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Biophysical characterization of interactions between the core binding factor α and β subunits and DNA
Author(s) -
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.
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)01312-0
Subject(s) - dna , core binding factor , biophysics , chemistry , circular dichroism , nuclear magnetic resonance spectroscopy , protein subunit , biochemistry , biology , stereochemistry , transcription factor , gene
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.