title: Key points to consider when studying RNA remodeling by proteins.
abstract: Cellular RNAs depend on proteins for efficient folding to specific functional structures and for transitions between functional structures. This dependence arises from intrinsic properties of RNA structure. Specifically, RNAs possess stable local structure, largely in the form of helices, and they have abundant opportunities to form alternative helices and tertiary contacts and therefore to populate alternative structures. Proteins with RNA chaperone activity, either ATP-dependent or ATP-independent, can promote structural transitions by interacting with single-stranded RNA (ssRNA) to compete away partner interactions and then release ssRNA so that it can form new interactions. In this chapter we review the basic properties of RNA and the proteins that function as chaperones and remodelers. We then use these properties as a foundation to explore key points for the design and interpretation of experiments that probe RNA rearrangements and their acceleration by proteins.
authors.affiliation: Department of Molecular Biosciences, Institute for Cellular and Molecular Biology, University of Texas at Austin, 105 E, 24th St. Stop A5300, Austin, TX, 78712, USA.
authors.forename: W Luke
authors.initials: WL
authors.lastname: Ward
authors.forename: Rick
authors.initials: R
authors.lastname: Russell
mesh_terms: D008954:Models, Biological; D009690:Nucleic Acid Conformation; D011506:Proteins / Q000378:metabolism*; D012313:RNA / Q000737:chemistry*; D059370:RNA Folding; D020365:RNA Helicases / Q000378:metabolism
chemical_list: D011506:Proteins; D012313:RNA; D020365:RNA Helicases