A short, disordered protein region mediates interactions between the homeodomain of the yeast α2 protein and the MCM1 protein

Andrew K. Vershon, Alexander D. Johnson

Research output: Contribution to journalArticle

99 Scopus citations

Abstract

Homeodomains are folded into a characteristic three-dimensional structure capable of recognizing DNA in a sequence-specific manner. We show that correct target site selection by the yeast α2 protein requires, as well as its homeodomain, an adjacent short and apparently unstructured region of the protein. This flexible homeodomain extension is responsible for specifying an interaction with a second regulatory protein, MCM1, which permits the cooperative binding of the two proteins to an operator. Two additional experiments suggest that this extension-homeodomain arrangement is likely to have some generality. First, when the extension of α2 is grafted onto the Drosophila engrailed homeodomain, it yields a protein with the DNA binding specificity of engrailed and the ability to bind cooperatively to DNA with MCM1. Second, the α2 extension specifies interaction not only with the yeast MCM1 protein, but also with the related human protein SRF.

Original languageEnglish (US)
Pages (from-to)105-112
Number of pages8
JournalCell
Volume72
Issue number1
DOIs
StatePublished - Jan 15 1993
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biochemistry, Genetics and Molecular Biology(all)

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