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.

Základní údaje

Originální název

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

Autoři

GRAF, M. (276 Německo), P. HUTER (276 Německo), C. MARACCI (276 Německo), Miroslav PETEREK (203 Česká republika, garant, domácí), M.V. RODNINA (276 Německo) a D.N. WILSON (276 Německo)

Vydání

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

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10402 Inorganic and nuclear chemistry

Stát vydavatele

Velká Británie a Severní Irsko

Utajení

není předmětem státního či obchodního tajemství

Impakt faktor

Impact factor: 11.878

Kód RIV

RIV/00216224:14740/18:00106644

Organizační jednotka

Středoevropský technologický institut

DOI

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

UT WoS

000440652500005

Klíčová slova anglicky

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

Štítky

CF CRYO, rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 18. 3. 2019 15:17, Mgr. Pavla Foltynová, Ph.D.

Anotace

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.

Návaznosti

LM2015043, projekt VaV

Název: Česká infrastruktura pro integrativní strukturní biologii (Akronym: CIISB)

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Czech Infrastructure for Integrative Structural Biology

Citovat

GRAF, M., P. HUTER, C. MARACCI, Miroslav PETEREK, M.V. RODNINA a 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, roč. 9, AUG, s. 3053-3063. ISSN 2041-1723. Dostupné z: 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 a 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, roč.~9, AUG, s.~3053-3063. ISSN~2041-1723. Dostupné z: https://dx.doi.org/10.1038/s41467-018-05465-1.

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