Protein displacement by DExH/D "RNA helicases" without duplex unwinding |
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Authors: | Fairman Margaret E Maroney Patricia A Wang Wen Bowers Heath A Gollnick Paul Nilsen Timothy W Jankowsky Eckhard |
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Affiliation: | Department of Biochemistry, School of Medicine, Case Western Reserve University, Cleveland, OH 44106, USA. |
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Abstract: | Members of the DExH/D superfamily of nucleic acid-activated nucleotide triphosphatases are essential for virtually all aspects of RNA metabolism, including pre-messenger RNA splicing, RNA interference, translation, and nucleocytoplasmic trafficking. Physiological substrates for these enzymes are thought to be regions of double-stranded RNA, because several DExH/D proteins catalyze strand separation in vitro. These "RNA helicases" can also disrupt RNA-protein interactions, but it is unclear whether this activity is coupled to duplex unwinding. Here we demonstrate that two unrelated DExH/D proteins catalyze protein displacement independently of duplex unwinding. Therefore, the essential functions of DExH/D proteins are not confined to RNA duplexes but can be exerted on a wide range of ribonucleoprotein substrates. |
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