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Record W2790692653 · doi:10.1093/jcag/gwy008.170

A169 FLUORESCENT LABELING OF THE HCV HELICASE TO MONITOR NUCLEIC ACID UNWINDING BY FRET

2018· article· en· W2790692653 on OpenAlexaffabout
Christopher J. Ablenas, Megan H. Powdrill, Tyler A. Shaw, Gonzalo Cosa, Matthias Götte

Bibliographic record

VenueJournal of the Canadian Association of Gastroenterology · 2018
Typearticle
Languageen
FieldBiochemistry, Genetics and Molecular Biology
TopicVirus-based gene therapy research
Canadian institutionsUniversity of AlbertaUniversity of OttawaMcGill University
Fundersnot available
KeywordsHelicaseFörster resonance energy transferNucleic acidFluorophoreBiochemistryChemistryRNA Helicase ABiophysicsAmino acidDNAMolecular biologyBiologyRNAFluorescenceGene

Abstract

fetched live from OpenAlex

The hepatitis C virus (HCV) non-structural protein 3 (NS3) contains a helicase activity essential for viral replication. The helicase binds to single-stranded (ss) regions of nucleic acids and unwinds duplexes in an ATP-dependent manner. The mechanism by which the helicase disrupts RNA secondary structure in the viral genome to make way for the replication machinery remains elusive. Several mechanisms have been proposed, which include an active mechanism whereby the helicase actively engages the ss/double-stranded (ds) junction of the substrate to unwind the duplex, and a passive mechanism where the helicase binds and translocates along a ss nucleic acid overhang, taking advantage of transient melting at the ss/ds junction. To generate site-specific fluorescently labeled HCV helicase as a tool to track the movement of the enzyme during unwinding and monitor the dynamics of this process. The unnatural amino acid p-azido phenylalanine was incorporated in the recombinant HCV helicase during protein expression in E. coli. Using a strain-promoted azide-alkyne click reaction we developed a one-step process to screen for both protein expression and reactivity of the azido group from the incorporated unnatural amino acid. After successfully identifying a position in the helicase for incorporation of the unnatural amino acid and fluorescent labeling with a Cy5 fluorophore, we used the site-specific fluorescently labeled enzyme to monitor the location of binding by Förster Resonance Energy Transfer (FRET) to DNA substrates modified with an appropriate Cy3 donor fluorophore. Using our approach to simultaneously screen for protein expression with the unnatural amino acid as well as reactivity of the incorporated unnatural amino acid, we identified a position in the HCV helicase suitable for incorporation of p-azido phenylalanine and fluorescent labeling with a Cy5 fluorescent dye. We then developed a plate-based FRET assay to confirm that we could detect the location of binding on a DNA substrate in a distance-dependent manner. Finally, using single molecule fluorescence microscopy we were able to detect binding by FRET for individual enzyme-substrate complexes. The FRET-based assay has the potential to monitor distinct steps of the unwinding process. Single molecule FRET experiments will provide a deeper understanding of the mechanism by which the helicase interacts with its substrate during unwinding and the dynamics involved in this process. CIHRthe Canadian Network on Hepatitis C (CanHepC), and the Fonds de recherche du Québec – Santé (FRQS)

Fetched live from OpenAlex and de-inverted. Abstracts are not stored in this database: the inverted indexes are 8.6 GB of the frame’s 9.3 GB of text, and the host has 13 GB free.

How this classification was reachedexpand

Full frame machine prediction

Teacher imitation

Not calibrated prevalence, not ground truth. Human validation pending. The Gemma side is a direct model label for every work in the frame, read from the title-only record. The Codex side is a classifier learned from the 10,348 direct Codex labels and calibrated to design-weighted sample rates; fields without enough sample support carry no Codex call. Candidate is the union of the two sides; consensus is their intersection. These outputs are machine_predicted_unvalidated and are not human labels.

metaresearch head score (Codex)0.000
metaresearch head score (Gemma)0.000
Version: metacan-v3-hybrid-931329e0061cValidation status: machine_predicted_unvalidated
Candidate categoriesnone
Consensus categoriesnone
DomainCandidate signal: none · Consensus signal: none
Study designCandidate signal: Bench or experimental · Consensus signal: Bench or experimental
GenreCandidate signal: Empirical · Consensus signal: Empirical
Teacher disagreement score0.001
Threshold uncertainty score0.005

Distilled classifier scores by category (both heads)

CategoryCodexGemma
Metaresearch0.0000.000
Meta-epidemiology (narrow)0.0010.000
Meta-epidemiology (broad)0.0000.000
Bibliometrics0.0000.000
Science and technology studies0.0000.000
Scholarly communication0.0000.000
Open science0.0010.000
Research integrity0.0010.001
Insufficient payload (model declined to judge)0.0010.001

Machine scores (provisional)

The two teacher heads of the student model, read on this work. A score orders the frame for review; it never asserts a category, and the validation status ships verbatim with every row.

Baseline scores from an immature model (maturity gate not passed, 7 training rounds). Scores rank; they never assert a category.

Opus teacher head0.008
GPT teacher head0.256
Teacher spread0.248 · how far apart the two teachers sit on this one work
Validation statusscore_only:v0-immature-baseline · verbatim from the scoring run: score_only means the number may rank works, and no category label ships from it

Classification

machine, unvalidated

Machine predicted; a candidate call from one source (direct Gemma or distilled Codex), not a consensus.

The models applied no category: nothing in the taxonomy fit this work.
Study designBench or experimental
Domainnot available
GenreEmpirical

How this classification was reached, model by model and score by score, is at the end of the page under "How this classification was reached".

Quick stats

Citations0
Published2018
Admission routes2
Has abstractyes

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