RNA chaperones, RNA annealers and RNA helicases

RNA Biol. 2007 Nov;4(3):118-30. doi: 10.4161/rna.4.3.5445.


RNA molecules face difficulties when folding into their native structures. In the cell, proteins can assist RNAs in reaching their functionally active states by binding and stabilizing a specific structure or, in a quite opposite way, by interacting in a non-specific manner. These proteins can either facilitate RNA-RNA interactions in a reaction termed RNA annealing, or they can resolve non-functional inhibitory structures. The latter is defined as "RNA chaperone activity" and is the main topic of this review. Here we define RNA chaperone activity in a stringent way and we review those proteins for which RNA chaperone activity has been clearly demonstrated. These proteins belong to quite diverse families such as hnRNPs, histone-like proteins, ribosomal proteins, cold shock domain proteins and viral nucleocapsid proteins. DExD/H-box containing RNA helicases are discussed as a special family of enzymes that restructure RNA or RNPs in an ATP-dependent manner. We further address the different mechanisms RNA chaperones might use to promote folding including the recently proposed theory of protein disorder as a key element in triggering RNA-protein interactions. Finally, we present a new website for proteins with RNA chaperone activity which compiles all the information on these proteins with the perspective to promote the understanding of their activity.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Humans
  • Molecular Chaperones / chemistry*
  • Molecular Chaperones / classification
  • Molecular Chaperones / physiology*
  • Nucleic Acid Conformation
  • RNA / chemistry*
  • RNA / metabolism*
  • RNA / physiology
  • RNA Helicases / chemistry*
  • RNA Helicases / classification
  • RNA Helicases / physiology*


  • Molecular Chaperones
  • RNA
  • RNA Helicases