ArticleJournal of molecular biology2012
Unwinding initiation by the viral RNA helicase NPH-II.
Article in Journal of molecular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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Who cites it
11 citing papers in PubMed.
- Superfamily II helicases: the potential therapeutic target for cardiovascular diseases.Frontiers in cardiovascular medicine · 2023Review
- Identification and analysis of the interaction network of African swine fever virus D1133L with host proteins.Frontiers in microbiology · 2022Article
- Optical tweezer and TIRF microscopy for single molecule manipulation of RNA/DNA nanostructures including their rubbery property and single molecule counting.Biophysics reports · 2021Article
- Alternative RNA degradation pathways by the exonuclease Pop2p fromRNA (New York, N.Y.) · 2021Article
- Approaches for measuring the dynamics of RNA-protein interactions.Wiley interdisciplinary reviews. RNA · 2020Review
- The Chd1 chromatin remodeler forms long-lived complexes with nucleosomes in the presence of ADP·BeFThe Journal of biological chemistry · 2019Article
- Single-molecule fluorescence imaging: Generating insights into molecular interactions in virology.Journal of biosciences · 2018Review
- Life under the Microscope: Single-Molecule Fluorescence Highlights the RNA World.Chemical reviews · 2018Review
- Sen1 has unique structural features grafted on the architecture of the Upf1-like helicase family.The EMBO journal · 2017Article
- Division of Labor in an Oligomer of the DEAD-Box RNA Helicase Ded1p.Molecular cell · 2015Article
- Helicase-mediated changes in RNA structure at the single-molecule level.RNA biology · 2013Review
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
Viral RNA helicases of the NS3/NPH-II group unwind RNA duplexes by processive, directional translocation on one of the duplex strands. The translocation is preceded by a poorly understood unwinding initiation phase. For NPH-II from vaccinia virus, unwinding initiation is rate limiting for the overall unwinding reaction. To develop a mechanistic understanding of the unwinding initiation, we studied kinetic and thermodynamic aspects of this reaction phase for NPH-II in vitro, using biochemical and single molecule fluorescence approaches. Our data show that NPH-II functions as a monomer and that different stages of the ATP hydrolysis cycle dictate distinct binding preferences of NPH-II for duplex versus single-stranded RNA. We further find that the NPH-II-RNA complex does not adopt a single conformation but rather at least two distinct conformations in each of the analyzed stages of ATP hydrolysis. These conformations interconvert with rate constants that depend on the stage of the ATP hydrolysis cycle. Our data establish a basic mechanistic framework for unwinding initiation by NPH-II and suggest that the various stages of the ATP hydrolysis cycle do not induce single, stage-specific conformations in the NPH-II-RNA complex but primarily control transitions between multiple states.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.