Control of nitrogenase reactivation by the GlnZ protein in Azospirillum brasilense.

نویسندگان

  • G Klassen
  • E M de Souza
  • M G Yates
  • L U Rigo
  • J Inaba
  • F de O Pedrosa
چکیده

The glnZ mutant of Azospirillum brasilense (strain 7611) showed only partial recovery (20 to 40%) after 80 min of ammonia-induced nitrogenase switch-off, whereas the wild type recovered totally within 10 min. In contrast, the two strains showed identical anoxic-induced switch-on/switch-off, indicating no cross talk between the two reactivation mechanisms.

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Interactions between PII proteins and the nitrogenase regulatory enzymes DraT and DraG in Azospirillum brasilense.

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Crystal structure of the GlnZ-DraG complex reveals a different form of PII-target interaction.

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Different responses of the GlnB and GlnZ proteins upon in vitro uridylylation by the Azospirillum brasilense GlnD protein.

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The nitrogenase regulatory enzyme dinitrogenase reductase ADP-ribosyltransferase (DraT) is activated by direct interaction with the signal transduction protein GlnB.

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عنوان ژورنال:
  • Journal of bacteriology

دوره 183 22  شماره 

صفحات  -

تاریخ انتشار 2001