ArticleNucleic acids research1997
Homeodomain-DNA interactions of the Pho2 protein are promoter-dependent.
Article in Nucleic acids research, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 12 citations in OpenAlex.
- Identification of Homeobox Transcription Factors in a Dimorphic FungusJournal of fungi (Basel, Switzerland) · 2024Article
- Article
- Max-E47, a designed minimalist protein that targets the E-box DNA site in vivo and in vitro.Journal of the American Chemical Society · 2009Article
- A phage display selection of engrailed homeodomain mutants and the importance of residue Q50.Nucleic acids research · 2004Article
- Interactions of the Mcm1 MADS box protein with cofactors that regulate mating in yeast.Molecular and cellular biology · 2002Article
- Mutations in the yeast Myb-like protein Bas1p resulting in discrimination between promoters in vivo but notin vitro.Nucleic acids research · 1998Article
- Cooperative Pho2-Pho4 interactions at the PHO5 promoter are critical for binding of Pho4 to UASp1 and for efficient transactivation by Pho4 at UASp2.Molecular and cellular biology · 1998Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The homeodomain (HD) is a conserved sequence-specific DNA-binding motif found in many eukaryotic transcriptional regulatory proteins. Despite the wealth of in vitro data on the mechanism HD proteins use to bind DNA, comparatively little is known about the roles of individual residues in these domains in vivo . The Saccharomyces cerevisiae Pho2 protein contains a HD that shares significant sequence identity with the Drosophila Engrailed protein. We have used the co-crystal structure of Engrailed as a model to predict how Pho2 might contact DNA and have examined how individual residues of the Pho2 HD contribute to transcriptional activation in vivo and to DNA binding in vitro. Our results demonstrate that Pho2 and Engrailed share many similar DNA-binding characteristics. However, our results also show that some highly conserved residues, which contact the DNA in many HD structures, make relatively small contributions to the DNA-binding affinity and in vivo activity of the Pho2 protein. We also show that the N-terminal arm of the Pho2 HD is a critical component in determining the DNA-binding specificity of the protein and that the requirements for residues in the N-terminal arm are promoter-dependent for Pho2 transcriptional activation and DNA binding.
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