ArticleJournal of bacteriology2006
Overlapping and specialized functions of the molybdenum-dependent regulators MopA and MopB in Rhodobacter capsulatus.
Article in Journal of bacteriology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 32 citations in OpenAlex.
- The archetypal gene transfer agent RcGTA is regulated via direct interaction with the enigmatic RNA polymerase omega subunit.Cell reports · 2022Article
- Interactions between paralogous bacterial enhancer-binding proteins enable metal-dependent regulation of alternative nitrogenases in Azotobacter vinelandii.Molecular microbiology · 2022Article
- Article
- Rhodobacter capsulatus AnfA is essential for production of Fe-nitrogenase proteins but dispensable for cofactor biosynthesis and electron supply.MicrobiologyOpen · 2020Article
- Antimicrobial Resistance andFrontiers in microbiology · 2020Article
- NifA is the master regulator of both nitrogenase systems in Rhodobacter capsulatus.MicrobiologyOpen · 2019Article
- Identification and characterization of a direct activator of a gene transfer agent.Nature communications · 2019Article
- Bacterial PerO Permeases Transport Sulfate and Related Oxyanions.Journal of bacteriology · 2017Article
- Proteome Profiling of the Rhodobacter capsulatus Molybdenum Response Reveals a Role of IscN in Nitrogen Fixation by Fe-Nitrogenase.Journal of bacteriology · 2015Article
- NifA- and CooA-coordinated cowN expression sustains nitrogen fixation by Rhodobacter capsulatus in the presence of carbon monoxide.Journal of bacteriology · 2014Article
- Coordinated expression of fdxD and molybdenum nitrogenase genes promotes nitrogen fixation by Rhodobacter capsulatus in the presence of oxygen.Journal of bacteriology · 2014Article
- Expression, purification, crystallization and preliminary X-ray analysis of the DNA-binding domain of Rhodobacter capsulatus MopB.Acta crystallographica. Section F, Structural biology and crystallization communications · 2011Article
- A Rhodobacter capsulatus member of a universal permease family imports molybdate and other oxyanions.Journal of bacteriology · 2010Article
- Specific interactions between four molybdenum-binding proteins contribute to Mo-dependent gene regulation in Rhodobacter capsulatus.Journal of bacteriology · 2009Article
- Molybdoproteomes and evolution of molybdenum utilization.Journal of molecular biology · 2008Article
- The GntR-like regulator TauR activates expression of taurine utilization genes in Rhodobacter capsulatus.Journal of bacteriology · 2008Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The phototrophic purple bacterium Rhodobacter capsulatus encodes two similar but functionally not identical molybdenum-dependent regulator proteins (MopA and MopB), which are known to replace each other in repression of the modABC genes (coding for an ABC-type high-affinity Mo transport system) and anfA (coding for the transcriptional activator of Fe-nitrogenase genes). We identified further Mo-regulated (mor) genes coding for a putative ABC-type transport system of unknown function (MorABC) and a putative Mo-binding protein (Mop). The genes coding for MopA and the ModABC transporter form part of a single transcriptional unit, mopA-modABCD, as shown by reverse transcriptase PCR. Immediately upstream of mopA and transcribed in the opposite direction is mopB. The genes coding for the putative MorABC transporter belong to two divergently transcribed operons, morAB and morC. Expression studies based on lacZ reporter gene fusions in mutant strains defective for either MopA, MopB, or both revealed that the regulators substitute for each other in Mo-dependent repression of morAB and morC. Specific Mo-dependent activation of the mop gene by MopA, but not MopB, was found to control the putative Mo-binding protein. Both MopA and MopB are thought to bind to conserved DNA sequences with dyad symmetry in the promoter regions of all target genes. The positions of these so-called Mo boxes relative to the transcription start sites (as determined by primer extension analyses) differed between Mo-repressed genes and the Mo-activated mop gene. DNA mobility shift assays showed that MopA and MopB require molybdenum to bind to their target sites with high affinity.
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