Published in

American Association for the Advancement of Science, Science, 6508(369), p. 1220-1227, 2020

DOI: 10.1126/science.aba4904

Links

Tools

Export citation

Search in Google Scholar

Structure of a human 48 S translational initiation complex

This paper was not found in any repository, but could be made available legally by the author.
This paper was not found in any repository, but could be made available legally by the author.

Full text: Unavailable

Green circle
Preprint: archiving allowed
Green circle
Postprint: archiving allowed
Red circle
Published version: archiving forbidden
Data provided by SHERPA/RoMEO

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