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  Structural basis for polyproline-mediated ribosome stalling and rescue by the translation elongation factor EF-P.

Huter, P., Arenz, S., Bock, L. V., Graf, M., Frister, J. O., Heuer, A., et al. (2017). Structural basis for polyproline-mediated ribosome stalling and rescue by the translation elongation factor EF-P. Molecular Cell, 68(3), 515-527. doi:10.1016/j.molcel.2017.10.014.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002E-22D5-8 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002E-22D9-F
Genre: Journal Article

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 Creators:
Huter, P., Author
Arenz, S., Author
Bock, L. V.1, Author              
Graf, M., Author
Frister, J. O.2, Author              
Heuer, A., Author
Peil, L., Author
Starosta, A. L., Author
Wohlgemuth, I.2, Author              
Peske, F.2, Author              
Nováček, J., Author
Berninghausen, O., Author
Grubmüller, H.1, Author              
Tenson, T., Author
Beckmann, R., Author
Rodnina, M. V.2, Author              
Vaiana, A. C.1, Author              
Wilson, D. N., Author
Affiliations:
1Department of Theoretical and Computational Biophysics, MPI for biophysical chemistry, Max Planck Society, ou_578631              
2Department of Physical Biochemistry, MPI for biophysical chemistry, Max Planck Society, ou_578598              

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Free keywords: EF-P, a-IF5A, eIF5A, translation elongation, stalling, prolines, nascent chain, single particle cryo-EM, ribosome, RNA
 Abstract: Ribosomes synthesizing proteins containing consecutive proline residues become stalled and require rescue via the action of uniquely modified translation elongation factors, EF-P in bacteria, or archaeal/eukaryotic a/eIF5A. To date, no structures exist of EF-P or eIF5A in complex with translating ribosomes stalled at polyproline stretches, and thus structural insight into how EF-P/eIF5A rescue these arrested ribosomes has been lacking. Here we present cryo-EM structures of ribosomes stalled on proline stretches, without and with modified EF-P. The structures suggest that the favored conformation of the polyproline-containing nascent chain is incompatible with the peptide exit tunnel of the ribosome and leads to destabilization of the peptidyl-tRNA. Binding of EF-P stabilizes the P-site tRNA, particularly via interactions between its modification and the CCA end, thereby enforcing an alternative conformation of the polyproline-containing nascent chain, which allows a favorable substrate geometry for peptide bond formation.

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Language(s): eng - English
 Dates: 2017-11-022017-11-02
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1016/j.molcel.2017.10.014
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Title: Molecular Cell
Source Genre: Journal
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Pages: - Volume / Issue: 68 (3) Sequence Number: - Start / End Page: 515 - 527 Identifier: -