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The RNA Chaperone Activity Website

MFPL website
Uni Wien

What is RNA Chaperone Activity (RCA) ?

Proteins can assist RNAs reach their native state by binding and stabilizing a specific structure or, in a quite opposite way, by interacting with broad specificity with RNAs resolving non-native structural intermediates, which slow down folding. The latter is defined as "RNA chaperone activity" and proteins with this activity are presented on this website. The term RNA chaperone has been widely used and encompasses many different activities. Here we discuss the diversity of proteins, which help RNAs not only to fold but also to recognize and bind targets or to assemble into large RNA protein particles. These proteins are members of diverse families like the hnRNP proteins, histone-like proteins, ribosomal proteins, the cold shock domain or OB fold proteins, and viral capsids to mention just the most frequent. We further discuss the different mechanisms that these proteins might use to promote folding including the recently proposed theory of protein disorder as a key element in triggering RNA-protein interactions.

Many different assays have been used to monitor RNA chaperone activity. See the link to the different assays. These assays help to define different classes. Some proteins, for example the E. coli protein Hfq (host factor for phage Q replication), have RNA annealing activity, but no RNA unfolding or RNA strand displacement actitivity. In contrast, ribosomal protein S1 has RNA strand displacement but no RNA annealing activity. The E. coli histone-like protein StpA has both, RNA annealing and strand displacement activities.

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