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• W1803509301 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." @default.
• W1803509301 created "2016-06-24" @default.
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• W1803509301 date "1994-03-01" @default.
• W1803509301 modified "2023-10-18" @default.
• W1803509301 title "Recognition of a DNA operator by a dimer composed of two different homeodomain proteins." @default.
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• W1803509301 doi "https://doi.org/10.1002/j.1460-2075.1994.tb06397.x" @default.
• W1803509301 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/394961" @default.
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