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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Marintchev, Assen Wagner, Gerhard Asano, Katsura Yamamoto, Yasufumi Hannig, Ernest M. Singh, Chingakham Ranjit Hall, Nathan S. |
| Description | Author Affiliation: Yamamoto Y ( Molecular Cellular Developmental Biology Program, Division of Biology, Kansas State University, Manhattan, KS 66506, USA.); |
| Abstract | Eukaryotic translation initiation factor (eIF) 5 is crucial for the assembly of the eukaryotic preinitiation complex. This activity is mediated by the ability of its C-terminal HEAT domain to interact with eIF1, eIF2, and eIF3 in the multifactor complex and with eIF4G in the 48S complex. However, the binding sites for these factors on eIF5-C-terminal domain (CTD) have not been known. Here we present a homology model for eIF5-CTD based on the HEAT domain of eIF2Bepsilon. We show that the binding site for eIF2beta is located in a surface area containing aromatic and acidic residues (aromatic/acidic boxes), that the binding sites for eIF1 and eIF3c are located in a conserved surface region of basic residues, and that eIF4G binds eIF5-CTD at an interface overlapping with the acidic area. Mutations in these distinct eIF5 surface areas impair GCN4 translational control by disrupting preinitiation complex interactions. These results indicate that the eIF5 HEAT domain is a critical nucleation core for preinitiation complex assembly and function. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 45 |
| Volume Number | 102 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 2005-11-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Eukaryotic Initiation Factor-1 Chemistry Eukaryotic Initiation Factor-2 Eukaryotic Initiation Factor-3 Eukaryotic Initiation Factor-4G Eukaryotic Initiation Factor-5 Protein Biosynthesis Binding Sites Physiology Mutation Protein Structure, Secondary Protein Structure, Tertiary Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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