Regulation of RNA helicase activity: principles and examples
- PMID: 33583161
- DOI: 10.1515/hsz-2020-0362
Regulation of RNA helicase activity: principles and examples
Abstract
RNA helicases are a ubiquitous class of enzymes involved in virtually all processes of RNA metabolism, from transcription, mRNA splicing and export, mRNA translation and RNA transport to RNA degradation. Although ATP-dependent unwinding of RNA duplexes is their hallmark reaction, not all helicases catalyze unwinding in vitro, and some in vivo functions do not depend on duplex unwinding. RNA helicases are divided into different families that share a common helicase core with a set of helicase signature motives. The core provides the active site for ATP hydrolysis, a binding site for non-sequence-specific interaction with RNA, and in many cases a basal unwinding activity. Its activity is often regulated by flanking domains, by interaction partners, or by self-association. In this review, we summarize the regulatory mechanisms that modulate the activities of the helicase core. Case studies on selected helicases with functions in translation, splicing, and RNA sensing illustrate the various modes and layers of regulation in time and space that harness the helicase core for a wide spectrum of cellular tasks.
Keywords: RNA binding; RNA unwinding; helicase; mechanism; regulation.
© 2021 Walter de Gruyter GmbH, Berlin/Boston.
References
-
- Absmeier, E., Becke, C., Wollenhaupt, J., Santos, K.F., and Wahl, M.C. (2017). Interplay of cis- and trans-regulatory mechanisms in the spliceosomal RNA helicase Brr2. Cell Cycle 16: 100–112. https://doi.org/10.1080/15384101.2016.1255384.
-
- Absmeier, E., Rosenberger, L., Apelt, L., Becke, C., Santos, K.F., Stelzl, U., and Wahl, M.C. (2015a). A noncanonical PWI domain in the N-terminal helicase-associated region of the spliceosomal Brr2 protein. Acta Crystallogr. D Biol. Crystallogr. 71: 762–771. https://doi.org/10.1107/S1399004715001005.
-
- Absmeier, E., Santos, K.F., and Wahl, M.C. (2016). Functions and regulation of the Brr2 RNA helicase during splicing. Cell Cycle 15: 3362–3377. https://doi.org/10.1080/15384101.2016.1249549.
-
- Absmeier, E., Santos, K.F., and Wahl, M.C. (2020). Molecular mechanism underlying inhibition of intrinsic ATPase activity in a Ski2-like RNA helicase. Structure 28: 236–243. https://doi.org/10.1016/j.str.2019.11.014.
-
- Absmeier, E., Wollenhaupt, J., Mozaffari-Jovin, S., Becke, C., Lee, C.T., Preussner, M., Heyd, F., Urlaub, H., Luhrmann, R., Santos, K.F., et al.. (2015b). The large N-terminal region of the Brr2 RNA helicase guides productive spliceosome activation. Genes Dev. 29: 2576–2587. https://doi.org/10.1101/gad.271528.115.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources