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RNA chaperones, RNA annealers and RNA helicases Rajkowitsch L; Chen D; Stampfl S; Semrad K; Waldsich C; Mayer O; Jantsch MF; Konrat R; Blasi U; Schroeder RRNA Biol 2007[Nov]; 4 (3): 118-30RNA 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.|Animals[MESH]|Humans[MESH]|Molecular Chaperones/*chemistry/classification/*physiology[MESH]|Nucleic Acid Conformation[MESH]|RNA Helicases/*chemistry/classification/*physiology[MESH]|RNA/*chemistry/*metabolism/physiology[MESH] |
