Real-time DNA binding measurements of the ETS1 recombinant oncoproteins reveal significant kinetic differences between the p42 and p51 isoforms.
作者： Robert J. Fisher , Matthew Fivash , Jose Casas-Finet , John W. Erickson , Akiko Kondoh
关键词: Binding site 、 Oligonucleotide 、 DNA binding site 、 Biology 、 Recombinant DNA 、 Point mutation 、 Binding domain 、 Biochemistry 、 DNA 、 HMG-box
摘要: The sequence-specific DNA binding of recombinant p42 and p51 ETS1 oncoprotein was examined quantitatively to determine whether the loss Exon VII phosphorylation domain in or expressed had an effect on activity. kinetics measured using real-time changes surface plasmon resonance with BIAcore (registered trademark, Pharmacia Biosensor) technology. displayed significant differences kinetic behavior. is characterized by a fast initial conversion stable complex, whereas exhibits slow complex. All states are rapid turnover, 4-20 times more stable. A model describing these steps presented. Stoichiometric titrations either specific oligonucleotides show 1:1 complex formation. sequence specificity as determined mutational analysis similar. vitro CAM kinase II obliterates its DNA, suggesting that regulation occurs through calcium-dependent second messenger. lacks this regulatory (Exon VII), not sensitive calcium signaling.
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