title: RNA unwinding assay for DExD/H-box RNA helicases.
abstract: The evolutionarily conserved DExD/H-box proteins are essential for all RNA-related biological processes. They are thought to modulate the structure and function of specific RNAs and/or ribonucleoprotein particles by using their intrinsic RNA-dependent ATPase activities to achieve the desired conformational changes. A number of DExD/H-box proteins have been shown to unwind short RNA duplexes in vitro, a hallmark of the so-called RNA helicases or unwindases. However, some are unable to do so, perhaps because of requirements for cofactors. Here, we present a "solid-state" method that may allow investigators to overcome such problems.
authors.affiliation: Department of Molecular Genetics, The Ohio State University, Columbus, OH, USA.
authors.forename: Stephanie S
authors.initials: SS
authors.lastname: Tseng-Rogenski
authors.forename: Tien-Hsien
authors.initials: TH
authors.lastname: Chang
mesh_terms: D001483:Base Sequence; D053487:DEAD-box RNA Helicases; D006801:Humans; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D029543:Nucleocytoplasmic Transport Proteins / Q000235:genetics* / Q000378:metabolism; D011233:Precipitin Tests; D012313:RNA / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D020365:RNA Helicases / Q000235:genetics* / Q000378:metabolism; D012326:RNA Splicing
chemical_list: D029543:Nucleocytoplasmic Transport Proteins; D012313:RNA; C121148:DDX19B protein, human; D053487:DEAD-box RNA Helicases; D020365:RNA Helicases