Molecular and General Genetics MGG

, Volume 194, Issue 1–2, pp 114–123 | Cite as

cis-dominant, glutamine synthetase constitutive mutations of Escherichia coli indepedent of activation by the glnG and glnF products

  • Aurora V. Osorio
  • Luis Servín-González
  • Mario Rocha
  • Alejandra A. Covarrubias
  • Fernando Bastarrachea


Mutants resistant to 80 μM L-methionine-DL-sulfoximine (MS) were isolated on glucose-minimal 15 mM NH + 4 medium plates from Escherichia coli cells which were hypersensitive to this concentration of the analogue by virtue of their harboring glnG mutations. MS-resistant mutants derived from strain MX902 carried, in addition to its glnG74::Tn5 allele, mutations tightly linked to glnA, as shown by P1-mediated transduction experiments. One particular allele, gln-76, which suppressed the MS-sensitivity conferred by glnG74::Tn5 but not its Ntr phenotype (inability to transport and utilize compounds such as arginine or proline as the only nitrogen sources), was shown to allow constitutive expression of glutamine synthetase in the absence not only of a functional glnG product but also of a functional glnF product. This behavior was found to be cis-dominant in complementation experiments with F'14 merogenotes. In an otherwise wild-type genetic background as in MX929 (gln-76 glnA+ glnL+ glnG+ glnF+), however, normal activation, mediated by the glnG and glnF products was preferred over that mediated by gln-76.


Nitrogen Escherichia Coli Proline Arginine Glutamine 
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Copyright information

© Springer-Verlag 1984

Authors and Affiliations

  • Aurora V. Osorio
    • 1
  • Luis Servín-González
    • 1
  • Mario Rocha
    • 1
  • Alejandra A. Covarrubias
    • 1
  • Fernando Bastarrachea
    • 1
  1. 1.Centro de Investigación sobre Ingeniería Genética y BiotecnologíaUniversidad Nacional Autónoma de MéxicoMéxico 20México

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