Structural Basis for Polyproline-Mediated Ribosome Stalling and Rescue by the Translation Elongation Factor EF-P

2017-11-02 | journal article

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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. & Peil, L. et al.​ (2017) 
Molecular cell68(3) pp. 515.e6​-527.e6​.​ DOI: https://doi.org/10.1016/j.molcel.2017.10.014 

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Authors
Huter, Paul; Arenz, Stefan; Bock, Lars V. ; Graf, Michael; Frister, Jan Ole; Heuer, Andre; Peil, Lauri; Starosta, Agata L.; Wohlgemuth, Ingo ; Peske, Frank ; Nováček, Jiří; Berninghausen, Otto; Grubmüller, Helmut ; Tenson, Tanel; Beckmann, Roland; Rodnina, Marina V. ; Vaiana, Andrea C. ; Wilson, Daniel N.
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.
Issue Date
2-November-2017
Journal
Molecular cell 
eISSN
1097-4164
Language
English

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