A multiprotein complex that mediates translational enhancement in Drosophila
| Autor: | Meryl R. Nelson, Heli K. Vari, Hua Luo, Craig A. Smibert, Henry M. Krause, Andrew J. Simmonds, Howard D. Lipshitz, Brian J. Cox |
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| Rok vydání: | 2007 |
| Předmět: |
Untranslated region
Multiprotein complex RNA Stability Biology Biochemistry Poly(A)-Binding Proteins Heterogeneous-Nuclear Ribonucleoproteins Affinity chromatography Animals Drosophila Proteins Binding site Molecular Biology 3' Untranslated Regions Heat-Shock Proteins Genetics Messenger RNA Binding Sites RNA Translation (biology) Cell Biology Cell biology DNA-Binding Proteins Drosophila melanogaster Multiprotein Complexes Protein Biosynthesis Function (biology) |
| Zdroj: | The Journal of biological chemistry. 282(47) |
| ISSN: | 0021-9258 |
| Popis: | Modulating the efficiency of translation plays an important role in a wide variety of cellular processes and is often mediated by trans-acting factors that interact with cis-acting sequences within the mRNA. Here we show that a cis-acting element, the Hsp83 degradation element (HDE), within the 3'-untranslated region of the Drosophila Hsp83 mRNA functions as a translational enhancer. We show that this element is bound by a multiprotein complex, and we identify components using a novel affinity-based method called tandem RNA affinity purification tagging. Three proteins (DDP1, Hrp48, and poly(A)-binding protein) are components of the HDE-binding complex and function in translational enhancement. Our data support a model whereby the HDE is composed of several cis-acting subelements that represent binding sites for trans-acting factors, and the combined action of these trans-acting factors underlies the ability of the HDE to stimulate translation. |
| Databáze: | OpenAIRE |
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