ArticleThe Journal of biological chemistry2013
Protein signatures that promote operator selectivity among paralog MerR monovalent metal ion regulators.
Article in The Journal of biological chemistry, 2013. 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, 23 citations in OpenAlex.
- Bacterial Metallostasis: Metal Sensing, Metalloproteome Remodeling, and Metal Trafficking.Chemical reviews · 2024Review
- Chimeric MerR-Family Regulators and Logic Elements for the Design of Metal Sensitive Genetic Circuits inACS synthetic biology · 2023Article
- Article
- Potential Whole-Cell Biosensors for Detection of Metal Using MerR Family Proteins fromMicromachines · 2021Article
- Clinical Evolution of New Delhi Metallo-β-Lactamase (NDM) Optimizes Resistance under Zn(II) Deprivation.Antimicrobial agents and chemotherapy · 2018Article
- Article
- Compartment and signal-specific codependence in the transcriptional control of Salmonella periplasmic copper homeostasis.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Zinc Resistance Mechanisms of P1B-type ATPases in Sinorhizobium meliloti CCNWSX0020.Scientific reports · 2016Article
- TRANSCRIPTION. Allosteric transcriptional regulation via changes in the overall topology of the core promoter.Science (New York, N.Y.) · 2015Article
- A single serine residue determines selectivity to monovalent metal ions in metalloregulators of the MerR family.Journal of bacteriology · 2015Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Two paralog transcriptional regulators of the MerR family, CueR and GolS, are responsible for monovalent metal ion sensing and resistance in Salmonella enterica. Although similar in sequence and also in their target binding sites, these proteins differ in signal detection and in the set of target genes they control. Recently, we demonstrated that selective promoter recognition depends on the presence of specific bases located at positions 3' and 3 within the operators they interact with. Here, we identify the amino acid residues within the N-terminal DNA-binding domain of these sensor proteins that are directly involved in operator discrimination. We demonstrate that a methionine residue at position 16 of GolS, absolutely conserved among GolS-like proteins but absent in all CueR-like xenologs, is the key to selectively recognize operators that harbor the distinctive GolS-operator signature, whereas the residue at position 19 finely tunes the regulator/operator interaction. Furthermore, swapping these residues switches the set of genes recognized by these transcription factors. These results indicate that co-evolution of a regulator and its cognate operators within the bacterial cell provides the conditions to avoid cross-recognition and guarantees the proper response to metal injury.
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Registered trials
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.