@article{mbs:/content/journal/micro/10.1099/00221287-125-2-301, author = "Lotz, W. and Fees, H. and Wohlleben, W. and Burkardt, H. J.", title = "Isolation and Characterization of the DNA-dependent RNA Polymerase of Rhizobium leguminosarum 300", journal= "Microbiology", year = "1981", volume = "125", number = "2", pages = "301-309", doi = "https://doi.org/10.1099/00221287-125-2-301", url = "https://www.microbiologyresearch.org/content/journal/micro/10.1099/00221287-125-2-301", publisher = "Microbiology Society", issn = "1465-2080", type = "Journal Article", abstract = "The DNA-dependent RNA polymerase isolated from Rhizobium leguminosarum 300 contains the following subunits: β′, β, polypeptide A and α (molecular weights 149000, 146000, 93000 and 42000, respectively). Polypeptide A is postulated to be the σ factor of the enzyme. The experimental conditions used for the in vitro assay of the enzyme activity, with plasmid pMB9 as template, included: 40 mm-Tris/HCl (pH 7.9), 150mm-NaCl, 5 mm MgCl2, at 34 °C. The isolated enzyme was shown by electron microscopy to bind specifically to the region of early promoters of DNA of the Escherichia coli bacteriophage T7. Therefore, Rhizobium-specific promoters may have base sequences in common with those of E. coli. ", }