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Essential structural elements in tRNAPro for EF-P-mediated alleviation of translation stalling.

MPG-Autoren
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Wohlgemuth,  I.
Department of Physical Biochemistry, MPI for biophysical chemistry, Max Planck Society;

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Rodnina,  M. V.
Department of Physical Biochemistry, MPI for biophysical chemistry, Max Planck Society;

Volltexte (frei zugänglich)

2296805.pdf
(Verlagsversion), 734KB

Ergänzendes Material (frei zugänglich)

2296805_Suppl_1.pdf
(Ergänzendes Material), 810KB

2296805_Suppl_2.xls
(Ergänzendes Material), 49KB

Zitation

Katoh, T., Wohlgemuth, I., Nagano, M., Rodnina, M. V., & Suga, H. (2016). Essential structural elements in tRNAPro for EF-P-mediated alleviation of translation stalling. Nature Communications, 7: 11657. doi:10.1038/ncomms11657.


Zitierlink: http://hdl.handle.net/11858/00-001M-0000-002A-7199-3
Zusammenfassung
The ribosome stalls on translation of polyproline sequences due to inefficient peptide bond formation between consecutive prolines. The translation factor EF-P is able to alleviate this stalling by accelerating Pro-Pro formation. However, the mechanism by which EF-P recognizes the stalled complexes and accelerates peptide bond formation is not known. Here, we use genetic code reprogramming through a flexible in-vitro translation (FIT) system to investigate how mutations in tRNAPro affect EF-P function. We show that the 9-nt D-loop closed by the stable D-stem sequence in tRNAPro is a crucial recognition determinant for EF-P. Such D-arm structures are shared only among the tRNAPro isoacceptors and tRNAfMet in Escherichia coli, and the D-arm of tRNAfMet is essential for EF-P-induced acceleration of fMet–puromycin formation. Thus, the activity of EF-P is controlled by recognition elements in the tRNA D-arm.