Human eIF5 and eIF1A Compete for Binding to eIF5B
| العنوان: | Human eIF5 and eIF1A Compete for Binding to eIF5B |
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| المؤلفون: | Assen Marintchev, Tatyana V. Pestova, Kai Ying Lin, Nabanita Nag |
| المصدر: | Biochemistry. 57:5910-5920 |
| بيانات النشر: | American Chemical Society (ACS), 2018. |
| سنة النشر: | 2018 |
| مصطلحات موضوعية: | 0301 basic medicine, eIF2, Chemistry, Protein subunit, Nerve Tissue Proteins, GTPase, RNA, Transfer, Amino Acyl, Biochemistry, Ribosome, Article, Neoplasm Proteins, Cell biology, 03 medical and health sciences, 030104 developmental biology, Eukaryotic translation, Start codon, Transcription preinitiation complex, Humans, Initiation factor, Guanosine Triphosphate, Eukaryotic Initiation Factors, Ribosomes, Protein Binding |
| الوصف: | Eukaryotic translation initiation is a multistep process requiring a number of eukaryotic translation initiation factors (eIFs). Two GTPases play key roles in the process. eIF2 brings the initiator Met-tRNA(i) to the pre-initiation complex (PIC). Upon start codon selection and GTP hydrolysis promoted by the GTPase-activating protein (GAP) eIF5, eIF2-GDP is displaced from Met-tRNA(i) by eIF5B-GTP and is released in complex with eIF5. eIF5B promotes ribosomal subunit joining, with the help of eIF1A. Upon subunit joining, eIF5B hydrolyzes GTP and is released together with eIF1A. We found that human eIF5 interacts with eIF5B and may help recruit eIF5B to the PIC. An eIF5B-binding motif was identified at the C-terminus of eIF5, similar to that found in eIF1A. Indeed, eIF5 competes with eIF1A for binding and has ~100-fold higher affinity for eIF5B. Since eIF5 is the GAP of eIF2, the newly discovered interaction offers a possible mechanism for coordination between the two steps in translation initiation controlled by GTPases: start codon selection and ribosomal subunit joining. Our results indicate that in human, eIF5B displacing eIF2 from Met-tRNA(i) upon subunit joining may be coupled to eIF1A displacing eIF5 from eIF5B, allowing the eIF5:eIF2-GDP complex to leave the ribosome. |
| تدمد: | 1520-4995 0006-2960 |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::04ff06a7a099cdc94d185ed489b429f8 https://doi.org/10.1021/acs.biochem.8b00839 |
| حقوق: | OPEN |
| رقم الأكسشن: | edsair.doi.dedup.....04ff06a7a099cdc94d185ed489b429f8 |
| قاعدة البيانات: | OpenAIRE |
Find this issue from the American Chemical Society | تدمد: | 15204995 00062960 |
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