Biophysical characterization of interactions between the core binding factor α and β subunits and DNA

Core binding factors (CBFs) play key roles in several developmental pathways and in human disease. CBFs consist of a DNA binding CBFα subunit and a non-DNA binding CBFβ subunit that increases the affinity of CBFα for DNA. We performed sedimentation equilibrium analyses to unequivocally establish the...

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Bibliographic Details
Published in:FEBS letters 2000-03, Vol.470 (2), p.167-172
Main Authors: Tang, Yen-Yee, Crute, Barbara E., Kelley, John J., Huang, Xuemei, Yan, Jiangli, Shi, Jianxia, Hartman, Kari L., Laue, Thomas M., Speck, Nancy A., Bushweller, John H.
Format: Article
Language:English
Subjects:
AML1
Animals
Biophysical
Calorimetry
Circular Dichroism
Core binding factor
Core Binding Factor Alpha 2 Subunit
Core Binding Factor alpha Subunits
Core binding factor β
Dimerization
DNA - chemistry
DNA - genetics
DNA - metabolism
DNA-Binding Proteins - chemistry
DNA-Binding Proteins - metabolism
Models, Molecular
Molecular Weight
Nuclear Magnetic Resonance, Biomolecular
Protein Binding
Protein Structure, Tertiary
Proto-Oncogene Proteins
Runx1
Thermodynamics
Transcription
Transcription Factor AP-2
Transcription Factors - chemistry
Transcription Factors - metabolism
Ultracentrifugation
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Summary:Core binding factors (CBFs) play key roles in several developmental pathways and in human disease. CBFs consist of a DNA binding CBFα subunit and a non-DNA binding CBFβ subunit that increases the affinity of CBFα for DNA. We performed sedimentation equilibrium analyses to unequivocally establish the stoichiometry of the CBFα:β:DNA complex. Dissociation constants for all four equilibria involving the CBFα Runt domain, CBFβ, and DNA were defined. Conformational changes associated with interactions between CBFα, CBFβ, and DNA were monitored by nuclear magnetic resonance and circular dichroism spectroscopy. The data suggest that CBFβ ‘locks in’ a high affinity DNA binding conformation of the CBFα Runt domain.
ISSN:0014-5793
1873-3468
DOI:10.1016/S0014-5793(00)01312-0