ArticleNucleic acids research2015
Heterogeneous dynamics in DNA site discrimination by the structurally homologous DNA-binding domains of ETS-family transcription factors.
Article in Nucleic acids research, 2015. 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.
- Sphingolipids with 2-hydroxy fatty acids aid in plasma membrane nanodomain organization and oxidative burst.Plant physiology · 2022Article
- 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
- Article
- Multiple DNA-binding modes for the ETS family transcription factor PU.1.The Journal of biological chemistry · 2017Article
- A modular design for minor groove binding and recognition of mixed base pair sequences of DNA.Chemical communications (Cambridge, England) · 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
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Authors and funding
4 authors.
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Abstract
The ETS family of transcription factors exemplifies current uncertainty in how eukaryotic genetic regulators with overlapping DNA sequence preferences achieve target site specificity. PU.1 and Ets-1 represent archetypes for studying site discrimination by ETS proteins because their DNA-binding domains are the most divergent in sequence, yet they share remarkably superimposable DNA-bound structures. To gain insight into the contrasting thermodynamics and kinetics of DNA recognition by these two proteins, we investigated the structure and dynamics of site discrimination by their DNA-binding domains. Electrophoretic mobilities of complexes formed by the two homologs with circularly permuted binding sites showed significant dynamic differences only for DNA complexes of PU.1. Free solution measurements by dynamic light scattering showed PU.1 to be more dynamic than Ets-1; moreover, dynamic changes are strongly coupled to site discrimination by PU.1, but not Ets-1. Interrogation of the protein/DNA interface by DNA footprinting showed similar accessibility to dimethyl sulfate for PU.1/DNA and Ets-1/DNA complexes, indicating that the dynamics of PU.1/DNA complexes reside primarily outside that interface. An information-based analysis of the two homologs' binding motifs suggests a role for dynamic coupling in PU.1's ability to enforce a more stringent sequence preference than Ets-1 and its proximal sequence homologs.
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