Unknown

Dataset Information

0

Involvement of protein IF2 N domain in ribosomal subunit joining revealed from architecture and function of the full-length initiation factor.


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)-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.

SUBMITTER: Simonetti A 

PROVIDER: S-EPMC3785770 | biostudies-literature | 2013 Sep

REPOSITORIES: biostudies-literature

altmetric image

Publications

Involvement of protein IF2 N domain in ribosomal subunit joining revealed from architecture and function of the full-length initiation factor.

Simonetti Angelita A   Marzi Stefano S   Billas Isabelle M L IM   Tsai Albert A   Fabbretti Attilio A   Myasnikov Alexander G AG   Roblin Pierre P   Vaiana Andrea C AC   Hazemann Isabelle I   Eiler Daniel D   Steitz Thomas A TA   Puglisi Joseph D JD   Gualerzi Claudio O CO   Klaholz Bruno P BP  

Proceedings of the National Academy of Sciences of the United States of America 20130912 39


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, a  ...[more]

Similar Datasets

| S-EPMC4779312 | biostudies-literature
| S-EPMC2865328 | biostudies-literature
| S-EPMC16334 | biostudies-literature
| PRJEB17706 | ENA
| S-EPMC3439930 | biostudies-literature
| S-EPMC4193923 | biostudies-literature
| S-EPMC7772474 | biostudies-literature
| S-EPMC5338232 | biostudies-literature
| S-EPMC6764996 | biostudies-literature
| S-EPMC1920251 | biostudies-literature