Translational regulation of Chk1 expression by eIF3a via interaction with the RNA-binding protein HuR.

In this study, we show that eIF3a up-regulates translation of Chk1 but not Chk2 mRNA by interacting with HuR, which binds directly to the 3'-UTR of Chk1 mRNA. The interaction between eIF3a and HuR occurs at the 10-amino-acid repeat domain of eIF3a and the RNA recognition motif domain of HuR. This interaction may effectively circularize Chk1 mRNA to form an end-to-end complex that has recently been suggested to accelerate mRNA translation. Together with previous findings, we conclude that eIF3a may regulate mRNA translation by directly binding to the 5'-UTR to suppress or interaction with RNA-binding proteins at 3'-UTRs to accelerate mRNA translation.
PMID: 32391557 [PubMed - as supplied by publisher]

Source: The Biochemical Journal - May 10, 2020 Category: Biochemistry Authors: Dong Z, Liu J, Zhang JT Tags: Biochem J Source Type: research