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• W2129793865 endingPage "2073" @default.
• W2129793865 startingPage "2065" @default.
• W2129793865 abstract "DNA binding by the eukaryotic transcription factor Ets-1 is negatively regulated by an intramolecular mechanism. Quantitative binding assays compared the DNA-binding activities of native Ets-1, three deletion mutants, and three tryptic fragments. Ets-1 and activated Ets-1 polypeptides differed in DNA-binding affinity as much as 23-fold. Inhibition was mediated by two regions flanking the minimal DNA-binding domain. Both regions regulated affinity by enhancing dissociation of the protein-DNA complex. Three lines of evidence indicated that inhibition requires cooperative interaction between the two regions: first, the two inhibitory regions acted through a common mechanism; second, neither region functioned independently of the other; finally, mutation of the C-terminal inhibitory region altered the conformation of the N-terminal inhibitory region. In addition, partial proteolysis detected an identical altered conformation in the N-terminal inhibitory region of Ets-1 bound to DNA. This finding suggested that repression is transiently disrupted during DNA binding. These results provide evidence that the two inhibitory regions of Ets-1 are structurally, as well as functionally, coupled. In addition, conformational change is shown to be a critical component of the inhibition mechanism. A cooperative, allosteric model of autoinhibition is described. Autoinhibition of Ets-1 could be relieved by either protein partner(s) or posttranslational modifications." @default.
• W2129793865 created "2016-06-24" @default.
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• W2129793865 date "1996-05-01" @default.
• W2129793865 modified "2023-10-16" @default.
• W2129793865 title "Characterization of the Cooperative Function of Inhibitory Sequences in Ets-1" @default.
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• W2129793865 doi "https://doi.org/10.1128/mcb.16.5.2065" @default.
• W2129793865 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/231193" @default.
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