ArticleProceedings of the National Academy of Sciences of the United States of America2008
Bacillus subtilis glutamine synthetase regulates its own synthesis by acting as a chaperone to stabilize GlnR-DNA complexes.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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27 citing papers in PubMed, 60 citations in OpenAlex.
- A c-di-AMP-controlled glutamine synthesis pathway promotes persistence ofbioRxiv : the preprint server for biology · 2026Article
- Allosteric activation mechanism of DriD, a WYL-domain containing transcription regulator.Communications biology · 2025Article
- Article
- A two-component system MechNtrB/MechNtrC related to nitrogen metabolism regulation inFrontiers in microbiology · 2025Article
- Design of a sorbitol-activated nitrogen metabolism-dependent regulatory system for redirection of carbon metabolism flow in Bacillus licheniformis.Nucleic acids research · 2023Article
- Glutamine synthetase and GlnR regulate nitrogen metabolism inApplied and environmental microbiology · 2023Article
- Understanding and application of Bacillus nitrogen regulation: A synthetic biology perspective.Journal of advanced research · 2023Review
- Genome-wide mapping of GlnR-binding sites reveals the global regulatory role of GlnR in controlling the metabolism of nitrogen and carbon in Paenibacillus polymyxa WLY78.BMC genomics · 2023Article
- Alanine synthesized by alanine dehydrogenase enables ammonium-tolerant nitrogen fixation inProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Molecular dissection of the glutamine synthetase-GlnR nitrogen regulatory circuitry in Gram-positive bacteria.Nature communications · 2022Article
- Article
- Role of GlnR in Controlling Expression of Nitrogen Metabolism Genes inJournal of bacteriology · 2020Article
- LmbU, a Cluster-Situated Regulator for Lincomycin, Consists of a DNA-Binding Domain, an Auto-Inhibitory Domain, and Forms Homodimer.Frontiers in microbiology · 2019Article
- Variants of theFrontiers in microbiology · 2019Article
- Positive and negative regulation of transferred nif genes mediated by indigenous GlnR in Gram-positive Paenibacillus polymyxa.PLoS genetics · 2018Article
- The Unexpected Essentiality ofFrontiers in microbiology · 2018Article
- Revisiting the in vivo GlnR-binding sites at the genome scale in Bacillus subtilis.BMC research notes · 2017Article
- Sirtuin-dependent reversible lysine acetylation of glutamine synthetases reveals an autofeedback loop in nitrogen metabolism.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- The Molecular Basis of TnrA Control by Glutamine Synthetase in Bacillus subtilis.The Journal of biological chemistry · 2016Article
- The GlnR Regulon in Streptococcus mutans Is Differentially Regulated by GlnR and PmrA.PloS one · 2016Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The Bacillus subtilis GlnR repressor controls gene expression in response to nitrogen availability. Because all GlnR-regulated genes are expressed constitutively in mutants lacking glutamine synthetase (GS), GS is required for repression by GlnR. Feedback-inhibited GS (FBI-GS) was shown to activate GlnR DNA binding with an in vitro electophoretic mobility shift assay (EMSA). The activation of GlnR DNA binding by GS in these experiments depended on the feedback inhibitor glutamine and did not occur with mutant GS proteins defective in regulating GlnR activity in vivo. Although stable GS-GlnR-DNA ternary complexes were not observed in the EMSA experiments, cross-linking experiments showed that a protein-protein interaction occurs between GlnR and FBI-GS. This interaction was reduced in the absence of the feedback inhibitor glutamine and with mutant GS proteins. Because FBI-GS significantly reduced the dissociation rate of the GlnR-DNA complexes, the stability of these complexes is enhanced by FBI-GS. These results argue that FBI-GS acts as a chaperone that activates GlnR DNA binding through a transient protein-protein interaction that stabilizes GlnR-DNA complexes. GS was shown to control the activity of the B. subtilis nitrogen transcription factor TnrA by forming a stable complex between FBI-GS and TnrA that inhibits TnrA DNA binding. Thus, B. subtilis GS is an enzyme with dual catalytic and regulatory functions that uses distinct mechanisms to control the activity of two different transcription factors.
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