title: Regulation of the Dbp5 ATPase cycle in mRNP remodeling at the nuclear pore: a lively new paradigm for DEAD-box proteins.
abstract: It is commonly assumed that all DEAD-box ATPases function via a shared mechanism, since this is the case for the few proteins characterized thus far. Hodge and colleagues (pp. 1052-1064) and Noble and colleagues (pp. 1065-1077) now describe a novel model for Dbp5's ATPase cycle in mRNA (messenger RNA)/protein complex (mRNP) remodeling during nuclear export. Notably, unlike other DEAD-box proteins, Dbp5 uses a conformational change distinct from ATP hydrolysis for its activity and requires an ADP release factor to reset its ATPase cycle.
authors.affiliation: Department of Biochemistry and Biophysics, University of California at San Francisco, USA.
authors.forename: Sarah
authors.initials: S
authors.lastname: Ledoux
authors.forename: Christine
authors.initials: C
authors.lastname: Guthrie
mesh_terms: D021581:Active Transport, Cell Nucleus; D000255:Adenosine Triphosphate / Q000378:metabolism; D002467:Cell Nucleus / Q000201:enzymology*; D053487:DEAD-box RNA Helicases / Q000737:chemistry / Q000378:metabolism*; D015971:Gene Expression Regulation, Enzymologic; D006801:Humans; D022022:Nuclear Pore / Q000378:metabolism*; D029543:Nucleocytoplasmic Transport Proteins / Q000737:chemistry / Q000378:metabolism*; D010833:Phytic Acid / Q000378:metabolism; D011485:Protein Binding; D012333:RNA, Messenger / Q000378:metabolism*; D012261:Ribonucleoproteins / Q000378:metabolism*
chemical_list: C474082:Gle1 protein, human; D029543:Nucleocytoplasmic Transport Proteins; D012333:RNA, Messenger; D012261:Ribonucleoproteins; C026452:messenger ribonucleoprotein; D010833:Phytic Acid; D000255:Adenosine Triphosphate; C121148:DDX19B protein, human; D053487:DEAD-box RNA Helicases