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| Content Provider | PubMed Central |
|---|---|
| Author | Fekete, Christie A. Applefield, Drew J. Blakely, Stephen A. Nikolay, Shirokikh Pestova, Tatyana Lorsch, Jon R. Hinnebusch, Alan G. |
| Copyright Year | 2005 |
| Abstract | Translation initiation factor 1A stimulates 40S-binding of the eukaryotic initiation factor 2 (eIF2)/GTP/Met-tRNAi Met ternary complex (TC) and promotes scanning in vitro. eIF1A contains an OB-fold present in bacterial IF1 plus N- and C-terminal extensions. Truncating the C-terminus (ΔC) or mutating OB-fold residues (66–70) of eIF1A reduced general translation in vivo but increased GCN4 translation (Gcd− phenotype) in a manner suppressed by overexpressing TC. Consistent with this, both mutations diminished 40S-bound TC, eIF5 and eIF3 in vivo, and ΔC impaired TC recruitment in vitro. The assembly defects of the OB-fold mutation can be attributed to reduced 40S-binding of eIF1A, whereas ΔC impairs eIF1A function on the ribosome. A substitution in the C-terminal helix (98–101) also reduced 43S assembly in vivo. Rather than producing a Gcd− phenotype, however, 98–101 impairs GCN4 derepression in a manner consistent with defective scanning by reinitiating ribosomes. Indeed, 98–101 allows formation of aberrant 48S complexes in vitro and increases utilization of non-AUG codons in vivo. Thus, the OB-fold is crucial for ribosome-binding and the C-terminal domain of eIF1A has eukaryotic-specific functions in TC recruitment and scanning. |
| Related Links | http://dx.doi.org/10.1038/sj.emboj.7600821 |
| Starting Page | 3588 |
| File Format | |
| ISSN | 14602075 |
| e-ISSN | 14602075 |
| Journal | The EMBO Journal |
| Issue Number | 20 |
| Volume Number | 24 |
| Language | English |
| Publisher Date | 2005-10-19 |
| Access Restriction | Open |
| Subject Keyword | Research in Higher Education |
| Content Type | Text |
| Resource Type | Article |
| Subject | Neuroscience Immunology and Microbiology Medicine Molecular Biology |
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