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: 13.783

Kód RIV

RIV/00216224:14740/21:00124438

Organizační jednotka

Středoevropský technologický institut

DOI

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

UT WoS

000615851800001

EID Scopus

2-s2.0-85100560703

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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