Structural Dynamics of Bacterial Translation Initiation Factor IF2

H.L.J. Wienk, E. Tishchenko, R. Belardinelli, S. Tomaselli, R. Dongre, R. Spurio, G.E. Folkers, C.O. Gualerzi, R. Boelens

Research output: Contribution to journalArticleAcademicpeer-review

Abstract

Bacterial translation initiation factor IF2 promotes ribosomal subunit association, recruitment, and binding of fMet-tRNA to the ribosomal P-site and initiation dipeptide formation. Here, we present the solution structures of GDP-bound and apo-IF2-G2 of Bacillus stearothermophilus and provide evidence that this isolated domain binds the 50 S ribosomal subunit and hydrolyzes GTP. Differences between the free and GDP-bound structures of IF2-G2 suggest that domain reorganization within the G2-G3-C1 regions underlies the different structural requirements of IF2 during the initiation process. However, these structural signals are unlikely forwarded from IF2-G2 to the C-terminal fMet-tRNA binding domain (IF2-C2) because the connected IF2-C1 and IF2-C2 modules show completely independent mobility, indicating that the bacterial interdomain connector lacks the rigidity that was found in the archaeal IF2 homolog aIF5B.
Original languageEnglish
Pages (from-to)10922-10932
Number of pages19
JournalJournal of Biological Chemistry
Volume287
Issue number14
DOIs
Publication statusPublished - 2012

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