Structure of a human 48 S translational initiation complex-Reference-Cited by-同舟云学术

Structure of a human 48 S translational initiation complex

Published:2020-09-04 Issue:6508 Volume:369 Page:1220-1227
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Brito Querido Jailson¹^ORCID,Sokabe Masaaki²^ORCID,Kraatz Sebastian¹^ORCID,Gordiyenko Yuliya¹^ORCID,Skehel J. Mark¹^ORCID,Fraser Christopher S.²^ORCID,Ramakrishnan V.¹^ORCID

Affiliation:

1. MRC Laboratory of Molecular Biology, Cambridge, UK.

2. Department of Molecular and Cellular Biology, College of Biological Sciences, University of California, Davis, CA, USA.

Abstract

Finding the start Eukaryotic translation involves many players in a dynamic and well-orchestrated process. A 43 S preinitiation complex (PIC) comprises the 40 S ribosomal subunit; initiation factors, including the eIF3 complex, which is known to play a key role; and the transfer RNA used for translation initiation. The PIC is recruited to the cap-binding complex eIF4F at the 5′ end of messenger RNA (mRNA) to form a 48 S complex that scans along the mRNA for a start codon. Brito Querido et al. determined the structure of a reconstituted human 48 S complex using cryo–electron microscopy. They found that eIF4F binds to eIF3 near the exit site of the ribosome. This positioning suggests that downstream mRNA is likely pulled through the 40 S subunit to find the start codon. Science , this issue p. 1220

Funder

National Institutes of Health

Federation of European Biochemical Societies

Louis-Jeantet Foundation

UK Medical Research Council

Wellcome Trust Senior Investigator Award

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

Reference73 articles.

1. New initiation factor activity required for globin mRNA translation.