Major structural rearrangements of the canonical eukaryotic translation initiation complex. (December 2018)

• Record Type: Journal Article
• Authors: Guca, Ewelina; Hashem, Yaser
• Is Part Of: Current opinion in structural biology. Volume 53(2018)
• Page Start: 151
• Page End: 158
• Publication Date: 2018-12
• Subjects: Molecular biology -- Periodicals; 570
• DOI: 10.1016/j.sbi.2018.08.006
• Languages: English
• ISSNs: 0959-440X

Abstract

Highlights: During translation initiation 48S complexes undergo deep structural rearrangements. mRNA recruitment models involve either 'threading' or 'slotting' into the channel. eIF3b-i-g module switches between two sites before, during and after scanning. The TC switches between the PIN and POUT conformations during scanning. Abstract : Translation initiation in eukaryotes is a complex multistep process that requires the interplay of over a dozen protein factors together with the small ribosomal subunit (SSU) and the mRNA. During all these steps, the SSU serves as a platform for attachment, displacement and release of different molecules. In recent years, the great number of high-resolution X-ray and cryo-EM structures provided unprecedented insights into the molecular mechanism of this important process in eukaryotes. More specifically, cryo-EM became a leading technique in uncovering the structural details of this process due to exceptional advances in resolution and in image processing. Here, we briefly review cap-dependent eukaryotic translation initiation with an emphasis on its major conformational changes at several key steps during the process, unraveled thanks to the recent advances in the structural biology field.