Evidence map›Paper›PMID 23763768›Full record

ArticleVirology2013

Revolution rather than rotation of AAA+ hexameric phi29 nanomotor for viral dsDNA packaging without coiling.

Chad Schwartz, Gian Marco De Donatis, Hui Zhang, Huaming Fang, Peixuan Guo

Open access · hybridAbstract read
In one paragraph

Article in Virology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
11.6field-weighted citation impact, top 1% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

39 citing papers in PubMed, 54 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Review
  6. Mechanisms of hexameric helicases.Critical reviews in biochemistry and molecular biology · 2021
    Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Assessing heterogeneity in oligomeric AAA+ machines.Cellular and molecular life sciences : CMLS · 2017
    Review
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Review
  18. Biological Nanomotors with a Revolution, Linear, or Rotation Motion Mechanism.Microbiology and molecular biology reviews : MMBR · 2016
    Review
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 1 country.

Chad SchwartzNanobiotechnology Center, Department of Pharmaceutical Sciences, and Markey Cancer Center, University of Kentucky, Lexington, KY 40536, USA.
Gian Marco De Donatis
Hui Zhang
Huaming Fang
Peixuan Guo
Markey Cancer Center · USUniversity of Kentucky · US

Funding

Phi29 Motor Nanopore for Single Molecule Sensing and dsDNA FingerprintingR01EB012135 · NIBIB · UNIVERSITY OF KENTUCKY · PI GUO, PEIXUAN · 2011 to 2019
$2.6M
Nanotube and nanogold to gear phi29 DNA packaging motorR01EB003730 · NIBIB · UNIVERSITY OF KENTUCKY · PI GUO, PEIXUAN · 2004 to 2012
$2.3M
RNA Nanotechnology in Cancer TherapyU01CA151648 · NCI · UNIVERSITY OF KENTUCKY · PI GUO, PEIXUAN, LI, HENRY · 2010 to 2014
$2.1M
NCI NIH HHS U01 CA151648NCI NIH HHS U01CA151648NIBIB NIH HHS R01 EB003730NIBIB NIH HHS R01EB003730NIBIB NIH HHS R01 EB012135
6 · The paper itself

Abstract

It has long been believed that the DNA-packaging motor of dsDNA viruses utilizes a rotation mechanism. Here we report a revolution rather than rotation mechanism for the bacteriophage phi29 DNA packaging motor. The phi29 motor contains six copies of the ATPase (Schwartz et al., this issue); ATP binding to one ATPase subunit stimulates the ATPase to adopt a conformation with a high affinity for dsDNA. ATP hydrolysis induces a new conformation with a lower affinity, thus transferring the dsDNA to an adjacent subunit by a power stroke. DNA revolves unidirectionally along the hexameric channel wall of the ATPase, but neither the dsDNA nor the ATPase itself rotates along its own axis. One ATP is hydrolyzed in each transitional step, and six ATPs are consumed for one helical turn of 360°. Transition of the same dsDNA chain along the channel wall, but at a location 60° different from the last contact, urges dsDNA to move forward 1.75 base pairs each step (10.5bp per turn/6ATP=1.75bp per ATP). Each connector subunit tilts with a left-handed orientation at a 30° angle in relation to its vertical axis that runs anti-parallel to the right-handed dsDNA helix, facilitating the one-way traffic of dsDNA. The connector channel has been shown to cause four steps of transition due to four positively charged lysine rings that make direct contact with the negatively charged DNA phosphate backbone. Translocation of dsDNA into the procapsid by revolution avoids the difficulties during rotation that are associated with DNA supercoiling. Since the revolution mechanism can apply to any stoichiometry, this motor mechanism might reconcile the stoichiometry discrepancy in many phage systems where the ATPase has been found as a tetramer, hexamer, or nonamer.

Indexed as

DNA PackagingAdenosine TriphosphatasesAdenosine TriphosphateBacillus PhagesDNA-Binding ProteinsDNA, ViralModels, BiologicalModels, MolecularProtein BindingProtein MultimerizationAdenosine TriphosphatasesAdenosine TriphosphateDNA-Binding ProteinsDNA, Viralprotein p16, bacteriophage phi29

Identifiers

PMID23763768
PMCPMC3850062
OpenAlexW2059231905

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
Read underepoch 390

Registered trials

None linked

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.