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Science 18 May 1990:
Vol. 248. no. 4957, pp. 847 - 850
DOI: 10.1126/science.2111578
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Articles

Science, Vol 248, Issue 4957, 847-850
Copyright © 1990 by American Association for the Advancement of Science

articles

Structural motif of the GCN4 DNA binding domain characterized by affinity cleaving

MG Oakley and PB Dervan

Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena 91125.

The NH2-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.


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