RNA chaperones, RNA annealers and RNA helicases. Export

@article{rajkowitsch07, abstract = {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.}, address = {Max F. Perutz Laboratories, University of Vienna, Vienna, Austria.}, author = {Rajkowitsch, L. and Chen, D. and Stampfl, S. and Semrad, K. and Waldsich, C. and Mayer, O. and Jantsch, M. F. and Konrat, R. and Bl\"{a}si, U. and Schroeder, R.}, citeulike-article-id = {2731257}, citeulike-linkout-0 = {http://view.ncbi.nlm.nih.gov/pubmed/18347437}, citeulike-linkout-1 = {http://www.hubmed.org/display.cgi?uids=18347437}, issn = {1555-8584}, journal = {RNA biology}, keywords = {annealing, chaperone, folding, helicase, review, rna}, month = {November}, number = {3}, pages = {118--130}, posted-at = {2008-05-29 17:13:19}, priority = {0}, title = {RNA chaperones, RNA annealers and RNA helicases.}, url = {http://view.ncbi.nlm.nih.gov/pubmed/18347437}, volume = {4}, year = {2007} }

TY - JOUR ID - rajkowitsch07 L3 - citeulike-article-id:2731257 N2 - 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. IS - 3 JF - RNA biology SN - 1555-8584 AD - Max F. Perutz Laboratories, University of Vienna, Vienna, Austria. EP - 130 TI - RNA chaperones, RNA annealers and RNA helicases. VL - 4 SP - 118 KW - annealing KW - chaperone KW - folding KW - helicase KW - review KW - rna AU - Rajkowitsch, L AU - Chen, D AU - Stampfl, S AU - Semrad, K AU - Waldsich, C AU - Mayer, O AU - Jantsch, MF AU - Konrat, R AU - Bläsi, U AU - Schroeder, R PY - 2007/11// UR - http://view.ncbi.nlm.nih.gov/pubmed/18347437 ER -