ArticleNature communications2014
Evidence for an electrostatic mechanism of force generation by the bacteriophage T4 DNA packaging motor.
Article in Nature communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
25 citing papers in PubMed.
- Dynamics of viral self-assembly, viral genome packaging, and virus-cell interactions studied by optical tweezers.European biophysics journal : EBJ · 2026Review
- Methods for Studying Motor-Driven Viral DNA Packaging in Bacteriophages phi29, Lambda, and T4 via Single DNA Molecule Manipulation and Rapid Solution Exchange.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Crucial Roles of Electricity in Virology.Reviews of physiology, biochemistry and pharmacology · 2025Review
- Viral Genomic DNA Packaging Machinery.Sub-cellular biochemistry · 2024Review
- Optical Tweezers to Study Viruses.Sub-cellular biochemistry · 2024Review
- Insights into a viral motor: the structure of the HK97 packaging termination assembly.Nucleic acids research · 2023Article
- Review
- Determining Trap Compliances, Microsphere Size Variations, and Response Linearities in Single DNA Molecule Elasticity Measurements with Optical Tweezers.Frontiers in molecular biosciences · 2021Article
- Function of a viral genome packaging motor from bacteriophage T4 is insensitive to DNA sequence.Nucleic acids research · 2020Article
- Functional Dissection of a Viral DNA Packaging Machine's Walker B Motif.Journal of molecular biology · 2019Article
- DNA Conformational Changes Play a Force-Generating Role during Bacteriophage Genome Packaging.Biophysical journal · 2019Article
- Evidence that a catalytic glutamate and an 'Arginine Toggle' act in concert to mediate ATP hydrolysis and mechanochemical coupling in a viral DNA packaging motor.Nucleic acids research · 2019Article
- Nucleotide-dependent DNA gripping and an end-clamp mechanism regulate the bacteriophage T4 viral packaging motor.Nature communications · 2018Article
- Artificial bio-nanomachines based on protein needles derived from bacteriophage T4.Biophysical reviews · 2018Review
- Mechanochemical coupling and bi-phasic force-velocity dependence in the ultra-fast ring ATPase SpoIIIE.eLife · 2018Article
- Charge Influences Substrate Recognition and Self-Assembly of Hydrophobic FG Sequences.Biophysical journal · 2017Article
- Altering the speed of a DNA packaging motor from bacteriophage T4.Nucleic acids research · 2017Article
- Experimental comparison of forces resisting viral DNA packaging and driving DNA ejection.Physical review. E · 2017Article
- A Molecular View of the Dynamics of dsDNA Packing Inside Viral Capsids in the Presence of Ions.Biophysical journal · 2017Article
- Walker-A Motif Acts to Coordinate ATP Hydrolysis with Motor Output in Viral DNA Packaging.Journal of molecular biology · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors.
Funding
Abstract
How viral packaging motors generate enormous forces to translocate DNA into viral capsids remains unknown. Recent structural studies of the bacteriophage T4 packaging motor have led to a proposed mechanism wherein the gp17 motor protein translocates DNA by transitioning between extended and compact states, orchestrated by electrostatic interactions between complimentarily charged residues across the interface between the N- and C-terminal subdomains. Here we show that site-directed alterations in these residues cause force dependent impairments of motor function including lower translocation velocity, lower stall force and higher frequency of pauses and slips. We further show that the measured impairments correlate with computed changes in free-energy differences between the two states. These findings support the proposed structural mechanism and further suggest an energy landscape model of motor activity that couples the free-energy profile of motor conformational states with that of the ATP hydrolysis cycle.
Indexed as
Identifiers
What OpenQuestion holds
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.