Evidence map›Paper›PMID 21846330›Full record

ArticleThe Biochemical journal2011

The human Suv3 helicase interacts with replication protein A and flap endonuclease 1 in the nucleus.

Susanne T Venø, Tomasz Kulikowicz, Cezar Pestana, Piotr P Stepien, Tinna Stevnsner, Vilhelm A Bohr

Open access · greenAbstract read
In one paragraph

Article in The Biochemical journal, 2011. 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 25% 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, 20 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. Human mitochondrial degradosome prevents harmful mitochondrial R loops and mitochondrial genome instability.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  7. Article
  8. Review
  9. Article
  10. Borrowing nuclear DNA helicases to protect mitochondrial DNA.International journal of molecular sciences · 2015
    Review
  11. Article
  12. Article
  13. Minimizing the damage: repair pathways keep mitochondrial DNA intact.Nature reviews. Molecular cell biology · 2012
    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

6 authors at 2 institutions in 2 countries.

Susanne T VenøLaboratory of Molecular Gerontology, National Institute on Aging, National Institutes of Health, Baltimore, MD 21224, USA.
Tomasz Kulikowicz
Cezar Pestana
Piotr P Stepien
Tinna Stevnsner
Vilhelm A Bohr
Aarhus University · DKUniversity of Warsaw · PL

Funding

Mitochondrial DNA Repair Processes In Oxidative Stress And AgingZIAAG000733 · NIA · NATIONAL INSTITUTE ON AGING · PI FERRUCCI, LUIGI · 2009 to 2022
$9.2M
OXIDATIVE STRESS MITOCHONDRIAZ01AG000733 · NIA · NATIONAL INSTITUTE ON AGING · PI BOHR, VILHELM A · 1996 to 2008
$1.6M
Intramural NIH HHS Z01 AG000733Intramural NIH HHS ZIA AG000733NIA NIH HHS Z01 AG000733-15
6 · The paper itself

Abstract

The hSuv3 (human Suv3) helicase has been shown to be a major player in mitochondrial RNA surveillance and decay, but its physiological role might go beyond this functional niche. hSuv3 has been found to interact with BLM (Bloom's syndrome protein) and WRN (Werner's syndrome protein), members of the RecQ helicase family involved in multiple DNA metabolic processes, and in protection and stabilization of the genome. In the present study, we have addressed the possible role of hSuv3 in genome maintenance by examining its potential association with key interaction partners of the RecQ helicases. By analysis of hSuv3 co-IP (co-immunoprecipitation) complexes, we identify two new interaction partners of hSuv3: the RPA (replication protein A) and FEN1 (flap endonuclease 1). Utilizing an in vitro biochemical assay we find that low amounts of RPA inhibit helicase activity of hSuv3 on a forked substrate. Another single-strand-binding protein, mtSSB (mitochondrial single-strand-binding protein), fails to affect hSuv3 activity, indicating that the functional interaction is specific for hSuv3 and RPA. Further in vitro studies demonstrate that the flap endonuclease activity of FEN1 is stimulated by hSuv3 independently of flap length. hSuv3 is generally thought to be a mitochondrial helicase, but the physical and functional interactions between hSuv3 and known RecQ helicase-associated proteins strengthen the hypothesis that hSuv3 may play a significant role in nuclear DNA metabolism as well.

Indexed as

Cell NucleusDEAD-box RNA HelicasesExodeoxyribonucleasesFlap EndonucleasesHumansImmunoprecipitationRecQ HelicasesReplication Protein ASubstrate SpecificityWerner Syndrome HelicaseBloom syndrome proteinDEAD-box RNA HelicasesExodeoxyribonucleasesFEN1 protein, humanFlap EndonucleasesRecQ HelicasesReplication Protein ASUPV3L1 protein, humanWerner Syndrome HelicaseWRN protein, human

Identifiers

PMID21846330
PMCPMC4366949
OpenAlexW2011873740

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.