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. 1994 Mar 15;13(6):1434–1442. doi: 10.1002/j.1460-2075.1994.tb06397.x

Recognition of a DNA operator by a dimer composed of two different homeodomain proteins.

C Goutte 1, A D Johnson 1
PMCID: PMC394961  PMID: 7907979

Abstract

The yeast homeodomain proteins a1 and alpha 2 interact to form a heterodimer that binds DNA with high specificity. The DNA recognition element consists of two similar half sites, arranged with dyad symmetry and separated by a fixed number of base pairs. We demonstrate that in the a1 alpha 2-DNA complex, one of these half-sites is bound by a1 while the other is bound by alpha 2. These assignments allow a comparison of the chemical and nuclease protection patterns produced by both proteins when bound together to the hsg operator. Contrary to simple expectations, we propose that the a1 and alpha 2 homeodomains are arranged on the DNA in tandem, despite the fact that the recognition sequence is dyad symmetric.

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