Evidence map›Paper›PMID 20538004›Full record

ArticleJournal of molecular biology2010

Architecture of the Tn7 posttransposition complex: an elaborate nucleoprotein structure.

Jason W Holder, Nancy L Craig

Open access · greenAbstract read
In one paragraph

Article in Journal of molecular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.0field-weighted citation impact, top 23% 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

15 citing papers in PubMed, 24 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Structural basis for DNA targeting by the Tn7 transposon.Nature structural & molecular biology · 2022
    Article
  8. Article
  9. Recruitment of CRISPR-Cas systems by Tn7-like transposons.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  10. Mechanisms of DNA Transposition.Microbiology spectrum · 2015
    Review
  11. Article
  12. The Tn7 transposition regulator TnsC interacts with the transposase subunit TnsB and target selector TnsD.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  13. Direct interaction between the TnsA and TnsB subunits controls the heteromeric Tn7 transposase.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  14. The emerging diversity of transpososome architectures.Quarterly reviews of biophysics · 2012
    Review
  15. Moving DNA around: DNA transposition and retroviral integration.Current opinion in structural biology · 2011
    Review
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

2 authors at 2 institutions in 1 country.

Jason W HolderHoward Hughes Medical Institute, Department of Molecular Biology & Genetics, Johns Hopkins University School of Medicine, 725 North Wolfe Street, 502 PCTB, Baltimore, MD 21205, USA.
Nancy L Craig
Howard Hughes Medical Institute · USJohns Hopkins University · US

Funding

BIOCHEMISTRY, CELLULAR AND MOLECULAR BIOLOGY PROGRAMT32GM007445 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI GREEN, RACHEL · 1985 to 2021
$24.1M
TRANSPOSITION OF TN7P01CA016519 · NCI · JOHNS HOPKINS UNIVERSITY · PI BOEKE, JEF D · 1985 to 2010
$21.4M
Transposition of Tn7 and HermesR01GM076425 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI CRAIG, NANCY CRAIG · 2006 to 2009
$1.6M
NCI NIH HHS P01 CA016519NCI NIH HHS P01 CA16519NIGMS NIH HHS R01 GM076425NIGMS NIH HHS T32 GM007445NIGMS NIH HHS T32-GM07445
6 · The paper itself

Abstract

Four transposition proteins encoded by the bacterial transposon Tn7, TnsA, TnsB, TnsC, and TnsD, mediate its site- and orientation-specific insertion into the chromosomal site attTn7. To establish which Tns proteins are actually present in the transpososome that executes DNA breakage and joining, we have determined the proteins present in the nucleoprotein product of transposition, the posttransposition complex (PTC), using fluorescently labeled Tns proteins. All four required Tns proteins are present in the PTC in which we also find that the Tn7 ends are paired by protein-protein contacts between Tns proteins bound to the ends. Quantification of the relative amounts of the fluorescent Tns proteins in the PTC indicates that oligomers of TnsA, TnsB, and TnsC mediate Tn7 transposition. High-resolution DNA footprinting of the DNA product of transposition attTn7Colon, two colonsTn7 revealed that about 350 bp of DNA on the transposon ends and on attTn7 contact the Tns proteins. All seven binding sites for TnsB, the component of the transposase that specifically binds the ends and mediates 3' end breakage and joining, are occupied in the PTC. However, the protection pattern of the sites closest to the Tn7 ends in the PTC are different from that observed with TnsB alone, likely reflecting the pairing of the ends and their interaction with the target nucleoprotein complex necessary for activation of the breakage and joining steps. We also observe extensive protection of the attTn7 sequences in the PTC and that alternative DNA structures in substrate attTn7 that are imposed by TnsD are maintained in the PTC.

Indexed as

Base SequenceBinding SitesDNA, BacterialDNA FootprintingDNA Transposable ElementsEscherichia coliEscherichia coli ProteinsMicroscopy, Atomic ForceMolecular Sequence DataMolecular StructureMultiprotein ComplexesNucleoproteinsTransposasesDNA, BacterialDNA Transposable ElementsEscherichia coli ProteinsMultiprotein ComplexesNucleoproteinsTransposases

Identifiers

PMID20538004
PMCPMC2927125
OpenAlexW1984559756

What OpenQuestion holds

Textmetadata
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.