ArticleThe Journal of biological chemistry2014
Mechanistic heterogeneity in site recognition by the structurally homologous DNA-binding domains of the ETS family transcription factors Ets-1 and PU.1.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 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
- ETS-1 in tumor immunology: implications for novel anti-cancer strategies.Frontiers in immunology · 2025Review
- Transcription factor ETS1‑mediated ECT2 expression promotes the malignant behavior of prostate cancer cells.Oncology letters · 2024Article
- DNA selection by the master transcription factor PU.1.Cell reports · 2023Article
- Spurious intragenic transcription is a feature of mammalian cellular senescence and tissue aging.Nature aging · 2023Article
- The Non-continuum Nature of Eukaryotic Transcriptional Regulation.Advances in experimental medicine and biology · 2022Article
- Pioneer factors in development and cancer.iScience · 2021Review
- DNA-facilitated target search by nucleoproteins: Extension of a biosensor-surface plasmon resonance method.Analytical biochemistry · 2021Article
- Salt bridge dynamics in protein/DNA recognition: a comparative analysis of Elk1 and ETV6.Physical chemistry chemical physics : PCCP · 2021Article
- 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
- Osmotic modulation of chromatin impacts on efficiency and kinetics of cell fate modulation.Scientific reports · 2018Article
- Multiple DNA-binding modes for the ETS family transcription factor PU.1.The Journal of biological chemistry · 2017Article
- Electrostatic control of DNA intersegmental translocation by the ETS transcription factor ETV6.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
- Mixed up minor groove binders: Convincing A·T specific compounds to recognize a G·C base pair.Bioorganic & medicinal chemistry letters · 2015Article
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6 authors.
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Abstract
ETS family transcription factors regulate diverse genes through binding at cognate DNA sites that overlap substantially in sequence. The DNA-binding domains of ETS proteins (ETS domains) are highly conserved structurally yet share limited amino acid homology. To define the mechanistic implications of sequence diversity within the ETS family, we characterized the thermodynamics and kinetics of DNA site recognition by the ETS domains of Ets-1 and PU.1, which represent the extremes in amino acid divergence among ETS proteins. Even though the two ETS domains bind their optimal sites with similar affinities under physiologic conditions, their nature of site recognition differs strikingly in terms of the role of hydration and counter ion release. The data suggest two distinct mechanisms wherein Ets-1 follows a "dry" mechanism that rapidly parses sites through electrostatic interactions and direct protein-DNA contacts, whereas PU.1 utilizes hydration to interrogate sequence-specific sites and form a long-lived complex relative to the Ets-1 counterpart. The kinetic persistence of the high affinity PU.1 · DNA complex may be relevant to an emerging role of PU.1, but not Ets-1, as a pioneer transcription factor in vivo. In addition, PU.1 activity is critical to the development and function of macrophages and lymphocytes, which present osmotically variable environments, and hydration-dependent specificity may represent an important regulatory mechanism in vivo, a hypothesis that finds support in gene expression profiles of primary murine macrophages.
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