An inhibitory domain of E12 transcription factor prevents DNA binding in E12 homodimers but not in E12 heterodimers
- Creators
- Sun, Xiao-Hong
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Baltimore, David
Abstract
The κE2 sequence binding proteins, E12 and E47, are generated by alternative splicing of the E2A gene, giving closely related basic and helix-loop-helix structures crucial for DNA binding and dimerization. Measurements of dimerization constants and binding strengths to the optimal DNA sequence (the κE2 site or its near relatives) showed that E47 homodimers and MyoD heterodimers with E12 or E47 dimerized and bound avidly, but E12 homodimerized efficiently and bound to DNA poorly; MyoD homodimerized poorly and bound strongly. An inhibitory domain N-terminal to the basic region of E12 prevents E12 homodimers but not E12/MyoD heterodimers from binding to DNA. Thus, E47 binds to DNA both as a heterodimer with MyoD and as a homodimer, while E12 and MyoD bind to DNA efficiently only as heterodimers.
Additional Information
© 1991 by Cell Press. Received 25 June 1990, Revised 26 September 1990. We are grateful to S. Ghosh, C. Murre, P. Jackson, and R. Andino for helpful advice and discussions. X.-H.S. was supported by a postdoctoral fellowship from the Cancer Research Institute. This work was supported by Public Health Service grant #GM39458. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 USC Section 1734 solely to indicate this fact.Additional details
- Eprint ID
- 103259
- Resolver ID
- CaltechAUTHORS:20200518-075320939
- Cancer Research Institute
- GM39458
- NIH
- Created
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2020-05-18Created from EPrint's datestamp field
- Updated
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2023-06-01Created from EPrint's last_modified field