ArticleNucleic acids research2002
DNA binding of the transcription activator protein MelR from Escherichia coli and its C-terminal domain.
Article in Nucleic acids research, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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9 citing papers in PubMed, 16 citations in OpenAlex.
- Finely tuned regulation of the aromatic amine degradation pathway in Escherichia coli.Journal of bacteriology · 2013Article
- Sequential XylS-CTD binding to the Pm promoter induces DNA bending prior to activation.Journal of bacteriology · 2010Article
- Functional domains of ExsA, the transcriptional activator of the Pseudomonas aeruginosa type III secretion system.Journal of bacteriology · 2009Article
- Residues near the amino terminus of Rns are essential for positive autoregulation and DNA binding.Journal of bacteriology · 2008Article
- Differences in the mechanism of the allosteric l-rhamnose responses of the AraC/XylS family transcription activators RhaS and RhaR.Molecular microbiology · 2008Article
- Transcription activation by the DNA-binding domain of the AraC family protein RhaS in the absence of its effector-binding domain.Journal of bacteriology · 2007Article
- Mutational analysis of the Escherichia coli melR gene suggests a two-state concerted model to explain transcriptional activation and repression in the melibiose operon.Journal of bacteriology · 2006Article
- Genomic studies with Escherichia coli MelR protein: applications of chromatin immunoprecipitation and microarrays.Journal of bacteriology · 2004Article
- Leucines 193 and 194 at the N-terminal domain of the XylS protein, the positive transcriptional regulator of the TOL meta-cleavage pathway, are involved in dimerization.Journal of bacteriology · 2003Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
MelR is an Escherichia coli transcription factor belonging to the AraC family. It activates expression of the melAB operon in response to melibiose. Full-length MelR (MelR303) binds to two pairs of sites upstream of the melAB transcription start site, denoted sites 1' and 1 and sites 2 and 2', and to a fifth site, R, which overlaps the divergent melR promoter. The C-terminal domain of MelR (MelR173) does not activate transcription. Here we show that, like MelR303, when MelR173 binds to sites 1 and 2 it recruits CRP to bind between these sites. Hence, the C-terminal domain is involved in heterologous interactions. MelR173 binds to the R site, which has 11 of 18 bp identical to sites 1 and 2 but, surprisingly, does not bind to site 1', which has 12 of 18 bp identical, nor to site 2'. Using electrophoretic mobility shift assays, we show that the binding of MelR303 to sites 1' and 2' is due to cooperative binding with the adjacent site. This homologous cooperativity requires the N-terminal domain of the protein. Activation of the melAB promoter requires MelR to occupy site 2', which overlaps the -35 hexamer. Hence, both domains of MelR are required for transcription activation.
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