|Title||MODULATION OF TRANSCRIPTION FACTOR ETS-1 DNA-BINDING - DNA-INDUCED UNFOLDING OF AN ALPHA-HELIX|
|Publication Type||Journal Article|
|Year of Publication||1995|
|Authors||Petersen, JM, Skalicky, JJ, Donaldson, LW, McIntosh, LP, Alber, T, Graves, BJ|
|Type of Article||Article|
|Keywords||BASIC REGION, CRYSTAL-STRUCTURE, DOMAIN, FAMILY, GCN4, INDUCED CONFORMATIONAL CHANGE, PROTEIN-KINASES, REPRESSOR, SEQUENCE, SUBUNITS|
Conformational changes, including local protein folding, play important roles in protein-DNA interactions. Here, studies of the transcription factor Ets-1 provided evidence that local protein unfolding also can accompany DNA binding. Circular dichroism and partial proteolysis showed that the secondary structure of the Ets-1 DNA-binding domain is unchanged in the presence of DNA. In contrast, DNA allosterically induced the unfolding of an cr helix that lies within a flanking region involved in the negative regulation of DNA binding. These findings suggest a structural basis for the intramolecular inhibition of DNA binding and a mechanism for the cooperative partnerships that are common features of many eukaryotic transcription factors.
|URL||<Go to ISI>://A1995RX19400036|