The DEAD-box protein Dbp5 controls mRNA export by triggering specific RNA:protein remodeling events.

Tran EJ, Zhou Y, Corbett AH, Wente SR
Mol Cell. 2007 28 (5): 850-9

PMID: 18082609 · DOI:10.1016/j.molcel.2007.09.019

Messenger RNA (mRNA) export involves the unidirectional passage of ribonucleoprotein particles (RNPs) through nuclear pore complexes (NPCs), presumably driven by the ATP-dependent activity of the DEAD-box protein Dbp5. Here we report that Dbp5 functions as an RNP remodeling protein to displace the RNA-binding protein Nab2 from RNA. Strikingly, the ADP-bound form of Dbp5 and not ATP hydrolysis is required for RNP remodeling. In vivo studies with nab2 and dbp5 mutants show that a Nab2-bound mRNP is a physiological Dbp5 target. We propose that Dbp5 functions as a nucleotide-dependent switch to control mRNA export efficiency and release the mRNP from the NPC.

MeSH Terms (16)

Active Transport, Cell Nucleus Binding Sites Cross-Linking Reagents DEAD-box RNA Helicases Fluorescent Antibody Technique In Situ Hybridization Nuclear Pore Nucleocytoplasmic Transport Proteins Phytic Acid Ribonucleoproteins RNA, Messenger RNA-Binding Proteins RNA Helicases Saccharomyces cerevisiae Saccharomyces cerevisiae Proteins Ultraviolet Rays

Connections (1)

This publication is referenced by other Labnodes entities: