English   español  
Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/123738
logo share SHARE   Add this article to your Mendeley library MendeleyBASE
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL
Exportar a otros formatos:


Three-way RNA junctions with remote tertiary contacts: A recurrent and highly versatile fold

AuthorsPeña, Marcos de la ; Dufour, David; Gallego, José
Keywordsfolding, hammerhead ribozyme, loop, ribonucleoprotein, ribosome, riboswitch, RNase P, signal recognition particle, structure, tertiary interaction, three-way junction
Issue Date1-Nov-2009
AbstractThree-way junction RNAs adopt a recurrent Y shape when two of the helices form a coaxial stack and the third helix establishes one or more tertiary contacts several base pairs away from the junction. In this review, the structure, distribution, and functional relevance of these motifs are examined. Structurally, the folds exhibit conserved junction topologies, and the distal tertiary interactions play a crucial role in determining the final shape of the structures. The junctions and remote tertiary contacts behave as flexible hinge motifs that respond to changes in the other region, providing these folds with switching mechanisms that have been shown to be functionally useful in a variety of contexts. In addition, the juxtaposition of RNA domains at the junction and at the distal tertiary complexes enables the RNA helices to adopt unusual conformations that are frequently used by proteins, RNA molecules, and antibiotics as platforms for specific binding. As a consequence of these properties, Y-shaped junctions are widely distributed in all kingdoms of life, having been observed in small naked RNAs such as riboswitches and ribozymes or embedded in complex ribonucleoprotein systems like ribosomal RNAs, RNase P, or the signal recognition particle. In all cases, the folds were found to play an essential role for the functioning or assembly of the RNA or ribonucleoprotein systems that contain them.
Appears in Collections:(IBMCP) Artículos
Files in This Item:
File Description SizeFormat 
1949.pdf1,51 MBAdobe PDFThumbnail