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.

Basic information

Original name

Yeast translation elongation factor eEF3 promotes late stages of tRNA translocation

Authors

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

Edition

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

Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10608 Biochemistry and molecular biology

Country of publisher

United States of America

Confidentiality degree

není předmětem státního či obchodního tajemství

References:

URL

Impact factor

Impact factor: 14.012

RIV identification code

RIV/00216224:14740/21:00124438

Organization unit

Central European Institute of Technology

DOI

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

UT WoS

000615851800001

Keywords in English

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

Abstract

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.

Links

90043, large research infrastructures

Name: CIISB

Citovat

RANJAN, N., A.A. POCHOPIEN, C.C.C. WU, B. BECKERT, S. BLANCHET, R. GREEN, M.V. RODNINA and D.N. WILSON. Yeast translation elongation factor eEF3 promotes late stages of tRNA translocation. EMBO Journal. Hoboken (USA): WILEY-BLACKWELL, 2021, vol. 40, No 6, p. 1-20. ISSN 0261-4189. Available from: 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 and D.N. WILSON. Yeast translation elongation factor eEF3 promotes late stages of tRNA translocation. \textit{EMBO Journal}. Hoboken (USA): WILEY-BLACKWELL, 2021, vol.~40, No~6, p.~1-20. ISSN~0261-4189. Available from: https://dx.doi.org/10.15252/embj.2020106449.

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