2-oxoglutarate triggers assembly of active dodecameric <i>Methanosarcina mazei</i> glutamine synthetase.

ABSTRACT: Glutamine synthetases (GS) are central enzymes essential for the nitrogen metabolism across all domains of life. Consequently, they have been extensively studied for more than half a century. Based on the ATP-dependent ammonium assimilation generating glutamine, GS expression and activity are strictly regulated in all organisms. In the methanogenic archaeon Methanosarcina mazei, it has been shown that the metabolite 2-oxoglutarate (2-OG) directly induces the GS activity. Besides, modulation of the activity by interaction with small proteins (GlnK₁ and sP26) has been reported. Here, we show that the strong activation of M. mazei GS (GlnA₁) by 2-OG is based on the 2-OG dependent dodecamer assembly of GlnA₁ by using mass photometry (MP) and singl

SUBMITTER: Herdering E 

PROVIDER: S-EPMC11957540 | biostudies-literature | 2025 Mar

REPOSITORIES: biostudies-literature