Evidence map›Paper›PMID 25245947›Full record

ArticleNucleic acids research2014

RecQ-core of BLM unfolds telomeric G-quadruplex in the absence of ATP.

Jagat B Budhathoki, Sujay Ray, Vaclav Urban, Pavel Janscak, Jaya G Yodh, Hamza Balci

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

41 citing papers in PubMed, 63 citations in OpenAlex.

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  11. Creation and resolution of non-B-DNA structural impediments during replication.Critical reviews in biochemistry and molecular biology · 2022
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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 4 institutions in 3 countries.

Jagat B BudhathokiDepartment of Physics, Kent State University, Kent, OH 44242, USA.
Sujay RayDepartment of Physics, Kent State University, Kent, OH 44242, USA.
Vaclav UrbanInstitute of Molecular Genetics AS CR, Prague, Czech Republic.
Pavel JanscakInstitute of Molecular Genetics AS CR, Prague, Czech Republic Institute of Molecular Cancer Research, University of Zurich, Zurich, Switzerland.
Jaya G YodhDepartment of Physics and Center for the Physics of Living Cells, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA hbalci@kent.edu.
Hamza BalciDepartment of Physics, Kent State University, Kent, OH 44242, USA hbalci@kent.edu.
Kent State University · USCzech Academy of Sciences, Institute of Molecular Genetics · CZUniversity of Illinois Urbana-Champaign · USUniversity of Zurich · CH

Funding

A Single Molecule Exploration of Protein and G-quadruplex InteractionsR15GM109386 · NIGMS · KENT STATE UNIVERSITY · PI BALCI, HAMZA · 2015 to 2015
$346k
NIGMS NIH HHS R15 GM109386
6 · The paper itself

Abstract

Various helicases and single-stranded DNA (ssDNA) binding proteins are known to destabilize G-quadruplex (GQ) structures, which otherwise result in genomic instability. Bulk biochemical studies have shown that Bloom helicase (BLM) unfolds both intermolecular and intramolecular GQ in the presence of ATP. Using single molecule FRET, we show that binding of RecQ-core of BLM (will be referred to as BLM) to ssDNA in the vicinity of an intramolecular GQ leads to destabilization and unfolding of the GQ in the absence of ATP. We show that the efficiency of BLM-mediated GQ unfolding correlates with the binding stability of BLM to ssDNA overhang, as modulated by the nucleotide state, ionic conditions, overhang length and overhang directionality. In particular, we observed enhanced GQ unfolding by BLM in the presence of non-hydrolysable ATP analogs, which has implications for the underlying mechanism. We also show that increasing GQ stability, via shorter loops or higher ionic strength, reduces BLM-mediated GQ unfolding. Finally, we show that while WRN has similar activity as BLM, RecQ and RECQ5 helicases do not unfold GQ in the absence of ATP at physiological ionic strength. In summary, our study points to a novel and potentially very common mechanism of GQ destabilization mediated by proteins binding to the vicinity of these structures.

Indexed as

G-QuadruplexesAdenosine DiphosphateAdenosine TriphosphateDNA, Single-StrandedHumansRecQ HelicasesTelomereadenosine 5'-O-(3-thiotriphosphate)Adenosine DiphosphateAdenosine TriphosphateBloom syndrome proteinDNA, Single-StrandedRecQ Helicases

Identifiers

PMID25245947
PMCPMC4191421
OpenAlexW2057859059

What OpenQuestion holds

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LicenceCC BY
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.