Library

feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
Filter
  • Glutamine synthetase NH inf4 sup+ switch off  (1)
  • Nitrogenase switch-off  (1)
  • 1
    ISSN: 1432-072X
    Keywords: Rhodospirillum rubrum ; Nitrogenase ; Glutamine synthetase NH inf4 sup+ switch off ; Complementation of R. rubrum Nif- mutants
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A spontaneous pleiotropic Nif- mutation in Rhodospirillum rubrum has been partially characterized biochemically and by complementation analysis with recombinant plasmids carrying Azotobacter vinelandii DNA in the vicinity of ORF12 [Jacobson et al. (1989) J. Bacteriol 171:1017–1027]. In addition to being unable to grow on N2 as a nitrogen source the phenotypic characterization of this and other metronidazole enriched spontaneous mutants showed (a) no nitrogenase activity, (b) the absence of NifHDK polypeptides, (c) a slower growth rate on NH inf4 sup+ , (d) approximately 50% higher glutamine synthetase (GS) activity than the wild-type, which was repressible, (e) an inability to switch-off GS activity in response to an NH inf4 sup+ up-shift, and (f) an inability to modify (32P-label) the GS polypeptide. The apparent relationship between the absence of nifHDK expression and the absence of GS adenylylation cannot be explained in terms of the current model for nif gene regulation. However, R. rubrum transconjugants receiving A. vinelandii DNA which originated immediately upstream from nifH, restored all aspects of the wild-type phenotype. These data suggest a here-to-fore unrecognized relationship between nif expression and GS switch-off (adenylylation) activity, and the existence of a previously unidentified regulatory locus in Azotobacter that complements this mutation.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 134 (1983), S. 45-48 
    ISSN: 1432-072X
    Keywords: Nitrogenase ; Methylamine ; Nitrogenase switch-off ; Rhodopseudomonas capsulata
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract In the photosynthetic bacterium Rhodopseudomonas capsulata, NH 4 + switch-off of nitrogenase activity can be mimicked by its analog, methylamine. Like NH 4 + , methylamine appeared to require processing by glutamine synthetase (GS) before it was effective; γ-glutamylmethylamide was shown to be the product of this reaction. Evidence that this glutamine analog functioned directly to initiate nitrogenase inactivation was suggested first by the fact that it was a poor substrate for glutamate synthase (i.e., it was not further metabolized by this pathway) and secondly, azaserine which blocks the transfer of the glutamine amide group had no effect on CH3NH 3 + (or NH 4 + ) switch-off. These observations are taken as preliminary evidence to suggest that when NH 4 + inhibits nitrogenase activity, inactivation is initiated by glutamine itself, and not a molecule derived from it. Finally, evidence was presented that R. capsulata would use CH3NH 3 + as a nitrogen substrate, but lag periods and generation times increased with subsequent passages.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...