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- W2048487719 abstract "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." @default.
- W2048487719 created "2016-06-24" @default.
- W2048487719 creator A5009672391 @default.
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- W2048487719 date "2006-12-15" @default.
- W2048487719 modified "2023-09-27" @default.
- W2048487719 title "Overlapping and Specialized Functions of the Molybdenum-Dependent Regulators MopA and MopB in <i>Rhodobacter capsulatus</i>" @default.
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- W2048487719 doi "https://doi.org/10.1128/jb.01188-06" @default.
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