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.
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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
Original language English
Type of outcome Article in a journal
Field of Study 10608 Biochemistry and molecular biology
Country of publisher United States of America
Confidentiality degree is not subject to a state or trade secret
WWW 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
Tags CF CRYO, ne MU, rivok
Tags International impact, Reviewed
Changed by Changed by: Mgr. Pavla Foltynová, Ph.D., učo 106624. Changed: 23/3/2022 11:58.
Abstract
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.
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90043, large research infrastructuresName: CIISB
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