Mycobacterium tuberculosis complex.Nature communications · 2019Article
- Review
- Comparing the Metabolic Capabilities of Bacteria in theMicroorganisms · 2019Review
- Horizontal acquisition of a hypoxia-responsive molybdenum cofactor biosynthesis pathway contributed to Mycobacterium tuberculosis pathoadaptation.PLoS pathogens · 2017Article
- Article
- Integration of Metabolic Modeling with Gene Co-expression Reveals Transcriptionally Programmed Reactions Explaining Robustness in Mycobacterium tuberculosis.Scientific reports · 2016Article
- New insights into TB physiology suggest untapped therapeutic opportunities.Immunological reviews · 2015Review
- Cleavage of the moaX-encoded fused molybdopterin synthase from Mycobacterium tuberculosis is necessary for activity.BMC microbiology · 2015Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Most mycobacterial species possess a full complement of genes for the biosynthesis of molybdenum cofactor (MoCo). However, a distinguishing feature of members of the Mycobacterium tuberculosis complex is their possession of multiple homologs associated with the first two steps of the MoCo biosynthetic pathway. A mutant of M. tuberculosis lacking the moaA1-moaD1 gene cluster and a derivative in which moaD2 was also deleted were significantly impaired for growth in media containing nitrate as a sole nitrogen source, indicating a reduced availability of MoCo to support the assimilatory function of the MoCo-dependent nitrate reductase, NarGHI. However, the double mutant displayed residual respiratory nitrate reductase activity, suggesting that it retains the capacity to produce MoCo. The M. tuberculosis moaD and moaE homologs were further analyzed by expressing these genes in mutant strains of M. smegmatis that lacked one or both of the sole molybdopterin (MPT) synthase-encoding genes, moaD2 and moaE2, and were unable to grow on nitrate, presumably as a result of the loss of MoCo-dependent nitrate assimilatory activity. Expression of M. tuberculosis moaD2 in the M. smegmatis moaD2 mutant and of M. tuberculosis moaE1 or moaE2 in the M. smegmatis moaE2 mutant restored nitrate assimilation, confirming the functionality of these genes in MPT synthesis. Expression of M. tuberculosis moaX also restored MoCo biosynthesis in M. smegmatis mutants lacking moaD2, moaE2, or both, thus identifying MoaX as a fused MPT synthase. By implicating multiple synthase-encoding homologs in MoCo biosynthesis, these results suggest that important cellular functions may be served by their expansion in M. tuberculosis.
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