Evidence map›Paper›PMID 15973401›Full record

ArticleNature2005

A structural basis for allosteric control of DNA recombination by lambda integrase.

Tapan Biswas, Hideki Aihara, Marta Radman-Livaja, David Filman, Arthur Landy, Tom Ellenberger

Open access · greenAbstract read
In one paragraph

Article in Nature, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 94 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
94citing papers in PubMed, 1 pooled it
6.8field-weighted citation impact, top 2% 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

94 citing papers in PubMed, 1 synthesis or guideline pooled it, 174 citations in OpenAlex.

  1. Pooled it
  2. Identification and characterization ofMicrobiology spectrum · 2025
    Article
  3. Article
  4. Dynamics in Cre-loxP site-specific recombination.Current opinion in structural biology · 2024
    Review
  5. Precise Gene Knock-In Tools with Minimized Risk of DSBs: A Trend for Gene Manipulation.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024
    Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Archaeal tyrosine recombinases.FEMS microbiology reviews · 2021
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Identification, Characterization, and Genomic Analysis of NovelInternational journal of molecular sciences · 2020
    Article
  17. Frontiers in molecular biosciences · 2020
    Article
  18. The Site-Specific Recombination System of theFrontiers in microbiology · 2020
    Article
  19. Review
  20. Review

34 more citing papers are in PubMed but not listed here.

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

6 authors at 3 institutions in 1 country.

Tapan BiswasDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 02115, USA.
Hideki Aihara
Marta Radman-Livaja
David Filman
Arthur Landy
Tom Ellenberger
Brown University · USHarvard University · USHarvard University Press · 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 R01 GM033928NIGMS NIH HHS R01 GM062723
6 · The paper itself

Abstract

Site-specific DNA recombination is important for basic cellular functions including viral integration, control of gene expression, production of genetic diversity and segregation of newly replicated chromosomes, and is used by bacteriophage lambda to integrate or excise its genome into and out of the host chromosome. lambda recombination is carried out by the bacteriophage-encoded integrase protein (lambda-int) together with accessory DNA sites and associated bending proteins that allow regulation in response to cell physiology. Here we report the crystal structures of lambda-int in higher-order complexes with substrates and regulatory DNAs representing different intermediates along the reaction pathway. The structures show how the simultaneous binding of two separate domains of lambda-int to DNA facilitates synapsis and can specify the order of DNA strand cleavage and exchange. An intertwined layer of amino-terminal domains bound to accessory (arm) DNAs shapes the recombination complex in a way that suggests how arm binding shifts the reaction equilibrium in favour of recombinant products.

Indexed as

Allosteric RegulationAttachment Sites, MicrobiologicalBacteriophage lambdaBase SequenceCatalysisCrystallography, X-RayDNA, CruciformIntegrasesIsomerismModels, MolecularNucleic Acid ConformationPliabilityProtein ConformationRecombination, GeneticStructure-Activity RelationshipDNA, CruciformIntegrases

Identifiers

PMID15973401
PMCPMC1809751
OpenAlexW2004996851

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.