Yeast translation elongation factor eEF3 promotes late stages
of tRNA translocation

J 2021

Yeast translation elongation factor eEF3 promotes late stages of tRNA translocation

RANJAN, N., A.A. POCHOPIEN, C.C.C. WU, B. BECKERT, S. BLANCHET et. al.

Základní údaje

Originální název

Yeast translation elongation factor eEF3 promotes late stages of tRNA translocation

Autoři

RANJAN, N., A.A. POCHOPIEN, C.C.C. WU, B. BECKERT, S. BLANCHET, R. GREEN, M.V. RODNINA a D.N. WILSON

Vydání

EMBO Journal, Hoboken (USA), WILEY-BLACKWELL, 2021, 0261-4189

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10608 Biochemistry and molecular biology

Stát vydavatele

Spojené státy

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 14.012

Kód RIV

RIV/00216224:14740/21:00124438

Organizační jednotka

Středoevropský technologický institut

DOI

http://dx.doi.org/10.15252/embj.2020106449

UT WoS

000615851800001

Klíčová slova anglicky

ABC ATPase; cryo‐ EM; eEF3; E‐ site tRNA; L1 stalk

Štítky

CF CRYO, ne MU, rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 23. 3. 2022 11:58, Mgr. Pavla Foltynová, Ph.D.

Anotace

V originále

In addition to the conserved translation elongation factors eEF1A and eEF2, fungi require a third essential elongation factor, eEF3. While eEF3 has been implicated in tRNA binding and release at the ribosomal A and E sites, its exact mechanism of action is unclear. Here, we show that eEF3 acts at the mRNA-tRNA translocation step by promoting the dissociation of the tRNA from the E site, but independent of aminoacyl-tRNA recruitment to the A site. Depletion of eEF3 in vivo leads to a general slowdown in translation elongation due to accumulation of ribosomes with an occupied A site. Cryo-EM analysis of native eEF3-ribosome complexes shows that eEF3 facilitates late steps of translocation by favoring non-rotated ribosomal states, as well as by opening the L1 stalk to release the E-site tRNA. Additionally, our analysis provides structural insights into novel translation elongation states, enabling presentation of a revised yeast translation elongation cycle.

Návaznosti

90043, velká výzkumná infrastruktura

Název: CIISB

Citovat

RANJAN, N., A.A. POCHOPIEN, C.C.C. WU, B. BECKERT, S. BLANCHET, R. GREEN, M.V. RODNINA a D.N. WILSON. Yeast translation elongation factor eEF3 promotes late stages of tRNA translocation. EMBO Journal. Hoboken (USA): WILEY-BLACKWELL, 2021, roč. 40, č. 6, s. 1-20. ISSN 0261-4189. Dostupné z: https://dx.doi.org/10.15252/embj.2020106449.

@article{1842605,
   author = {Ranjan, N. and Pochopien, A.A. and Wu, C.C.C. and Beckert, B. and Blanchet, S. and Green, R. and Rodnina, M.V. and Wilson, D.N.},
   article_location = {Hoboken (USA)},
   article_number = {6},
   doi = {http://dx.doi.org/10.15252/embj.2020106449},
   keywords = {ABC ATPase; cryo‐ EM; eEF3; E‐ site tRNA; L1 stalk},
   language = {eng},
   issn = {0261-4189},
   journal = {EMBO Journal},
   title = {Yeast translation elongation factor eEF3 promotes late stages of tRNA translocation},
   url = {https://www.embopress.org/doi/full/10.15252/embj.2020106449},
   volume = {40},
   year = {2021}
}

TY  - JOUR
ID  - 1842605
AU  - Ranjan, N. - Pochopien, A.A. - Wu, C.C.C. - Beckert, B. - Blanchet, S. - Green, R. - Rodnina, M.V. - Wilson, D.N.
PY  - 2021
TI  - Yeast translation elongation factor eEF3 promotes late stages of tRNA translocation
JF  - EMBO Journal
VL  - 40
IS  - 6
SP  - 1-20
EP  - 1-20
PB  - WILEY-BLACKWELL
SN  - 02614189
KW  - ABC ATPase
KW  - cryo‐ EM
KW  - eEF3
KW  - E‐ site tRNA
KW  - L1 stalk
UR  - https://www.embopress.org/doi/full/10.15252/embj.2020106449
N2  - In addition to the conserved translation elongation factors eEF1A and eEF2, fungi require a third essential elongation factor, eEF3. While eEF3 has been implicated in tRNA binding and release at the ribosomal A and E sites, its exact mechanism of action is unclear. Here, we show that eEF3 acts at the mRNA-tRNA translocation step by promoting the dissociation of the tRNA from the E site, but independent of aminoacyl-tRNA recruitment to the A site. Depletion of eEF3 in vivo leads to a general slowdown in translation elongation due to accumulation of ribosomes with an occupied A site. Cryo-EM analysis of native eEF3-ribosome complexes shows that eEF3 facilitates late steps of translocation by favoring non-rotated ribosomal states, as well as by opening the L1 stalk to release the E-site tRNA. Additionally, our analysis provides structural insights into novel translation elongation states, enabling presentation of a revised yeast translation elongation cycle.
ER  -

RANJAN, N., A.A. POCHOPIEN, C.C.C. WU, B. BECKERT, S. BLANCHET, R. GREEN, M.V. RODNINA a D.N. WILSON. Yeast translation elongation factor eEF3 promotes late stages of tRNA translocation. \textit{EMBO Journal}. Hoboken (USA): WILEY-BLACKWELL, 2021, roč.~40, č.~6, s.~1-20. ISSN~0261-4189. Dostupné z: https://dx.doi.org/10.15252/embj.2020106449.

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