ArticleMolecular bioSystems2016
Histidine switch controlling pH-dependent protein folding and DNA binding in a transcription factor at the core of synthetic network devices.
Article in Molecular bioSystems, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
11 citing papers in PubMed.
- A PadR family transcriptional repressor regulates the transcription of chromate efflux transporter in Enterobacter sp. Z1.Journal of microbiology (Seoul, Korea) · 2024Article
- Structural basis of DNA binding by the NAC transcription factor ORE1, a master regulator of plant senescence.Plant communications · 2023Article
- Expression of SSEA-4 and Oct-4 from somatic cells in primary mouse gastric cell culture induced by brief strong acid.Molecular and cellular biochemistry · 2021Article
- Discovery and mechanism of a pH-dependent dual-binding-site switch in the interaction of a pair of protein modules.Science advances · 2020Article
- An EmrB multidrug efflux pump inThe Journal of biological chemistry · 2019Article
- Cross Talk between MarR-Like Transcription Factors Coordinates the Regulation of Motility in Uropathogenic Escherichia coli.Infection and immunity · 2018Article
- Tuning site-specific dynamics to drive allosteric activation in a pneumococcal zinc uptake regulator.eLife · 2018Article
- Functional Mechanism of the Efflux Pumps Transcription Regulators FromFrontiers in molecular biosciences · 2018Review
- Metallochaperones and metalloregulation in bacteria.Essays in biochemistry · 2017Review
- Redox-Sensitive MarR Homologue BifR from Burkholderia thailandensis Regulates Biofilm Formation.Biochemistry · 2017Article
- Regulation of Metabolic Pathways by MarR Family Transcription Factors.Computational and structural biotechnology journal · 2017Review
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
Therapeutic strategies have been reported that depend on synthetic network devices in which a urate-sensing transcriptional regulator detects pathological levels of urate and triggers production or release of urate oxidase. The transcription factor involved, HucR, is a member of the multiple antibiotic resistance (MarR) protein family. We show that protonation of stacked histidine residues at the pivot point of long helices that form the scaffold of the dimer interface leads to reversible formation of a molten globule state and significantly attenuated DNA binding at physiological temperatures. We also show that binding of urate to symmetrical sites in each protein lobe is communicated via the dimer interface. This is the first demonstration of regulation of a MarR family transcription factor by pH-dependent interconversion between a molten globule and a compact folded state. Our data further suggest that HucR may be utilized in synthetic devices that depend on detection of pH changes.
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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.