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  • 1
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: The Escherichia coli proU operon encodes a high-affinity, binding-protein-dependent transport system for the osmoprotectant glycine betaine. Expression of proU is osmoregulated, and transcription of this operon is greatly increased In cells grown at high osmolarity. Characterization of the proU operon and its promoter provided results similar to those published elsewhere (Gowrishankar, 1989; Stirling et al., 1989). The previously identified proU601 mutation, which leads to increased proU expression both at low-and high osmolarity, is a G to A transition in the Pribnow box of the proU promoter, which increases the homology of the -10 region to the consensus sequence of E. coli promoters. Using an antiserum raised against a ProV-β-galactosidase hybrid protein, we have identified ProV as a protein associated with the cytoplasmic membrane. This cellular location is consistent with its proposed role as the energy -coupling component of the ProU transport system.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Molecular microbiology 4 (1990), S. 0 
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Further genetic evidence is provided here that Bradyrhizobium japonieum possesses a mitochondria-like electron-transport pathway: 2[H]→UQ→bc1→c→aa3→O2. Two Tn5-induced mutants, COX122 and COX132, having cytochrome c oxidase-negative phenotypes, were obtained and characterized. Mutant COX122 was defective in a novel gene, named cycM, which was responsible for the synthesis of a c-type cytochrome with an Mr, of 20000 (20K). This 20K cytochrome c appeared to catalyse electron transport from the cytochrome bc1, complex to the aa3-type terminal oxidase and, unlike mitochondrial cytochrome c, was membrane-bound in B. japonicum. The Tn5 insertion of mutant COX132 was localized in coxA, the structural gene for subunit I of cytochrome aa3. This finding also led to the cloning and sequencing of the corresponding wild-type coxA gene that encoded a 541 -amino-acid protein with a predicted Mr of 59247. The CoxA protein shared about 60% sequence identity with the cytochrome aa3 subunit I of mitochondria. The B. japonicum cycM and coxA mutants were able to fix nitrogen in symbiosis with soybean (Fix+). In contrast, mutants described previously which lacked the bc1 complex did not develop into endosymbiotic bacteroids and were thus Fix−. The data suggest that a symbiosis-specific respiratory chain exists in B. japonicum in which the electrons branch off at the bc1 complex.
    Type of Medium: Electronic Resource
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