
pmid: 11141562
All aspects of cellular RNA metabolism and the replication of many viruses require DExH/D proteins that manipulate RNA in a manner that requires nucleoside triphosphates. Although DExH/D proteins have been shown to unwind purified RNA duplexes, most RNA molecules in the cellular environment are complexed with proteins. It has therefore been speculated that DExH/D proteins may also affect RNA-protein interactions. We demonstrate that the DExH protein NPH-II from vaccinia virus can displace the protein U1A from RNA in an active adenosine triphosphate–dependent fashion. NPH-II increases the rate of U1A dissociation by more than three orders of magnitude while retaining helicase processivity. This indicates that DExH/D proteins can effectively catalyze protein displacement from RNA and thereby participate in the structural reorganization of ribonucleoprotein assemblies.
Models, Molecular, Binding Sites, Base Sequence, Protein Conformation, Molecular Sequence Data, RNA-Binding Proteins, Nucleoside-Triphosphatase, Acid Anhydride Hydrolases, Ribonucleoprotein, U1 Small Nuclear, Kinetics, Adenosine Triphosphate, Nucleic Acid Conformation, RNA, 3' Untranslated Regions, RNA Helicases, Protein Binding
Models, Molecular, Binding Sites, Base Sequence, Protein Conformation, Molecular Sequence Data, RNA-Binding Proteins, Nucleoside-Triphosphatase, Acid Anhydride Hydrolases, Ribonucleoprotein, U1 Small Nuclear, Kinetics, Adenosine Triphosphate, Nucleic Acid Conformation, RNA, 3' Untranslated Regions, RNA Helicases, Protein Binding
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