ArticleJournal of bacteriology2006
Mutational analysis of the Escherichia coli melR gene suggests a two-state concerted model to explain transcriptional activation and repression in the melibiose operon.
Article in Journal of bacteriology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 19 citations in OpenAlex.
- Article
- Effector Overlap between theJournal of bacteriology · 2017Article
- Thermodynamic mechanism for inhibition of lactose permease by the phosphotransferase protein IIAGlc.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- A transcription blocker isolated from a designed repeat protein combinatorial library by in vivo functional screen.Scientific reports · 2015Article
- Insights into the inhibitory mechanisms of the regulatory protein IIA(Glc) on melibiose permease activity.The Journal of biological chemistry · 2014Article
- DNA looping in prokaryotes: experimental and theoretical approaches.Journal of bacteriology · 2013Review
- Induction of the galactose enzymes in Escherichia coli is independent of the C-1-hydroxyl optical configuration of the inducer D-galactose.Journal of bacteriology · 2008Article
- Roles of effectors in XylS-dependent transcription activation: intramolecular domain derepression and DNA binding.Journal of bacteriology · 2008Article
- Autoregulation of the Escherichia coli melR promoter: repression involves four molecules of MelR.Nucleic acids research · 2008Article
- Differences in the mechanism of the allosteric l-rhamnose responses of the AraC/XylS family transcription activators RhaS and RhaR.Molecular microbiology · 2008Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Transcription of the Escherichia coli melAB operon is regulated by the MelR protein, an AraC family member whose activity is modulated by the binding of melibiose. In the absence of melibiose, MelR is unable to activate the melAB promoter but autoregulates its own expression by repressing the melR promoter. Melibiose triggers MelR-dependent activation of the melAB promoter and relieves MelR-dependent repression of the melR promoter. Twenty-nine single amino acid substitutions in MelR that result in partial melibiose-independent activation of the melAB promoter have been identified. Combinations of different substitutions result in almost complete melibiose-independent activation of the melAB promoter. MelR carrying each of the single substitutions is less able to repress the melR promoter, while MelR carrying some combinations of substitutions is completely unable to repress the melR promoter. These results argue that different conformational states of MelR are responsible for activation of the melAB promoter and repression of the melR promoter. Supporting evidence for this is provided by the isolation of substitutions in MelR that block melibiose-dependent activation of the melAB promoter while not changing melibiose-independent repression of the melR promoter. Additional experiments with a bacterial two-hybrid system suggest that interactions between MelR subunits differ according to the two conformational states.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.