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

FEBS Letters

Shi, Jianxia²  Crute, Barbara E.¹  Laue, Thomas M.³  Huang, Xuemei²  Bushweller, John H.²  Kelley, John J.²  Tang, Yen-Yee¹  Yan, Jiangli²  Hartman, Kari L.³  Speck, Nancy A.¹ 

[1] Department of Biochemistry, Dartmouth Medical School, Hanover, NH 03755, USA;Department of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville, VA 22906-0011, USA;Department of Biochemistry, University of New Hampshire, Durham, NH 03824, USA

关键词: Core binding factor;    AML1;    Runx1;    Core binding factor β;    Transcription;    Biophysical;   

DOI  :  10.1016/S0014-5793(00)01312-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown