ArticleThe Journal of biological chemistry2012
Sequence discrimination by DNA-binding domain of ETS family transcription factor PU.1 is linked to specific hydration of protein-DNA interface.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
23 citing papers in PubMed.
- Molecular basis of UV lesion binding and repair inhibition by ETS-family transcription factors.Nucleic acids research · 2026Article
- Molecular basis of UV lesion binding and repair inhibition by ETS-family transcription factors.bioRxiv : the preprint server for biology · 2026Article
- Pharmacological restriction of genomic binding sites redirects PU.1 pioneer transcription factor activity.Nature genetics · 2024Article
- Dissection of integrated readout reveals the structural thermodynamics of DNA selection by transcription factors.Structure (London, England : 1993) · 2024Article
- Salt bridge dynamics in protein/DNA recognition: a comparative analysis of Elk1 and ETV6.Physical chemistry chemical physics : PCCP · 2021Article
- Modulating DNA by polyamides to regulate transcription factor PU.1-DNA binding interactions.Biochimie · 2019Article
- Mechanism of cognate sequence discrimination by the ETS-family transcription factor ETS-1.The Journal of biological chemistry · 2019Article
- Mapping interfacial hydration in ETS-family transcription factor complexes with DNA: a chimeric approach.Nucleic acids research · 2018Article
- ETS transcription factors induce a unique UV damage signature that drives recurrent mutagenesis in melanoma.Nature communications · 2018Article
- Osmotic modulation of chromatin impacts on efficiency and kinetics of cell fate modulation.Scientific reports · 2018Article
- Two distinct DNA sequences recognized by transcription factors represent enthalpy and entropy optima.eLife · 2018Article
- Multiple DNA-binding modes for the ETS family transcription factor PU.1.The Journal of biological chemistry · 2017Article
- Signatures of DNA target selectivity by ETS transcription factors.Transcription · 2017Review
- Distinct Roles for Interfacial Hydration in Site-Specific DNA Recognition by ETS-Family Transcription Factors.The journal of physical chemistry. B · 2017Article
- Differential sensitivity to methylated DNA by ETS-family transcription factors is intrinsically encoded in their DNA-binding domains.Nucleic acids research · 2016Article
- Pharmacologic efficacy of PU.1 inhibition by heterocyclic dications: a mechanistic analysis.Nucleic acids research · 2016Article
- A Role for Autoinhibition in Preventing Dimerization of the Transcription Factor ETS1.The Journal of biological chemistry · 2015Article
- Heterogeneous dynamics in DNA site discrimination by the structurally homologous DNA-binding domains of ETS-family transcription factors.Nucleic acids research · 2015Article
- Quantitative Investigation of Protein-Nucleic Acid Interactions by Biosensor Surface Plasmon Resonance.Methods in molecular biology (Clifton, N.J.) · 2015Article
- Mechanistic heterogeneity in site recognition by the structurally homologous DNA-binding domains of the ETS family transcription factors Ets-1 and PU.1.The Journal of biological chemistry · 2014Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
1 author.
Funding
No grant is acknowledged in the PubMed record.
Abstract
PU.1 is an essential transcription factor in normal hematopoietic lineage development. It recognizes a large number of promoter sites differing only in bases flanking a core consensus of 5'-GGAA-3'. DNA binding is mediated by its ETS domain, whose sequence selectivity directly corresponds to the transactivational activity and frequency of binding sites for full-length PU.1 in vivo. To better understand the basis of sequence discrimination, we characterized its binding properties to a high affinity and low affinity site. Despite sharing a homologous structural framework as confirmed by DNase I and hydroxyl radical footprinting, the two complexes exhibit striking heterogeneity in terms of hydration properties. High affinity binding is destabilized by osmotic stress, whereas low affinity binding is insensitive. Dimethyl sulfate footprinting showed that the major groove at the core consensus is protected in the high affinity complex but accessible in the low affinity one. Finally, destabilization of low affinity binding by salt is in quantitative agreement with the number of phosphate contacts but is substantially attenuated in high affinity binding. These observations support a mechanism of sequence discrimination wherein specifically bound water molecules couple flanking backbone contacts with base-specific interactions in a sequestered cavity at the core consensus. The implications of this model with respect to other ETS paralogs are discussed.
Indexed as
Identifiers
What OpenQuestion holds
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.