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MODULATION OF TRANSCRIPTION FACTOR ETS-1 DNA-BINDING - DNA-INDUCED UNFOLDING OF AN ALPHA-HELIX

TitleMODULATION OF TRANSCRIPTION FACTOR ETS-1 DNA-BINDING - DNA-INDUCED UNFOLDING OF AN ALPHA-HELIX
Publication TypeJournal Article
Year of Publication1995
AuthorsPetersen, JM, Skalicky, JJ, Donaldson, LW, McIntosh, LP, Alber, T, Graves, BJ
JournalScience
Volume269
Pagination1866-1869
Date PublishedSep
Type of ArticleArticle
ISBN Number0036-8075
KeywordsBASIC REGION, CRYSTAL-STRUCTURE, DOMAIN, FAMILY, GCN4, INDUCED CONFORMATIONAL CHANGE, PROTEIN-KINASES, REPRESSOR, SEQUENCE, SUBUNITS
Abstract

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