title: Transcription factor TnrA inhibits the biosynthetic activity of glutamine synthetase in Bacillus subtilis.
abstract: The Bacillus subtilis glutamine synthetase (GS) plays a dual role in cell metabolism by functioning as catalyst and regulator. GS catalyses the ATP-dependent synthesis of glutamine from glutamate and ammonium. Under nitrogen-rich conditions, GS becomes feedback-inhibited by high intracellular glutamine levels and then binds transcription factors GlnR and TnrA, which control the genes of nitrogen assimilation. While GS-bound TnrA is no longer able to interact with DNA, GlnR-DNA binding is shown to be stimulated by GS complex formation. In this paper we show a new physiological feature of the interaction between glutamine synthetase and TnrA. The transcription factor TnrA inhibits the biosynthetic activity of glutamine synthetase in vivo and in vitro, while the GlnR protein does not affect the activity of the enzyme.
authors.affiliation: Kazan (Volga region) Federal University, Department of Microbiology, Kremlevskaya 18, 420008 Kazan, Russia.
authors.forename: Ksenia
authors.initials: K
authors.lastname: Fedorova
authors.forename: Airat
authors.initials: A
authors.lastname: Kayumov
authors.forename: Kathrin
authors.initials: K
authors.lastname: Woyda
authors.forename: Olga
authors.initials: O
authors.lastname: Ilinskaja
authors.forename: Karl
authors.initials: K
authors.lastname: Forchhammer
mesh_terms: D001412:Bacillus subtilis / Q000201:enzymology / Q000378:metabolism*; D001426:Bacterial Proteins / Q000378:metabolism*; D005974:Glutamate-Ammonia Ligase / Q000096:biosynthesis*; D011485:Protein Binding; D012097:Repressor Proteins / Q000378:metabolism*
chemical_list: D001426:Bacterial Proteins; D012097:Repressor Proteins; C101458:ScgR protein, Bacillus subtilis; D005974:Glutamate-Ammonia Ligase