Evidence map›Paper›PMID 17889664›Full record

ArticleMolecular cell2007

An interlocked dimer of the protelomerase TelK distorts DNA structure for the formation of hairpin telomeres.

Hideki Aihara, Wai Mun Huang, Tom Ellenberger

Abstract read
In one paragraph

Article in Molecular cell, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
–field-weighted citation impact
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

25 citing papers in PubMed.

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  20. Dicentric breakage at telomere fusions.Genes & development · 2010
    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.

Hideki AiharaDepartment of Biochemistry and Molecular Biophysics, Washington University School of Medicine, 660 South Euclid Avenue, St. Louis, MO 63110, USA.
Wai Mun Huang
Tom Ellenberger

Funding

STRUCTURAL STUDIES OF SITE-SPECIFIC RECOMBINATIONR01GM059902 · NIGMS · WASHINGTON UNIVERSITY · PI ELLENBERGER, TOM E. · 1999 to 2011
$3.0M
NIGMS NIH HHS GM59902NIGMS NIH HHS R01 GM059902
6 · The paper itself

Abstract

The termini of linear chromosomes are protected by specialized DNA structures known as telomeres that also facilitate the complete replication of DNA ends. The simplest type of telomere is a covalently closed DNA hairpin structure found in linear chromosomes of prokaryotes and viruses. Bidirectional replication of a chromosome with hairpin telomeres produces a catenated circular dimer that is subsequently resolved into unit-length chromosomes by a dedicated DNA cleavage-rejoining enzyme known as a hairpin telomere resolvase (protelomerase). Here we report a crystal structure of the protelomerase TelK from Klebsiella oxytoca phage varphiKO2, in complex with the palindromic target DNA. The structure shows the TelK dimer destabilizes base pairing interactions to promote the refolding of cleaved DNA ends into two hairpin ends. We propose that the hairpinning reaction is made effectively irreversible by a unique protein-induced distortion of the DNA substrate that prevents religation of the cleaved DNA substrate.

Indexed as

Nucleic Acid ConformationAmino Acid SequenceBacteriophagesBinding SitesDimerizationDNADNA ReplicationEnzyme PrecursorsModels, MolecularMolecular Sequence DataProtein BindingStatic ElectricitySubstrate SpecificityTelomeraseTelomereViral ProteinsDNAEnzyme PrecursorsTelomeraseViral Proteins

Identifiers

PMID17889664
PMCPMC2041798

What OpenQuestion holds

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Read underepoch 390

Registered trials

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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.