Structural basis for+1 ribosomal frameshifting during
EF-G-catalyzed translocation

J 2021

Structural basis for+1 ribosomal frameshifting during EF-G-catalyzed translocation

DEMO, Gabriel; H.B. GAMPER; A.B. LOVELAND; I. MASUDA; C.E. CARBONE et. al.

Základní údaje

Originální název

Structural basis for+1 ribosomal frameshifting during EF-G-catalyzed translocation

Autoři

DEMO, Gabriel; H.B. GAMPER; A.B. LOVELAND; I. MASUDA; C.E. CARBONE; E. SVIDRITSKIY; Y.M. HOU a A.A. KOROSTELEV

Vydání

Nature Communications, London, Nature Publishing Group, 2021, 2041-1723

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10608 Biochemistry and molecular biology

Stát vydavatele

Německo

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 17.694

Kód RIV

RIV/00216224:14740/21:00119665

Organizační jednotka

Středoevropský technologický institut

DOI

https://doi.org/10.1038/s41467-021-24911-1

UT WoS

000684299000001

EID Scopus

2-s2.0-85111641609

Klíčová slova anglicky

RELEASE FACTOR-IITRANSFER-RNAANTICODON LOOPMESSENGER-RNAGENE-EXPRESSIONDECODING CENTERSUPPRESSORTRANSLATIONVISUALIZATIONMECHANISM

Štítky

rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 22. 2. 2022 15:32, Mgr. Pavla Foltynová, Ph.D.

Anotace

V originále

Frameshifting of mRNA during translation provides a strategy to expand the coding repertoire of cells and viruses. How and where in the elongation cycle +1-frameshifting occurs remains poorly understood. We describe seven similar to 3.5-angstrom-resolution cryo-EM structures of 70S ribosome complexes, allowing visualization of elongation and translocation by the GTPase elongation factor G (EF-G). Four structures with a + 1-frameshifting-prone mRNA reveal that frameshifting takes place during translocation of tRNA and mRNA. Prior to EF-G binding, the pre-translocation complex features an in-frame tRNA-mRNA pairing in the A site. In the partially translocated structure with EF-G center dot GDPCP, the tRNA shifts to the +1-frame near the P site, rendering the freed mRNA base to bulge between the P and E sites and to stack on the 16S rRNA nucleotide G926. The ribosome remains frameshifted in the nearly post-translocation state. Our findings demonstrate that the ribosome and EF-G cooperate to induce +1 frameshifting during tRNA-mRNA translocation.

Návaznosti

GJ20-16013Y, projekt VaV

Název: Simultánní transkripce a translace genu

Investor: Grantová agentura ČR, Simultaneous gene transcription and translation

Citovat

DEMO, Gabriel; H.B. GAMPER; A.B. LOVELAND; I. MASUDA; C.E. CARBONE; E. SVIDRITSKIY; Y.M. HOU a A.A. KOROSTELEV. Structural basis for+1 ribosomal frameshifting during EF-G-catalyzed translocation. Nature Communications. London: Nature Publishing Group, 2021, roč. 12, č. 1, s. 4644-4655. ISSN 2041-1723. Dostupné z: https://doi.org/10.1038/s41467-021-24911-1.

@article{1836382,
   author = {Demo, Gabriel and Gamper, H.B. and Loveland, A.B. and Masuda, I. and Carbone, C.E. and Svidritskiy, E. and Hou, Y.M. and Korostelev, A.A.},
   article_location = {London},
   article_number = {1},
   doi = {https://doi.org/10.1038/s41467-021-24911-1},
   keywords = {RELEASE FACTOR-IITRANSFER-RNAANTICODON LOOPMESSENGER-RNAGENE-EXPRESSIONDECODING CENTERSUPPRESSORTRANSLATIONVISUALIZATIONMECHANISM},
   language = {eng},
   issn = {2041-1723},
   journal = {Nature Communications},
   title = {Structural basis for+1 ribosomal frameshifting during EF-G-catalyzed translocation},
   url = {https://www.nature.com/articles/s41467-021-24911-1},
   volume = {12},
   year = {2021}
}

TY  - JOUR
ID  - 1836382
AU  - Demo, Gabriel - Gamper, H.B. - Loveland, A.B. - Masuda, I. - Carbone, C.E. - Svidritskiy, E. - Hou, Y.M. - Korostelev, A.A.
PY  - 2021
TI  - Structural basis for+1 ribosomal frameshifting during EF-G-catalyzed translocation
JF  - Nature Communications
VL  - 12
IS  - 1
SP  - 4644
EP  - 4644
PB  - Nature Publishing Group
SN  - 20411723
KW  - RELEASE FACTOR-IITRANSFER-RNAANTICODON LOOPMESSENGER-RNAGENE-EXPRESSIONDECODING CENTERSUPPRESSORTRANSLATIONVISUALIZATIONMECHANISM
UR  - https://www.nature.com/articles/s41467-021-24911-1
N2  - Frameshifting of mRNA during translation provides a strategy to expand the coding repertoire of cells and viruses. How and where in the elongation cycle +1-frameshifting occurs remains poorly understood. We describe seven similar to 3.5-angstrom-resolution cryo-EM structures of 70S ribosome complexes, allowing visualization of elongation and translocation by the GTPase elongation factor G (EF-G). Four structures with a + 1-frameshifting-prone mRNA reveal that frameshifting takes place during translocation of tRNA and mRNA. Prior to EF-G binding, the pre-translocation complex features an in-frame tRNA-mRNA pairing in the A site. In the partially translocated structure with EF-G center dot GDPCP, the tRNA shifts to the +1-frame near the P site, rendering the freed mRNA base to bulge between the P and E sites and to stack on the 16S rRNA nucleotide G926. The ribosome remains frameshifted in the nearly post-translocation state. Our findings demonstrate that the ribosome and EF-G cooperate to induce +1 frameshifting during tRNA-mRNA translocation.
ER  -

DEMO, Gabriel; H.B. GAMPER; A.B. LOVELAND; I. MASUDA; C.E. CARBONE; E. SVIDRITSKIY; Y.M. HOU a A.A. KOROSTELEV. Structural basis for+1 ribosomal frameshifting during EF-G-catalyzed translocation. \textit{Nature Communications}. London: Nature Publishing Group, 2021, roč.~12, č.~1, s.~4644-4655. ISSN~2041-1723. Dostupné z: https://doi.org/10.1038/s41467-021-24911-1.

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