ArticleNucleic acids research2010
Dynamics on multiple timescales in the RNA-directed RNA polymerase from the cystovirus phi6.
Article in Nucleic acids research, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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Who cites it
10 citing papers in PubMed.
- Cystoviral RNA-directed RNA polymerases: Regulation of RNA synthesis on multiple time and length scales.Virus research · 2017Review
- Methyl Relaxation Measurements Reveal Patterns of Fast Dynamics in a Viral RNA-Directed RNA Polymerase.Biochemistry · 2015Article
- Common and unique features of viral RNA-dependent polymerases.Cellular and molecular life sciences : CMLS · 2014Review
- Cystoviral polymerase complex protein P7 uses its acidic C-terminal tail to regulate the RNA-directed RNA polymerase P2.Journal of molecular biology · 2014Article
- Vaccine-derived mutation in motif D of poliovirus RNA-dependent RNA polymerase lowers nucleotide incorporation fidelity.The Journal of biological chemistry · 2013Article
- Nuclear magnetic resonance spectroscopy of the circadian clock of cyanobacteria.Integrative and comparative biology · 2013Review
- Motif D of viral RNA-dependent RNA polymerases determines efficiency and fidelity of nucleotide addition.Structure (London, England : 1993) · 2012Article
- Molecular dynamics simulations of viral RNA polymerases link conserved and correlated motions of functional elements to fidelity.Journal of molecular biology · 2011Article
- Slow conformational dynamics in the cystoviral RNA-directed RNA polymerase P2: influence of substrate nucleotides and template RNA.Biochemistry · 2011Article
- Long-range interaction networks in the function and fidelity of poliovirus RNA-dependent RNA polymerase studied by nuclear magnetic resonance.Biochemistry · 2010Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
Abstract
The de novo initiating RNA-directed RNA polymerase (RdRP), P2, forms the central machinery in the infection cycle of the bacteriophage phi6 by performing the dual tasks of replication and transcription of the double-stranded RNA genome in the host cell. By measurement and quantitative analysis of multiple-quantum spin-relaxation data for the delta1 positions of Ile residues that are distributed over the 3D-fold of P2, we find that the enzyme is dynamic both on the fast (ps-ns) and slow (micros-ms) timescales. The characteristics of several motional modes including those that coincide with the catalytic timescale (500-800/s) are altered in the presence of substrate analogs and single-stranded RNA templates. These studies reveal the plasticity of this finely tuned molecular machine and represent a first step towards linking structural information available from a host of crystal structures to catalytic mechanisms and timescales obtained from the measurements of kinetics for homologous systems in solution.
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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.