The DOI matches its Crossref record; 64 of the 64 references it cites were found in a registry or an index.
Translocation and Unwinding Mechanisms of RNA and DNA Helicases
Abstract
Helicases and remodeling enzymes are ATP-dependent motor proteins that play a critical role in every aspect of RNA and DNA metabolism. Most RNA-remodeling enzymes are members of helicase superfamily 2 (SF2), which includes many DNA helicase enzymes that display similar structural and mechanistic features. Although SF2 enzymes are typically called helicases, many of them display other types of functions, including single-strand translocation, strand annealing, and protein displacement. There are two mechanisms by which RNA helicase enzymes unwind RNA: The nonprocessive DEAD group catalyzes local unwinding of short duplexes adjacent to their binding sites. Members of the processive DExH group often translocate along single-stranded RNA and displace paired strands (or proteins) in their path. In the latter case, unwinding is likely to occur by an active mechanism that involves Brownian motor function and stepwise translocation along RNA. Through structural and single-molecule investigations, researchers are developing coherent models to explain the functions and dynamic motions of helicase enzymes.
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Cites
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Structure and Mechanism of Helicases and Nucleic Acid Translocases
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Mechanical Devices of the Spliceosome: Motors, Clocks, Springs, and Things
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The DEAD-box protein family of RNA helicases
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DEAD-box proteins: the driving forces behind RNA metabolism
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Helicase structure and mechanism
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Dead-box proteins: a family affair—active and passive players in RNP-remodeling
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Cited by
The Spliceosome: Design Principles of a Dynamic RNP Machine
Wahl, M. C., Will, C. L., & Lührmann, R. (2009) · Cell · doi:10.1016/j.cell.2009.02.009 · Cited by 2,665
RNA Splicing by the Spliceosome
Wilkinson, M. E., Charenton, C., & Nagai, K. (2020) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-091719-064225 · Cited by 718
DNA topoisomerases: harnessing and constraining energy to govern chromosome topology
Schoeffler, A. J., & Berger, J. M. (2008) · Quarterly Reviews of Biophysics · doi:10.1017/s003358350800468x · Cited by 490
Mendoza, O., Bourdoncle, A., Boulé, J.-B., Brosh, R. M., & Mergny, J.-L. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw079 · Cited by 458
The flavivirus NS2B–NS3 protease–helicase as a target for antiviral drug development
Luo, D., Vasudevan, S. G., & Lescar, J. (2015) · Antiviral Research · doi:10.1016/j.antiviral.2015.03.014 · Cited by 288
Metadata
- Authors
- Pyle, A. M.
- Venue
- Annual Review of Biophysics
- Publisher
- Annual Reviews
- Published
- 2008-06-01
- Volume
- 37
- Issue
- 1
- Pages
- 317-336
- ISSN
- 1936-122X (ISSN-L)
- 1936-1238
- OpenAlex
- W2166288313
- Cited by
- 517
- References
- 64
- FWCI
- 2.29
- Type
- journal article
- Language
- en
- Open access
- closed
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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