ArticleNucleic acids research2018
Mapping interfacial hydration in ETS-family transcription factor complexes with DNA: a chimeric approach.
Article in Nucleic acids research, 2018. 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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Who cites it
11 citing papers in PubMed, 12 citations in OpenAlex.
- 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
- Dissection of integrated readout reveals the structural thermodynamics of DNA selection by transcription factors.Structure (London, England : 1993) · 2024Article
- DNA selection by the master transcription factor PU.1.Cell reports · 2023Article
- Total free energy analysis of fully hydrated proteins.Proteins · 2023Article
- Isolevuglandins disrupt PU.1-mediated C1q expression and promote autoimmunity and hypertension in systemic lupus erythematosus.JCI insight · 2022Article
- The Non-continuum Nature of Eukaryotic Transcriptional Regulation.Advances in experimental medicine and biology · 2022Article
- DNA-facilitated target search by nucleoproteins: Extension of a biosensor-surface plasmon resonance method.Analytical biochemistry · 2021Article
- Constrained chromatin accessibility in PU.1-mutated agammaglobulinemia patients.The Journal of experimental medicine · 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
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Hydration of interfaces is a major determinant of target specificity in protein/DNA interactions. Interfacial hydration is a highly variable feature in DNA recognition by ETS transcription factors and functionally relates to cellular responses to osmotic stress. To understand how hydration is mediated in the conserved ETS/DNA binding interface, secondary structures comprising the DNA contact surface of the strongly hydrated ETS member PU.1 were substituted, one at a time, with corresponding elements from its sparsely hydrated relative Ets-1. The resultant PU.1/Ets-1 chimeras exhibited variably reduced sensitivity to osmotic pressure, indicative of a distributed pattern of interfacial hydration in wildt-ype PU.1. With the exception of the recognition helix H3, the chimeras retained substantially high affinities. Ets-1 residues could therefore offset the loss of favorable hydration contributions in PU.1 via low-water interactions, but at the cost of decreased selectivity at base positions flanking the 5'-GGA-3' core consensus. Substitutions within H3 alone, which contacts the core consensus, impaired binding affinity and PU.1 transactivation in accordance with the evolutionary separation of the chimeric residues involved. The combined biophysical, bioinformatics and functional data therefore supports hydration as an evolved specificity determinant that endows PU.1 with more stringent sequence selection over its ancestral relative Ets-1.
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