EIF4B stimulates eIF4A ATPase and unwinding activities by direct interaction through its 7-repeats region.

ABSTRACT: Eukaryotic translation initiation starts with binding of the eIF4F complex to the 5'-m⁷G cap of the mRNA. Recruitment of the 43S pre-initiation complex (PIC), formed by the 40S ribosomal subunit and other translation initiation factors, leads to formation of the 48S PIC that then scans the 5'-untranslated region (5'-UTR) toward the start codon. The eIF4F complex consists of eIF4E, the cap binding protein, eIF4A, a DEAD-box RNA helicase that is believed to unwind secondary structures in the 5'-UTR during scanning, and eIF4G, a scaffold protein that binds to both eIF4E and eIF4A. The ATPase and helicase activities of eIF4A are jointly stimulated by eIF4G and the translation initiation factor eIF4B. Yeast eIF4B mediates recruitment of the 43S PIC to the cap-bound eIF4F complex by i

SUBMITTER: Andreou AZ 

PROVIDER: S-EPMC5270515 | biostudies-literature | 2017 Jan

REPOSITORIES: biostudies-literature