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Literature summary for 6.3.1.2 extracted from

  • Kayumov, A.; Heinrich, A.; Fedorova, K.; Ilinskaya, O.; Forchhammer, K.
    Interaction of the general transcription factor TnrA with the PII-like protein GlnK and glutamine synthetase in Bacillus subtilis (2011), FEBS J., 278, 1779-1789.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
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General Information

General Information Comment Organism
physiological function glutathione synthetase binds to transcription factor TnrA in its feedback-inhibited form, and also in its non-feedback-inhibited form, although less efficiently. TnrA forms either a stable soluble complex with GlnK in the absence of transmembrane ammonium transporter AmtB, or constitutively binds to glutathione synthetase in the absence of regulatuor GlnK. In vitro, the TnrA C-terminus is responsible for interactions with either glutathione synthetase or GlnK, and this region appears also to mediate proteolysis, suggesting that binding of GlnK or glutathione synthetase protects TnrA from degradation Bacillus subtilis