A Genetic Model for Interaction of the Homeodomain Recognition Helix with DNA
- 25 January 1991
- journal article
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 251 (4992) , 426-430
- https://doi.org/10.1126/science.1671176
Abstract
The Bicoid homeodomain protein controls anterior development in the Drosophila embryo by binding to DNA and regulating gene expression. With the use of genetic assays in yeast, the interaction between the Bicoid homeodomain and a series of mutated DNA sites was studied. These experiments defined important features of homeodomain binding sites, identified specific amino acid-base pair contacts, and suggested a model for interaction of the recognition alpha-helices of Bicoid and Antennapedia-class homeodomain proteins with DNA. The model is in general agreement with results of crystallographic and magnetic resonance studies, but differs in important details. It is likely that genetic studies of protein-DNA interaction will continue to complement conventional structural approaches.Keywords
This publication has 37 references indexed in Scilit:
- Determination of spatial domains of zygotic gene expression in the Drosophila embryo by the affinity of binding sites for the bicoid morphogenNature, 1989
- DNA specificity of the bicoid activator protein is determined by homeodomain recognition helix residue 9Cell, 1989
- The gradient morphogen bicoid is a concentration-dependent transcriptional activatorCell, 1989
- The Drosophila fushi tarazu polypeptide is a DNA-binding transcriptional activator in yeast cellsNature, 1989
- The bicoid protein determines position in the Drosophila embryo in a concentration-dependent mannerPublished by Elsevier ,1988
- A new-specificity mutant of 434 repressor that defines an amino acid–base pair contactNature, 1987
- How λ repressor and λ Cro distinguish between OR1 and OR3Cell, 1986
- Homologous interactions of λ repressor and λ Cro with the λ operatorCell, 1986
- A eukaryotic transcriptional activator bearing the DNA specificity of a prokaryotic repressorCell, 1985
- Changing the binding specificity of a represser by redesigning an α-helixNature, 1985