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  • Electronic Resource  (2)
  • 1975-1979  (2)
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  • Electronic Resource  (2)
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  • 1
    Electronic Resource
    Electronic Resource
    Genetics of Bacterial RNA Polymerases (1979)
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Genetics 13 (1979), S. 59-97 
    Details
    ISSN: 0066-4197
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1146/annurev.ge.13.120179.000423
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    RNA polymerase mutants of Escherichia coli (1976)
    Springer
    Molecular genetics and genomics 143 (1976), S. 233-241 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Temperature-sensitive mutants of Escherichia coli that are unable to grow at high temperature can be obtained among those selected for resistance to streptovaricin or rifampicin at low temperature (Yura et al., 1970). One of these mutants (KY5323) that was supposed to carry a single mutation affecting both rifampicin resistance and temperature sensitivity was further investigated. Using purified RNA polymerase preparations obtained from the mutant and the wild type, it was found that the activity for DNA chain elongation is more sensitive to heat treatment than that for RNA chain initiation or DNA binding, and that the mutant enzyme is significantly more labile than the wild-type enzyme with respect to RNA chain elongation, when heat treatment is carried out at high salt concentration. These results, taken together with those of the enzyme reconstitution experiments, strongly suggest that the β subunit of the polymerase is directly involved in both RNA chain initiation and elongation reactions. Enzyme reconstitution experiments using isolated subunits derived from the mutant and the wild-type polymerases demonstrate that the alteration of β subunit is primarily responsible for both rifampicin resistance and thermolability of the mutant enzyme. In addition, the results suggested the apparent alteration of both β′ and α subunits in this mutant. Extensive transduction experiments provided genetic evidence that are consistent with the view that the strain KY5323 carries a second mutation affecting the β′ subunit, beside the primary mutation affecting the β subunit. The hypothetical β′ subunit mutation seems to modify quantitatively the rifampicin resistance caused by the β subunit mutation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00269399
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    Paper (German National Licenses)
    Fulltext
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