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TitleeIF3 Peripheral Subunits Rearrangement after mRNA Binding and Start-Codon Recognition.
Journal, issue, pagesMol Cell, Vol. 63, Issue 2, Page 206-217, Year 2016
Publish dateJul 21, 2016
AuthorsAngelita Simonetti / Jailson Brito Querido / Alexander G Myasnikov / Eder Mancera-Martinez / Adeline Renaud / Lauriane Kuhn / Yaser Hashem /
PubMed AbstractmRNA translation initiation in eukaryotes requires the cooperation of a dozen eukaryotic initiation factors (eIFs) forming several complexes, which leads to mRNA attachment to the small ribosomal ...mRNA translation initiation in eukaryotes requires the cooperation of a dozen eukaryotic initiation factors (eIFs) forming several complexes, which leads to mRNA attachment to the small ribosomal 40S subunit, mRNA scanning for start codon, and accommodation of initiator tRNA at the 40S P site. eIF3, composed of 13 subunits, 8 core (a, c, e, f, h, l, k, and m) and 5 peripheral (b, d, g, i, and j), plays a central role during this process. Here we report a cryo-electron microscopy structure of a mammalian 48S initiation complex at 5.8 Å resolution. It shows the relocation of subunits eIF3i and eIF3g to the 40S intersubunit face on the GTPase binding site, at a late stage in initiation. On the basis of a previous study, we demonstrate the relocation of eIF3b to the 40S intersubunit face, binding below the eIF2-Met-tRNAi(Met) ternary complex upon mRNA attachment. Our analysis reveals the deep rearrangement of eIF3 and unravels the molecular mechanism underlying eIF3 function in mRNA scanning and timing of ribosomal subunit joining.
External linksMol Cell / PubMed:27373335
MethodsEM (single particle)
Resolution4.9 - 5.8 Å
Structure data

8190

5k0y

EMDB-8190, PDB-5k0y:
m48S late-stage initiation complex, purified from rabbit reticulocytes lysates, displaying eIF2 ternary complex and eIF3 i and g subunits relocated to the intersubunit face
Method: EM (single particle) / Resolution: 5.8 Å

8195

5k1h

EMDB-8195: m48S late-stage initiation complex, purified from rabbit reticulocytes lysates, displaying eIF2 ternary complex and eIF3 i and g subunits relocated to the intersubunit face
PDB-5k1h: eIF3b relocated to the intersubunit face to interact with eIF1 and below the eIF2 ternary-complex. from the structure of a partial yeast 48S preinitiation complex in closed conformation.
Method: EM (single particle) / Resolution: 5.8 Å

Source
  • oryctolagus cuniculus (rabbit)
  • homo sapiens (human)
KeywordsTRANSLATION / eukaryotic translation initiation / ribosome / eIF3 peripheral subunits / cryo-EM

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