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

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Structural Basis for Polyproline-Mediated Ribosome Stalling and Rescue by the Translation ...

Přehled o publikaci

J 2017

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

HUTER, P.; S. ARENZ; L.V. BOCK; M. GRAF; J.O. FRISTER et. al.

Základní údaje

Originální název

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

Autoři

Vydání

Molecular Cell, CAMBRIDGE, CELL PRESS, 2017, 1097-2765

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Stát vydavatele

Spojené státy

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Kód RIV

RIV/00216224:14740/17:00100397

Organizace

Středoevropský technologický institut – Masarykova univerzita – Repozitář

UT WoS

000414250700007

Klíčová slova anglicky

PEPTIDE-BOND FORMATION; AMINOACYL-TRANSFER-RNA; MOLECULAR-DYNAMICS; PROTEIN-SYNTHESIS; 70S RIBOSOME; CRYO-EM; CRYSTAL-STRUCTURE; PROLINE RESIDUES; FACTOR EIF5A; MECHANISM

Návaznosti

LM2015043, projekt VaV.

Změněno: 5. 9. 2020 12:41, RNDr. Daniel Jakubík

Anotace

V originále

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 peptidyltRNA. 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.

Přiložené soubory

https://is.muni.cz/publication/1411418/Huter_EFP_text_figures_110817_LR.pdf Verze souboru

Citovat

HUTER, P.; S. ARENZ; L.V. BOCK; M. GRAF; J.O. FRISTER; A. HEUER; L. PEIL; A.L. STAROSTA; I. WOHLGEMUTH; F. PESKE; Jiří NOVÁČEK; O. BERNINGHAUSEN; H. GRUBMULLER; T. TENSON; R. BECKMANN; M.V. RODNINA; A.C. VAIANA a D.N. WILSON. Structural Basis for Polyproline-Mediated Ribosome Stalling and Rescue by the Translation Elongation Factor EF-P. Molecular Cell. CAMBRIDGE: CELL PRESS, 2017, roč. 68, č. 3, s. 515-533. ISSN 1097-2765.

@article{39963,
   author = {Huter, P. and Arenz, S. and Bock, L.V. and Graf, M. and Frister, J.O. and Heuer, A. and Peil, L. and Starosta, A.L. and Wohlgemuth, I. and Peske, F. and Nováček, Jiří and Berninghausen, O. and Grubmuller, H. and Tenson, T. and Beckmann, R. and Rodnina, M.V. and Vaiana, A.C. and Wilson, D.N.},
   article_location = {CAMBRIDGE},
   article_number = {3},
   keywords = {PEPTIDE-BOND FORMATION; AMINOACYL-TRANSFER-RNA; MOLECULAR-DYNAMICS; PROTEIN-SYNTHESIS; 70S RIBOSOME; CRYO-EM; CRYSTAL-STRUCTURE; PROLINE RESIDUES; FACTOR EIF5A; MECHANISM},
   language = {eng},
   issn = {1097-2765},
   journal = {Molecular Cell},
   title = {Structural Basis for Polyproline-Mediated Ribosome Stalling and Rescue by the Translation Elongation Factor EF-P},
   url = {https://www.sciencedirect.com/science/article/pii/S109727651730789X?via%3Dihub},
   volume = {68},
   year = {2017}
}

TY  - JOUR
ID  - 39963
AU  - Huter, P. - Arenz, S. - Bock, L.V. - Graf, M. - Frister, J.O. - Heuer, A. - Peil, L. - Starosta, A.L. - Wohlgemuth, I. - Peske, F. - Nováček, Jiří - Berninghausen, O. - Grubmuller, H. - Tenson, T. - Beckmann, R. - Rodnina, M.V. - Vaiana, A.C. - Wilson, D.N.
PY  - 2017
TI  - Structural Basis for Polyproline-Mediated Ribosome Stalling and Rescue by the Translation Elongation Factor EF-P
JF  - Molecular Cell
VL  - 68
IS  - 3
SP  - 515
EP  - 515
PB  - CELL PRESS
SN  - 1097-2765
KW  - PEPTIDE-BOND FORMATION
KW  - AMINOACYL-TRANSFER-RNA
KW  - MOLECULAR-DYNAMICS
KW  - PROTEIN-SYNTHESIS
KW  - 70S RIBOSOME
KW  - CRYO-EM
KW  - CRYSTAL-STRUCTURE
KW  - PROLINE RESIDUES
KW  - FACTOR EIF5A
KW  - MECHANISM
UR  - https://www.sciencedirect.com/science/article/pii/S109727651730789X?via%3Dihub
N2  - 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 peptidyltRNA. 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.
ER  -

HUTER, P.; S. ARENZ; L.V. BOCK; M. GRAF; J.O. FRISTER; A. HEUER; L. PEIL; A.L. STAROSTA; I. WOHLGEMUTH; F. PESKE; Jiří NOVÁČEK; O. BERNINGHAUSEN; H. GRUBMULLER; T. TENSON; R. BECKMANN; M.V. RODNINA; A.C. VAIANA a D.N. WILSON. Structural Basis for Polyproline-Mediated Ribosome Stalling and Rescue by the Translation Elongation Factor EF-P. \textit{Molecular Cell}. CAMBRIDGE: CELL PRESS, 2017, roč.~68, č.~3, s.~515-533. ISSN~1097-2765.