A Heterodimeric Transcriptional Repressor Becomes Crystal Clear
| Autor: | Michael S. Donoviel, Brenda J. Andrews |
|---|---|
| Rok vydání: | 1995 |
| Předmět: |
Operator Regions
Genetic Saccharomyces cerevisiae Proteins Transcription Genetic Macromolecular Substances Protein Conformation Saccharomyces cerevisiae Sequence (biology) Biology Crystallography X-Ray Protein Structure Secondary Fungal Proteins chemistry.chemical_compound DNA Fungal Homeodomain Proteins Genetics Multidisciplinary biology.organism_classification Yeast Protein Structure Tertiary Cell biology Repressor Proteins chemistry Transcriptional Repressor Nucleic Acid Conformation Homeobox Transcription Repressor DNA |
| Zdroj: | Science. 270:251-251 |
| ISSN: | 1095-9203 0036-8075 |
| DOI: | 10.1126/science.270.5234.251 |
| Popis: | The crystal structure of a heterodimeric transcriptional repressor from yeast, a 1/alpha-2, reported in the same issue of Science , reveals a mechanism for ensuring DNA-binding specificity that may be used by many other DNA-binding heterodimers. B. J. Andrews and M. S. Donoviel explain how sequence specificity is controlled by the spacing between the proteins, which must match that of the contact points on the DNA. The carboxyl-terminal tail of alpha-2 is the key interface with a 1 and determines the interprotein distance. |
| Databáze: | OpenAIRE |
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