Structural motif of the GCN4 DNA binding domain characterized by affinity cleaving
- Creators
- Oakley, Martha G.
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Dervan, Peter B.
Abstract
The NH_2-terminal locations of a dimer containing the DNA binding domain of the yeast transcriptional activator GCN4 have been mapped on the binding sites 5'-CTGACTAAT-3' and 5'-ATGACTCTT-3'. Affinity cleaving was effected by synthetic GCN4 proteins with Fe.EDTA moieties at the NH2-terminus. Analysis of the DNA cleavage patterns for dimers of the Fe·EDTA-proteins corresponding to GCN4 residues 222 to 281 and 226 to 281 revealed that the NH2-termini were in the major groove nine to ten base pairs apart and were symmetrically displaced four to five base pairs from the central C of the recognition site. This result is consistent with the Y-shaped scissor grip-leucine zipper model recently proposed for a class of DNA binding proteins important in the regulation of gene expression.
Additional Information
© 1990 American Association for the Advancement of Science. 16 January 1990; accepted 23 March 1990. Supported by grants from the DARPA University Research Initiative Program, the National Foundation for Cancer Research, and an NSF predoctoral fellowship to M.G.O. We thank C. S. Parker for the plasmid pARE/GCRE (18).Additional details
- Eprint ID
- 66966
- Resolver ID
- CaltechAUTHORS:20160510-155633674
- Defense Advanced Research Projects Agency (DARPA)
- National Foundation for Cancer Research
- NSF Predoctoral Fellowship
- Created
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2016-05-19Created from EPrint's datestamp field
- Updated
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2021-11-11Created from EPrint's last_modified field