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Biophysics of RNA Folding pp 205–230Cite as

The Roles of Chaperones in RNA Folding

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Part of the book series: Biophysics for the Life Sciences ((BIOPHYS,volume 3))

Abstract

Because of its limited structural diversity, RNA has a strong tendency to misfold, and the stability of local structure often causes misfolded conformations to be long-lived on the biological time scale. The effects of RNA misfolding are dealt with in vivo by chaperones. Some of these chaperones function by interacting strongly with unstructured RNA and do not depend on a source of energy for their activities, while a second group couples unfavorable RNA rearrangements to the favorable hydrolysis of ATP. This latter group is made up of RNA helicase ­proteins, with the largest group being the DEAD-box proteins. While some ATP-dependent RNA chaperone proteins are evolved to function on specific substrate RNAs or RNA–protein complexes, others function as general chaperones by interacting ­functionally with a broad range of RNA structures. Experimental studies using diverse approaches have begun to ­elucidate the mechanisms of RNA ­chaperones in rearranging RNAs. In this chapter, we describe the mechanistic ­features that are thought to underlie chaperone activity, with a focus on group I and group II introns as experimental systems.

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Acknowledgments

Research in the Russell’s lab is supported by grants from the NIH (GM070456) and the Welch Foundation (F-1563).

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  1. Department of Chemistry and Biochemistry, Institute for Cellular and Molecular Biology, University of Texas at Austin, 2500 Speedway, Austin, TX, 78712, USA

    Pilar Tijerina & Rick Russell

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  1. Pilar Tijerina
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Correspondence to Rick Russell .

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    Rick Russell

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Tijerina, P., Russell, R. (2013). The Roles of Chaperones in RNA Folding. In: Russell, R. (eds) Biophysics of RNA Folding. Biophysics for the Life Sciences, vol 3. Springer, New York, NY. https://doi.org/10.1007/978-1-4614-4954-6_11

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