Evidence map›Paper›PMID 21840995›Full record

ArticleThe Journal of biological chemistry2011

Coupling dTTP hydrolysis with DNA unwinding by the DNA helicase of bacteriophage T7.

Ajit K Satapathy, Arkadiusz W Kulczyk, Sharmistha Ghosh, Antoine M van Oijen, Charles C Richardson

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
0.7field-weighted citation impact, top 31% 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

13 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
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  6. Cryo-EM structure of the replisome reveals multiple interactions coordinating DNA synthesis.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
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  12. Molecular interactions in the priming complex of bacteriophage T7.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  13. 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 2 countries.

Ajit K SatapathyDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 02115, USA.
Arkadiusz W Kulczyk
Sharmistha Ghosh
Antoine M van Oijen
Charles C Richardson
Harvard University · USInstitute of Molecular Biology and Biophysics · RU

Funding

STRUCTURE AND SYNTHESIS OF DNAR01GM054397 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI RICHARDSON, CHARLES C. · 1996 to 2011
$7.6M
NIGMS NIH HHS GM54397NIGMS NIH HHS R01 GM054397
6 · The paper itself

Abstract

The DNA helicase encoded by gene 4 of bacteriophage T7 assembles on single-stranded DNA as a hexamer of six identical subunits with the DNA passing through the center of the toroid. The helicase couples the hydrolysis of dTTP to unidirectional translocation on single-stranded DNA and the unwinding of duplex DNA. Phe(523), positioned in a β-hairpin loop at the subunit interface, plays a key role in coupling the hydrolysis of dTTP to DNA unwinding. Replacement of Phe(523) with alanine or valine abolishes the ability of the helicase to unwind DNA or allow T7 polymerase to mediate strand-displacement synthesis on duplex DNA. In vivo complementation studies reveal a requirement for a hydrophobic residue with long side chains at this position. In a crystal structure of T7 helicase, when a nucleotide is bound at a subunit interface, Phe(523) is buried within the interface. However, in the unbound state, it is more exposed on the outer surface of the helicase. This structural difference suggests that the β-hairpin bearing the Phe(523) may undergo a conformational change during nucleotide hydrolysis. We postulate that upon hydrolysis of dTTP, Phe(523) moves from within the subunit interface to a more exposed position where it contacts the displaced complementary strand and facilitates unwinding.

Indexed as

Bacteriophage T7Crystallography, X-RayDNA PrimaseDNA, ViralEscherichia coliHydrolysisHydrophobic and Hydrophilic InteractionsProtein Structure, SecondaryThymine NucleotidesViral ProteinsDNA PrimaseDNA, Viralthymidine 5'-triphosphateThymine NucleotidesViral Proteins

Identifiers

PMID21840995
PMCPMC3190778
OpenAlexW2107875903

What OpenQuestion holds

Textmetadata
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.