Evidence map›Paper›PMID 22858866›Full record

ArticleJournal of molecular biology2012

Structural and functional studies of the phage Sf6 terminase small subunit reveal a DNA-spooling device facilitated by structural plasticity.

Haiyan Zhao, Yvonne N Kamau, Theodore E Christensen, Liang Tang

Open access · bronzeAbstract read
In one paragraph

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 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.9field-weighted citation impact, top 10% 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

22 citing papers in PubMed, 30 citations in OpenAlex.

  1. Structural basis for DNA recognition by a viral genome-packaging machine.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  2. Microbiology spectrum · 2024
    Article
  3. Article
  4. Investigating the Prevalence of RNA-Binding Metabolic Enzymes inInternational journal of molecular sciences · 2023
    Article
  5. Terminase Subunits from the Pseudomonas-Phage E217.Journal of molecular biology · 2022
    Article
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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

4 authors at 1 institution in 1 country.

Haiyan ZhaoDepartment of Molecular Biosciences, University of Kansas, Lawrence, KS 66045, USA.
Yvonne N Kamau
Theodore E Christensen
Liang Tang
University of Kansas · US

Funding

Genome packaging in DNA virusesR01GM090010 · NIGMS · UNIVERSITY OF KANSAS LAWRENCE · PI TANG, LIANG · 2010 to 2014
$1.3M
NIGMS NIH HHS R01 GM090010NIGMS NIH HHS R01GM090010
6 · The paper itself

Abstract

In many DNA viruses, genome packaging is initiated by the small subunit of the packaging terminase, which specifically binds to the packaging signal on viral DNA and directs assembly of the terminase holoenzyme. We have experimentally mapped the DNA-interacting region on Shigella virus Sf6 terminase small subunit gp1, which occupies extended surface areas encircling the gp1 octamer, indicating that DNA wraps around gp1 through extensive contacts. High-resolution structures reveal large-scale motions of the gp1 DNA-binding domain mediated by the curved helix formed by residues 54-81 and an intermolecular salt bridge formed by residues Arg67 and Glu73, indicating remarkable structural plasticity underlying multivalent, pleomorphic gp1:DNA interactions. These results provide spatial restraints for protein:DNA interactions, which enable construction of a three-dimensional pseudo-atomic model for a DNA-packaging initiation complex assembled from the terminase small subunit and the packaging region on viral DNA. Our results suggest that gp1 functions as a DNA-spooling device, which may transform DNA into a specific architecture appropriate for interaction with and cleavage by the terminase large subunit prior to DNA translocation into viral procapsid. This may represent a common mechanism for the initiation step of DNA packaging in tailed double-stranded DNA bacterial viruses.

Indexed as

Adenosine TriphosphatasesCrystallography, X-RayDNA-Binding ProteinsDNA PackagingDNA, ViralEndodeoxyribonucleasesNucleoproteinsPodoviridaeShigellaViral ProteinsVirus AssemblyAdenosine Triphosphatasesbacteriophage SPP1 terminaseDNA-Binding ProteinsDNA, ViralEndodeoxyribonucleasesNucleoproteinsterminaseViral Proteins

Identifiers

PMID22858866
PMCPMC3572731
OpenAlexW2087279780

What OpenQuestion holds

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LicenceTDM
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.