Structural Determination of Functional Domains in Early B-cell Factor (EBF) Family of Transcription Factors Reveals Similarities to Rel DNA-binding Proteins and a Novel Dimerization Motif
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The early B-cell factor (EBF) transcription factors are central regulators of development in several organs and tissues. This protein family shows low sequence similarity to other protein families, which is why structural information for the functional domains of these proteins is crucial to understand their biochemical features. We have used a modular approach to determine the crystal structures of the structured domains in the EBF family. The DNA binding domain reveals a striking resemblance to the DNA binding domains of the Rel homology superfamily of transcription factors but contains a unique zinc binding structure, termed zinc knuckle. Further the EBF proteins contain an IPT/TIG domain and an atypical helix-loop-helix domain with a novel type of dimerization motif. The data presented here provide insights into unique structural features of the EBF proteins and open possibilities for detailed molecular investigations of this important transcription factor family.
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Similar interactions between homologues have been reported for many other transcription factor families, such as Ebf and Irx.
“Similar interactions between homologues have been reported for many other transcription factor families, such as Ebf98 and Irx99.”
From A high-resolution transcriptomic and spatial atlas of cell types in the whole mouse brain (2023) · cites this paper as [98]
The Results (page unavailable) report dimer formation in both EBF1 and EBF3 crystals, supporting interactions between EBF molecules. They do not report an interaction between different EBF homologues, such as EBF1 with EBF3. The separate Irx citation is outside the scope of this verdict. (LLM, conf=0.83)
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A high-resolution transcriptomic and spatial atlas of cell types in the whole mouse brain
Yao, Z., van Velthoven, C. T. J., Kunst, M., Zhang, M., McMillen, D., Lee, C., Jung, W., Goldy, J., Abdelhak, A., Aitken, M., et al. (2023) · Nature · doi:10.1038/s41586-023-06812-z · Cited by 1,194 · see citing works
- Authors
- Siponen, M. I., Wisniewska, M., Lehtiö, L., Johansson, I., Svensson, L., Raszewski, G., Nilsson, L., Sigvardsson, M., & Berglund, H.
- Affiliations
- Karolinska Institutet (SE)
- Åbo Akademi University (FI)
- Linköping University (SE)
- Corresponding author
- Berglund, Helena
- ORCID
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2010-08
- Volume
- 285
- Issue
- 34
- Pages
- 25875-25879
- ISSN
- 0021-9258 (ISSN-L)
- PMC
- PMC2923972
- OpenAlex
- W2077599560
- Cited by
- 34
- References
- 37
- Citations by year
- 2026: 2 · 2025: 1 · 2024: 2 · 2023: 4 · 2022: 3 · 2021: 2 · 2020: 3 · 2018: 1 · 2017: 3 · 2016: 1 · 2014: 5 · 2013: 2 · 2012: 1
- FWCI
- 0.91
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by-nc)
- PubMed (publishedVersion)
- KTH Publication Database DiVA (KTH Royal Institute of Technology) (submittedVersion, other-oa)
- HZB Repository (Helmholtz-Zentrum Berlin für Materialien und Energie GmbH (HZB)) (submittedVersion, other-oa)
- Funders
- GlaxoSmithKline
- Ontario Innovation Trust
- Genome Canada
- Wellcome Trust (1097737)
- Ontario Genomics
- Ontario Genomics Institute
- Stiftelsen för Strategisk Forskning
- Academy of Finland (128322)
- Karolinska Institutet
- Knut och Alice Wallenbergs Stiftelse
- Canadian Institutes of Health Research
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Keywords
- early B cell factor, Rel homology domain, helix-loop-helix domain, DNA-binding domain, protein crystal structure, transcription factor structure
- MeSH terms
- Humans, Protein Conformation, Transcription Factors, Zinc, Trans-Activators, Crystallography, X-Ray, Proto-Oncogene Proteins c-rel, Structural Homology, Protein, Protein Interaction Domains and Motifs, Protein Multimerization
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