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

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.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002A-7199-3 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002A-719E-A
Genre: Journal Article

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 Creators:
Katoh, T., Author
Wohlgemuth, I.1, Author              
Nagano, M., Author
Rodnina, M. V.1, Author              
Suga, H., Author
Affiliations:
1Department of Physical Biochemistry, MPI for biophysical chemistry, Max Planck Society, ou_578598              

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 Abstract: 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.

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Language(s): eng - English
 Dates: 2016-05-24
 Publication Status: Published online
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 Rev. Method: Peer
 Identifiers: DOI: 10.1038/ncomms11657
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Title: Nature Communications
Source Genre: Journal
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Pages: 12 Volume / Issue: 7 Sequence Number: 11657 Start / End Page: - Identifier: -