Publications
2013
Simonetti A, Marzi S, Billas I M, Tsai A, Fabbretti A, Myasnikov A G, Roblin P, Vaiana A C, Hazemann I, Eiler D, Steitz T A, Puglisi J D, Gualerzi C O, Klaholz B P
Involvement of protein IF2 N domain in ribosomal subunit joining revealed from architecture and function of the full-length initiation factor. Article de journal
Dans: Proc Natl Acad Sci U S A, vol. 110, no. 39, p. 15656-61, 2013, ISBN: 24029017.
Résumé | Liens | BibTeX | Étiquettes: ERIANI, integrated structural biology protein synthesis, ROMBY, Unité ARN
@article{,
title = {Involvement of protein IF2 N domain in ribosomal subunit joining revealed from architecture and function of the full-length initiation factor.},
author = {A Simonetti and S Marzi and I M Billas and A Tsai and A Fabbretti and A G Myasnikov and P Roblin and A C Vaiana and I Hazemann and D Eiler and T A Steitz and J D Puglisi and C O Gualerzi and B P Klaholz},
url = {http://www.ncbi.nlm.nih.gov/pubmed/24029017?dopt=Abstract},
doi = {10.1073/pnas.1309578110},
isbn = {24029017},
year = {2013},
date = {2013-01-01},
journal = {Proc Natl Acad Sci U S A},
volume = {110},
number = {39},
pages = {15656-61},
abstract = {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)-tRNAfMet 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.},
keywords = {ERIANI, integrated structural biology protein synthesis, ROMBY, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
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)-tRNAfMet 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.