ArticleBMC molecular biology2009
DNA binding by Corynebacterium glutamicum TetR-type transcription regulator AmtR.
Article in BMC molecular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 15 citations in OpenAlex.
- The role of the transcriptional repressor CssR inHeliyon · 2024Article
- Production of l-glutamate family amino acids inSynthetic and systems biotechnology · 2021Review
- PII Signal Transduction Protein GlnK Alleviates Feedback Inhibition ofApplied and environmental microbiology · 2020Article
- A putative TetR regulator is involved in nitric oxide stress resistance in Porphyromonas gingivalis.Molecular oral microbiology · 2016Article
- The TetR family of regulators.Microbiology and molecular biology reviews : MMBR · 2013Review
- Crystallization and preliminary crystallographic analysis of the global nitrogen regulator AmtR from Corynebacterium glutamicum.Acta crystallographica. Section F, Structural biology and crystallization communications · 2009Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundThe TetR family member AmtR is the central regulator of nitrogen starvation response in Corynebacterium glutamicum. While the AmtR regulon was physiologically characterized in great detail up to now, mechanistic questions of AmtR binding were not addressed. This study presents a characterization of functionally important amino acids in the DNA binding domain of AmtR and of crucial nucleotides in the AmtR recognition motif.
resultsSite-directed mutagenesis, the characterization of corresponding mutant proteins by gel retardation assays and surface plasmon resonance and molecular modelling revealed several amino acids, which are directly involved in DNA binding, while others have more structural function. Furthermore, we could show that the spacing of the binding motif half sites is crucial for repression of transcription by AmtR.
conclusionAlthough the DNA binding domain of TetR-type repressors is highly conserved and a core binding motif was identified for AmtR and TetR(D), the AmtR binding domain shows individual properties compared to other TetR proteins. Besides by distinct amino acids of AmtR, DNA binding is influenced by nucleotides not only of the conserved binding motif but also by spacing nucleotides in C. glutamicum.
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