SGD Paper 
Goutte C and Johnson AD (1994) Recognition of a DNA operator by a dimer composed of two different homeodomain proteins. EMBO J 13(6):1434-42
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.
| Status: Published | Type: Journal Article | PubMed ID: 7907979 |
Topics addressed in this paper
Number of different genes curated to this paper: 3
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