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Protein Displacement by DExH/D "RNA Helicases" Without Duplex Unwinding
Margaret E. Fairman,1*Patricia A. Maroney,2*Wen Wang,1Heath A. Bowers,1Paul Gollnick,3Timothy W. Nilsen,2Eckhard Jankowsky1,2
Members of the DExH/D superfamily of nucleic acidactivatednucleotide triphosphatases are essential for virtually all aspectsof RNA metabolism, including premessenger RNA splicing,RNA interference, translation, and nucleocytoplasmic trafficking.Physiological substrates for these enzymes are thought to beregions of double-stranded RNA, because several DExH/D proteinscatalyze strand separation in vitro. These "RNA helicases" canalso disrupt RNA-protein interactions, but it is unclear whetherthis activity is coupled to duplex unwinding. Here we demonstratethat two unrelated DExH/D proteins catalyze protein displacementindependently of duplex unwinding. Therefore, the essentialfunctions of DExH/D proteins are not confined to RNA duplexesbut can be exerted on a wide range of ribonucleoprotein substrates.
1 Department of Biochemistry, School of Medicine, Case Western Reserve University, Cleveland, OH 44106, USA. 2 The Center for RNA Molecular Biology, School of Medicine, Case Western Reserve University, Cleveland, OH 44106, USA. 3 Department of Biological Sciences, State University of New York at Buffalo, Buffalo, NY 14260, USA.
* These authors contributed equally to this work.
To whom correspondence should be addressed. E-mail: exj13{at}po.cwru.edu (E.J.); twn{at}po.cwru.edu (T.W.N.)
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Patrick Linder (30 April 2004) Science304 (5671), 694.
[DOI: 10.1126/science.1097850] |Summary »|Full Text »|PDF »
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