Evidence map›Paper›PMID 20212038›Full record

ArticleThe Journal of biological chemistry2010

Dynamic effects of cofactors and DNA on the oligomeric state of human mitochondrial DNA helicase.

Tawn D Ziebarth, Rocio Gonzalez-Soltero, Magdalena M Makowska-Grzyska, Rafael Núñez-Ramírez, Jose-Maria Carazo, Laurie S Kaguni

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
1.2field-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

29 citing papers in PubMed, 39 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. Structural insight and characterization of human Twinkle helicase in mitochondrial disease.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  7. Article
  8. Review
  9. Review
  10. Organization of DNA in Mammalian Mitochondria.International journal of molecular sciences · 2019
    Review
  11. Article
  12. Article
  13. Review
  14. Assessing heterogeneity in oligomeric AAA+ machines.Cellular and molecular life sciences : CMLS · 2017
    Review
  15. Article
  16. Structure, function and evolution of the animal mitochondrial replicative DNA helicase.Critical reviews in biochemistry and molecular biology · 2016
    Review
  17. Article
  18. Mitochondrial DNA maintenance: an appraisal.Molecular and cellular biochemistry · 2015
    Review
  19. Article
  20. 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

6 authors at 2 institutions in 2 countries.

Tawn D ZiebarthDepartment of Biochemistry and Molecular Biology and the Center for Mitochondrial Science and Medicine, Michigan State University, East Lansing, Michigan 49924-1319, USA.
Rocio Gonzalez-Soltero
Magdalena M Makowska-Grzyska
Rafael Núñez-Ramírez
Jose-Maria Carazo
Laurie S Kaguni
Consejo Superior de Investigaciones Científicas · ESMichigan State University · US

Funding

Mitochondrial DNA Replisome: Mechanism, Structure and PhysiologyR01GM045295 · NIGMS · MICHIGAN STATE UNIVERSITY · PI KAGUNI, LAURIE SIMON · 1991 to 2013
$4.0M
NIGMS NIH HHS GM45295NIGMS NIH HHS R01 GM045295
6 · The paper itself

Abstract

We examined the effects of cofactors and DNA on the stability, oligomeric state and conformation of the human mitochondrial DNA helicase. We demonstrate that low salt conditions result in protein aggregation that may cause dissociation of oligomeric structure. The low salt sensitivity of the mitochondrial DNA helicase is mitigated by the presence of magnesium, nucleotide, and increased temperature. Electron microscopic and glutaraldehyde cross-linking analyses provide the first evidence of a heptameric oligomer and its interconversion from a hexameric form. Limited proteolysis by trypsin shows that binding of nucleoside triphosphate produces a conformational change that is distinct from the conformation observed in the presence of nucleoside diphosphate. We find that single-stranded DNA binding occurs in the absence of cofactors and renders the mitochondrial DNA helicase more susceptible to proteolytic digestion. Our studies indicate that the human mitochondrial DNA helicase shares basic properties with the SF4 replicative helicases, but also identify common features with helicases outside the superfamily, including dynamic conformations similar to other AAA(+) ATPases.

Indexed as

Protein MultimerizationAdenosine TriphosphatasesAdenosine TriphosphateBinding, CompetitiveCross-Linking ReagentsDNA HelicasesDNA, MitochondrialHumansHydrolysisMitochondriaModels, MolecularProtein BindingProtein ConformationThermodynamicsadenosine 5'-O-(3-thiotriphosphate)Adenosine TriphosphatasesAdenosine TriphosphateCross-Linking ReagentsDNA HelicasesDNA, Mitochondrial

Identifiers

PMID20212038
PMCPMC2863210
OpenAlexW1970885300

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.