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Bacillus subtilis Glutamine Synthetase Controls Gene Expression through a Protein-Protein Interaction with Transcription Factor TnrA
- Source :
- Cell. 107(4):427-435
- Publication Year :
- 2001
- Publisher :
- Elsevier BV, 2001.
-
Abstract
- Bacillus subtilis TnrA, a global regulator of transcription, responds to nitrogen availability, but the specific signal to which it responds has been elusive. Genetic studies indicate that glutamine synthetase is required for the regulation of TnrA activity in vivo. We report here that the feedback-inhibited form of glutamine synthetase directly interacts with TnrA and blocks the DNA binding activity of TnrA. Mutations in the tnrA gene ( tnrA C ) that allow constitutive high level expression of tnrA -activated genes were isolated and characterized. Feedback-inhibited glutamine synthetase had a significantly reduced ability to block the in vitro DNA binding by three of the TnrA C proteins. Thus, glutamine synthetase, an enzyme of central metabolism, directly interacts with and regulates the DNA binding activity of TnrA.
- Subjects :
- DNA, Bacterial
Transcription, Genetic
Nitrogen
Glutamine
Molecular Sequence Data
Glutamic Acid
Bacillus subtilis
Biology
General Biochemistry, Genetics and Molecular Biology
Feedback
03 medical and health sciences
chemistry.chemical_compound
Bacterial Proteins
Glutamate-Ammonia Ligase
Transcription (biology)
Glutamine synthetase
Consensus Sequence
Gene expression
Amino Acid Sequence
Transcription factor
Gene
030304 developmental biology
chemistry.chemical_classification
0303 health sciences
Sequence Homology, Amino Acid
030306 microbiology
Biochemistry, Genetics and Molecular Biology(all)
Gene Expression Regulation, Bacterial
biology.organism_classification
Quaternary Ammonium Compounds
Repressor Proteins
Enzyme
chemistry
Biochemistry
Mutation
Sequence Alignment
DNA
Protein Binding
Signal Transduction
Transcription Factors
Subjects
Details
- ISSN :
- 00928674
- Volume :
- 107
- Issue :
- 4
- Database :
- OpenAIRE
- Journal :
- Cell
- Accession number :
- edsair.doi.dedup.....c01c31086937bf59e8aa380ebb0fa33a
- Full Text :
- https://doi.org/10.1016/s0092-8674(01)00572-4