The DEAD-box RNA helicase Dbp5 is a key protein that couples multiple steps in gene expression

Abstract

Cell viability largely depends on the surveillance of mRNA export and translation. Upon pre-mRNA processing and nuclear quality control, mature mRNAs are exported into the cytoplasm via Mex67-Mtr2 attachment. At the cytoplasmic site of the nuclear pore complex, the export receptor is displaced by the action of the DEAD-box RNA helicase Dbp5. Subsequent quality control of the open reading frame requires translation. Our studies suggest an involvement of Dbp5 in cytoplasmic no-go-and non-stop decay. Most importantly, we have also identified a key function for Dbp5 in translation termination, which identifies this helicase as a master regulator of mRNA expression.

RNA biogenesis and RNA metabolism factors as R-loop suppressors: a hidden role in genome integrity

“…Some have been shown to unwind DNA–RNA hybrids in vitro ( Table 2 ), such as the Ski2 helicase MTR4 of the TRAMP complex, which cooperates with the exosome and SETX in the process of Ig class switch recombination ( Lim et al 2017 ; Puno and Lima 2018 ). Also, DDX19 relocates from the nuclear pore to the nucleoplasm, where it may counteract R-loops formed at DNA damage sites ( Hodroj et al 2017 ; Querl and Krebber 2023 ). However, more helicases have been reported to counteract R-loops in vivo despite the lack of evidence for DNA–RNA hybrid-unwinding activity in vitro.…”