作者: Hernán Terenzi , Isabelle Petropoulos , Christine Ellouze , Masayuki Takahashi , Mario M. Zakin
DOI: 10.1016/0014-5793(95)00767-4
关键词: DNA 、 DNA binding site 、 Transcription factor 、 Binding domain 、 HMG-box 、 Enhancer 、 Protein–DNA interaction 、 DNA-binding domain 、 Biology 、 Biochemistry 、 Biophysics 、 Genetics 、 Cell biology 、 Molecular biology 、 Structural biology
摘要: Abstract Transferrin hepato-specific gene enhancer, associated with the liver-enriched HNF-3α transcriptional factor and ubiquitous proteins, is a complex molecular edifice maintained through DNA-protein protein-protein interactions. As first step to understand mechanisms responsible for its organization activity, we have analyzed interaction of DNA binding domain (HDBD) specific segment present in transferrin enhancer by different biophysical techniques. The kinetic constants this were measured using surface plasmon resonance. HDBD-DNA was also characterized circular dichroism fluorescence spectroscopy. HDBD binds site high affinity ( K d ≊10 −8 M ). reduced after sequence modification target DNA. Size exclusion chromatography stoichiometry determined measurements indicate that protein monomeric form before secondary structure not significantly altered upon By contrast, structural change seems occur.