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


Tran| Zhou| Corbett| Wente EJ| Y| AH| SRElizabeth J| Yingna| Anita H| Susan R . Molecular cell. 2007 12 14; 28(5). 850-9


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.

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