Evidence map›Paper›PMID 18319248›Full record

ArticleThe Journal of biological chemistry2008

A biotin interference assay highlights two different asymmetric interaction profiles for lambda integrase arm-type binding sites in integrative versus excisive recombination.

Dane Hazelbaker, Marco A Azaro, Arthur Landy

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2008. 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
1.1field-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

13 citing papers in PubMed, 18 citations in OpenAlex.

  1. The Integration and Excision of CTnDOT.Microbiology spectrum · 2015
    Review
  2. Review
  3. Article
  4. Nucleoprotein architectures regulating the directionality of viral integration and excision.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  5. New applications for phage integrases.Journal of molecular biology · 2014
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Teaching Cre to follow directions.Proceedings of the National Academy of Sciences of the United States of America · 2009
    Article
  13. A chimeric Cre recombinase with regulated directionality.Proceedings of the National Academy of Sciences of the United States of America · 2008
    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

3 authors at 2 institutions in 1 country.

Dane HazelbakerDepartment of Molecular Biology, Cellular Biology, and Biochemistry, Brown University, Providence, Rhode Island 02912, USA.
Marco A Azaro
Arthur Landy
Brown University · USRutgers, The State University of New Jersey · US

Funding

MECHANISMS OF SITE SPECIFIC RECOMBINATIONR01GM062723 · NIGMS · BROWN UNIVERSITY · PI LANDY, ARTHUR · 2000 to 2012
$6.4M
RECOMBINATION INTERMEDIATES-- PROPERTIES &PROCESSINGR01GM033928 · NIGMS · BROWN UNIVERSITY · PI LANDY, ARTHUR · 1985 to 2011
$6.2M
NIGMS NIH HHS GM33928NIGMS NIH HHS GM62723NIGMS NIH HHS R01 GM033928NIGMS NIH HHS R01 GM062723
6 · The paper itself

Abstract

The site-specific recombinase integrase encoded by bacteriophage lambda promotes integration and excision of the viral chromosome into and out of its Escherichia coli host chromosome through a Holliday junction recombination intermediate. This intermediate contains an integrase tetramer bound via its catalytic carboxyl-terminal domains to the four "core-type" sites of the Holliday junction DNA and via its amino-terminal domains to distal "arm-type" sites. The two classes of integrase binding sites are brought into close proximity by an ensemble of accessory proteins that bind and bend the intervening DNA. We have used a biotin interference assay that probes the requirement for major groove protein binding at specified DNA loci in conjunction with DNA protection, gel mobility shift, and genetic experiments to test several predictions of the models derived from the x-ray crystal structures of minimized and symmetrized surrogates of recombination intermediates lacking the accessory proteins and their cognate DNA targets. Our data do not support the predictions of "non-canonical" DNA targets for the N-domain of integrase, and they indicate that the complexes used for x-ray crystallography are more appropriate for modeling excisive rather than integrative recombination intermediates. We suggest that the difference in the asymmetric interaction profiles of the N-domains and arm-type sites in integrative versus excisive recombinogenic complexes reflects the regulation of recombination, whereas the asymmetry of these patterns within each reaction contributes to directionality.

Indexed as

Attachment Sites, MicrobiologicalBacteriophage lambdaBinding SitesBiological AssayBiotinDNA, CruciformDNA NucleotidyltransferasesIntegrasesModels, BiologicalNucleic Acid ConformationProtein BindingProtein Structure, TertiaryRecombination, GeneticSequence DeletionBiotinDNA, CruciformDNA NucleotidyltransferasesIntegrasesSite-specific recombinase

Identifiers

PMID18319248
PMCPMC2384228
OpenAlexW2071929839

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.