The DOI matches its Crossref record; 14 of the 14 references it cites were found in a registry or an index.
Active Disruption of an RNA-Protein Interaction by a DExH/D RNA Helicase
Abstract
All aspects of cellular RNA metabolism and the replication of many viruses require DExH/D proteins that manipulate RNA in a manner that requires nucleoside triphosphates. Although DExH/D proteins have been shown to unwind purified RNA duplexes, most RNA molecules in the cellular environment are complexed with proteins. It has therefore been speculated that DExH/D proteins may also affect RNA-protein interactions. We demonstrate that the DExH protein NPH-II from vaccinia virus can displace the protein U1A from RNA in an active adenosine triphosphate–dependent fashion. NPH-II increases the rate of U1A dissociation by more than three orders of magnitude while retaining helicase processivity. This indicates that DExH/D proteins can effectively catalyze protein displacement from RNA and thereby participate in the structural reorganization of ribonucleoprotein assemblies.
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Cites
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Cited by
Structural Basis for RNA Unwinding by the DEAD-Box Protein Drosophila Vasa
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Structure of the Exon Junction Core Complex with a Trapped DEAD-Box ATPase Bound to RNA
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Messenger RNA Turnover in Eukaryotes: Pathways and Enzymes
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Modulation of RNA Condensation by the DEAD-Box Protein eIF4A
Tauber, D., Tauber, G., Khong, A., Van Treeck, B., Pelletier, J., & Parker, R. (2020) · Cell · doi:10.1016/j.cell.2019.12.031 · Cited by 281
Preprotein-controlled catalysis in the helicase motor of SecA.
Karamanou, S., Gouridis, G., Papanikou, E., Sianidis, G., Gelis, I., Keramisanou, D., Vrontou, E., Kalodimos, C. G., & Economou, A. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601721 · Cited by 59
Metadata
- Authors
- Jankowsky, E., Gross, C. H., Shuman, S., & Pyle, A. M.
- Venue
- Science
- Published
- 2001-01-05
- Volume
- 291
- Issue
- 5501
- Pages
- 121-125
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2065868028
- Cited by
- 305
- References
- 14
- FWCI
- 8.47
- Type
- journal article
- Language
- en
- Open access
- closed
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