RNA Recognition via the SAM Domain of Smaug
| Autor: | Cary D. Gardner, Robin P. Wharton, Justin B. Green, Aneel K. Aggarwal |
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| Rok vydání: | 2003 |
| Předmět: |
Models
Molecular Molecular Sequence Data Static Electricity Repressor RNA-binding protein Biology Crystallography X-Ray Protein Structure Secondary Consensus Sequence Consensus sequence Animals Drosophila Proteins Amino Acid Sequence Molecular Biology Conserved Sequence Genetics Base Sequence Sequence Homology Amino Acid RNA-Binding Proteins RNA Cell Biology Protein Structure Tertiary Cell biology Repressor Proteins Regulatory sequence Mutation Drosophila Smaug Sterile alpha motif Binding domain |
| Zdroj: | Molecular Cell. 11:1537-1548 |
| ISSN: | 1097-2765 |
| Popis: | The Nanos protein gradient in Drosophila, required for proper abdominal segmentation, is generated in part via translational repression of its mRNA by Smaug. We report here the crystal structure of the Smaug RNA binding domain, which shows no sequence homology to any previously characterized RNA binding motif. The structure reveals an unusual makeup in which a SAM domain, a common protein-protein interaction module, is affixed to a pseudo-HEAT repeat analogous topology (PHAT) domain. Unexpectedly, we find through a combination of structural and genetic analysis that it is primarily the SAM domain that interacts specifically with the appropriate nanos mRNA regulatory sequence. Therefore, in addition to their previously characterized roles in protein-protein interactions, some SAM domains play crucial roles in RNA binding. |
| Databáze: | OpenAIRE |
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