ArticlePloS one2012
Tat-dependent translocation of an F420-binding protein of Mycobacterium tuberculosis.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
What it found
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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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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
19 citing papers in PubMed, 29 citations in OpenAlex.
- Article
- Tat-dependent protein translocation and its evolution.FEMS microbiology reviews · 2026Review
- Functions of nitroreductases in mycobacterial physiology and drug susceptibility.Journal of bacteriology · 2025Review
- Novel role of PE_PGRS47 in the alteration of mycobacterial cell wall integrity and drug resistance.Archives of microbiology · 2023Article
- Article
- Cofactor F420: an expanded view of its distribution, biosynthesis and roles in bacteria and archaea.FEMS microbiology reviews · 2021Article
- The pMy vector series: A versatile cloning platform for the recombinant production of mycobacterial proteins in Mycobacterium smegmatis.Protein science : a publication of the Protein Society · 2020Article
- Reconstructing the evolutionary history of FScientific reports · 2018Article
- A GFP-strategy for efficient recombinant protein overexpression and purification inRSC advances · 2018Article
- Discovery and characterization of an FApplied microbiology and biotechnology · 2017Article
- Rv2074 is a novel F420 H2 -dependent biliverdin reductase in Mycobacterium tuberculosis.Protein science : a publication of the Protein Society · 2016Article
- Physiology, Biochemistry, and Applications of F420- and Fo-Dependent Redox Reactions.Microbiology and molecular biology reviews : MMBR · 2016Review
- Elongation of the Poly-γ-glutamate Tail of F420 Requires Both Domains of the F420:γ-Glutamyl Ligase (FbiB) of Mycobacterium tuberculosis.The Journal of biological chemistry · 2016Article
- Octanoylation of early intermediates of mycobacterial methylglucose lipopolysaccharides.Scientific reports · 2015Article
- Production of recombinant proteins in Mycobacterium smegmatis for structural and functional studies.Protein science : a publication of the Protein Society · 2015Review
- Article
- Mycobacterium tuberculosis serine protease Rv3668c can manipulate the host-pathogen interaction via Erk-NF-κB axis-mediated cytokine differential expression.Journal of interferon & cytokine research : the official journal of the International Society for Interferon and Cytokine Research · 2014Article
- Article
- Rv0132c of Mycobacterium tuberculosis encodes a coenzyme F420-dependent hydroxymycolic acid dehydrogenase.PloS one · 2013Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
F(420) is a unique cofactor present in a restricted range of microorganisms, including mycobacteria. It has been proposed that F(420) has an important role in the oxidoreductive reactions of Mycobacterium tuberculosis, possibly associated with anaerobic survival and persistence. The protein encoded by Rv0132c has a predicted N-terminal signal sequence and is annotated as an F(420)-dependent glucose-6-phosphate dehydrogenase. Here we show that Rv0132c protein does not have the annotated activity. It does, however, co-purify with F(420) during expression experiments in M. smegmatis. We also show that the Rv0132c-F(420) complex is a substrate for the Tat pathway, which mediates translocation of the complex across the cytoplasmic membrane, where Rv0132c is anchored to the cell envelope. This is the first report of any F(420)-binding protein being a substrate for the Tat pathway and of the presence of F(420) outside of the cytosol in any F(420)-producing microorganism. The Rv0132c protein and its Tat export sequence are essentially invariant in the Mycobacterium tuberculosis complex. Taken together, these results show that current understanding of F(420) biology in mycobacteria should be expanded to include activities occurring in the extra-cytoplasmic cell envelope.
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Registered trials
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.