Visualization of translation termination intermediates trapped
by the Apidaecin 137 peptide during RF3-mediated recycling of
RF1

J 2018

Visualization of translation termination intermediates trapped by the Apidaecin 137 peptide during RF3-mediated recycling of RF1

GRAF, M., P. HUTER, C. MARACCI, Miroslav PETEREK, M.V. RODNINA et. al.

Basic information

Original name

Visualization of translation termination intermediates trapped by the Apidaecin 137 peptide during RF3-mediated recycling of RF1

Authors

GRAF, M. (276 Germany), P. HUTER (276 Germany), C. MARACCI (276 Germany), Miroslav PETEREK (203 Czech Republic, guarantor, belonging to the institution), M.V. RODNINA (276 Germany) and D.N. WILSON (276 Germany)

Edition

Nature Communications, London, Nature Publishing Group, 2018, 2041-1723

Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10402 Inorganic and nuclear chemistry

Country of publisher

United Kingdom of Great Britain and Northern Ireland

Confidentiality degree

není předmětem státního či obchodního tajemství

Impact factor

Impact factor: 11.878

RIV identification code

RIV/00216224:14740/18:00106644

Organization unit

Central European Institute of Technology

DOI

http://dx.doi.org/10.1038/s41467-018-05465-1

UT WoS

000440652500005

Keywords in English

RELEASE FACTOR RF3; ELONGATION-FACTOR-G; STOP CODON RECOGNITION; ESCHERICHIA-COLI; CRYSTAL-STRUCTURE; ELECTRON CRYOMICROSCOPY; GTPASE ACTIVATION; GGQ MOTIF; CRYO-EM; EF-G

Abstract

V originále

During translation termination in bacteria, the release factors RF1 and RF2 are recycled from the ribosome by RF3. While high-resolution structures of the individual termination factors on the ribosome exist, direct structural insight into how RF3 mediates dissociation of the decoding RFs has been lacking. Here we have used the Apidaecin 137 peptide to trap RF1 together with RF3 on the ribosome and visualize an ensemble of termination intermediates using cryo-electron microscopy. Binding of RF3 to the ribosome induces small subunit (SSU) rotation and swivelling of the head, yielding intermediate states with shifted P-site tRNAs and RF1 conformations. RF3 does not directly eject RF1 from the ribosome, but rather induces full rotation of the SSU that indirectly dislodges RF1 from its binding site. SSU rotation is coupled to the accommodation of the GTPase domain of RF3 on the large subunit (LSU), thereby promoting GTP hydrolysis and dissociation of RF3 from the ribosome.

Links

LM2015043, research and development project

Name: Česká infrastruktura pro integrativní strukturní biologii (Acronym: CIISB)

Investor: Ministry of Education, Youth and Sports of the CR

Citovat

GRAF, M., P. HUTER, C. MARACCI, Miroslav PETEREK, M.V. RODNINA and D.N. WILSON. Visualization of translation termination intermediates trapped by the Apidaecin 137 peptide during RF3-mediated recycling of RF1. Nature Communications. London: Nature Publishing Group, 2018, vol. 9, AUG, p. 3053-3063. ISSN 2041-1723. Available from: https://dx.doi.org/10.1038/s41467-018-05465-1.

@article{1507057,
   author = {Graf, M. and Huter, P. and Maracci, C. and Peterek, Miroslav and Rodnina, M.V. and Wilson, D.N.},
   article_location = {London},
   article_number = {AUG},
   doi = {http://dx.doi.org/10.1038/s41467-018-05465-1},
   keywords = {RELEASE FACTOR RF3; ELONGATION-FACTOR-G; STOP CODON RECOGNITION; ESCHERICHIA-COLI; CRYSTAL-STRUCTURE; ELECTRON CRYOMICROSCOPY; GTPASE ACTIVATION; GGQ MOTIF; CRYO-EM; EF-G},
   language = {eng},
   issn = {2041-1723},
   journal = {Nature Communications},
   title = {Visualization of translation termination intermediates trapped by the Apidaecin 137 peptide during RF3-mediated recycling of RF1},
   volume = {9},
   year = {2018}
}

TY  - JOUR
ID  - 1507057
AU  - Graf, M. - Huter, P. - Maracci, C. - Peterek, Miroslav - Rodnina, M.V. - Wilson, D.N.
PY  - 2018
TI  - Visualization of translation termination intermediates trapped by the Apidaecin 137 peptide during RF3-mediated recycling of RF1
JF  - Nature Communications
VL  - 9
IS  - AUG
SP  - 3053
EP  - 3053
PB  - Nature Publishing Group
SN  - 20411723
KW  - RELEASE FACTOR RF3
KW  - ELONGATION-FACTOR-G
KW  - STOP CODON RECOGNITION
KW  - ESCHERICHIA-COLI
KW  - CRYSTAL-STRUCTURE
KW  - ELECTRON CRYOMICROSCOPY
KW  - GTPASE ACTIVATION
KW  - GGQ MOTIF
KW  - CRYO-EM
KW  - EF-G
N2  - During translation termination in bacteria, the release factors RF1 and RF2 are recycled from the ribosome by RF3. While high-resolution structures of the individual termination factors on the ribosome exist, direct structural insight into how RF3 mediates dissociation of the decoding RFs has been lacking. Here we have used the Apidaecin 137 peptide to trap RF1 together with RF3 on the ribosome and visualize an ensemble of termination intermediates using cryo-electron microscopy. Binding of RF3 to the ribosome induces small subunit (SSU) rotation and swivelling of the head, yielding intermediate states with shifted P-site tRNAs and RF1 conformations. RF3 does not directly eject RF1 from the ribosome, but rather induces full rotation of the SSU that indirectly dislodges RF1 from its binding site. SSU rotation is coupled to the accommodation of the GTPase domain of RF3 on the large subunit (LSU), thereby promoting GTP hydrolysis and dissociation of RF3 from the ribosome.
ER  -

GRAF, M., P. HUTER, C. MARACCI, Miroslav PETEREK, M.V. RODNINA and D.N. WILSON. Visualization of translation termination intermediates trapped by the Apidaecin 137 peptide during RF3-mediated recycling of RF1. \textit{Nature Communications}. London: Nature Publishing Group, 2018, vol.~9, AUG, p.~3053-3063. ISSN~2041-1723. Available from: https://dx.doi.org/10.1038/s41467-018-05465-1.

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