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TitleInvolvement of protein IF2 N domain in ribosomal subunit joining revealed from architecture and function of the full-length initiation factor.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 110, Issue 39, Page 15656-15661, Year 2013
Publish dateSep 24, 2013
AuthorsAngelita Simonetti / Stefano Marzi / Isabelle M L Billas / Albert Tsai / Attilio Fabbretti / Alexander G Myasnikov / Pierre Roblin / Andrea C Vaiana / Isabelle Hazemann / Daniel Eiler / Thomas A Steitz / Joseph D Puglisi / Claudio O Gualerzi / Bruno P Klaholz /
PubMed AbstractTranslation initiation factor 2 (IF2) promotes 30S initiation complex (IC) formation and 50S subunit joining, which produces the 70S IC. The architecture of full-length IF2, determined by small angle ...Translation initiation factor 2 (IF2) promotes 30S initiation complex (IC) formation and 50S subunit joining, which produces the 70S IC. The architecture of full-length IF2, determined by small angle X-ray diffraction and cryo electron microscopy, reveals a more extended conformation of IF2 in solution and on the ribosome than in the crystal. The N-terminal domain is only partially visible in the 30S IC, but in the 70S IC, it stabilizes interactions between IF2 and the L7/L12 stalk of the 50S, and on its deletion, proper N-formyl-methionyl(fMet)-tRNA(fMet) positioning and efficient transpeptidation are affected. Accordingly, fast kinetics and single-molecule fluorescence data indicate that the N terminus promotes 70S IC formation by stabilizing the productive sampling of the 50S subunit during 30S IC joining. Together, our data highlight the dynamics of IF2-dependent ribosomal subunit joining and the role played by the N terminus of IF2 in this process.
External linksProc Natl Acad Sci U S A / PubMed:24029017 / PubMed Central
MethodsEM (single particle)
Resolution11.5 Å
Structure data

2448

3j4j

EMDB-2448: Cryo-EM structure of T. thermophilus 30S Translation Initiation complex
PDB-3j4j: Model of full-length T. thermophilus Translation Initiation Factor 2 refined against its cryo-EM density from a 30S Initiation Complex map
Method: EM (single particle) / Resolution: 11.5 Å

Source
  • Thermus thermophilus HB8 (bacteria)
  • synthetic construct (others)
  • Escherichia coli (E. coli)
  • thermus thermophilus (bacteria)
KeywordsTRANSLATION / IF2 / GTP-Binding Protein / fMet-tRNA binding / ribosome binding

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