Evidence map›Paper›PMID 10869431›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2000

In organello formaldehyde crosslinking of proteins to mtDNA: identification of bifunctional proteins.

B A Kaufman, S M Newman, R L Hallberg, C A Slaughter, P S Perlman, R A Butow

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 76 papers.

0numbers the graph read from it
0cells of the map it votes in
76citing papers in PubMed
5.1field-weighted citation impact, top 4% 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

76 citing papers in PubMed, 207 citations in OpenAlex.

  1. Article
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  8. Mitochondrial functional resilience after TFAM ablation in the adult heart.American journal of physiology. Cell physiology · 2021
    Article
  9. Review
  10. Review
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  12. Review
  13. Organization of DNA in Mammalian Mitochondria.International journal of molecular sciences · 2019
    Review
  14. Review
  15. Review
  16. Review
  17. Molecular model of the mitochondrial genome segregation machinery inProceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  18. Review
  19. Article
  20. Article

16 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.

B A KaufmanDepartment of Molecular Biology, and Howard Hughes Medical Institute, University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75390-9148, USA.
S M Newman
R L Hallberg
C A Slaughter
P S Perlman
R A Butow
Howard Hughes Medical Institute · USSyracuse University · USSouthwestern Medical Center · US

Funding

NIGMS NIH HHS GM33510
6 · The paper itself

Abstract

The segregating unit of mtDNA is a protein-DNA complex called the nucleoid. In an effort to understand how nucleoid proteins contribute to mtDNA organization and inheritance, we have developed an in organello formaldehyde crosslinking procedure to identify proteins associated with mtDNA. Using highly purified mitochondria, we observed a time-dependent crosslinking of protein to mtDNA as determined by sedimentation through isopycnic cesium chloride gradients. We detected approximately 20 proteins crosslinked to mtDNA and identified 11, mostly by mass spectrometry. Among them is Abf2p, an abundant, high-mobility group protein that is known to function in nucleoid morphology, and in mtDNA transactions. In addition to several other proteins with known DNA binding properties or that function in mtDNA maintenance, we identified other mtDNA-associated proteins that were not anticipated, such as the molecular chaperone Hsp60p and a Krebs cycle protein, Kgd2p. Genetic experiments indicate that hsp60-ts mutants have a petite-inducing phenotype at the permissive temperature and that a kgd2Delta mutation increases the petite-inducing phenotype of an abf2Delta mutation. Crosslinking and DNA gel shift experiments show that Hsp60p binds to single-stranded DNA with high specificity for the template strand of a putative origin of mtDNA replication. These data identify bifunctional proteins that participate in the stability of rho(+) mtDNA.

Indexed as

Cell FractionationChaperonin 60Citric Acid CycleCross-Linking ReagentsDNA-Binding ProteinsDNA, FungalDNA, MitochondrialDNA ReplicationDNA, Single-StrandedFormaldehydeFungal ProteinsKetoglutarate Dehydrogenase ComplexMass SpectrometryMitochondriaPoint MutationProtein BindingChaperonin 60Cross-Linking ReagentsDNA-Binding ProteinsDNA, FungalDNA, MitochondrialDNA, Single-StrandedFormaldehydeFungal ProteinsKetoglutarate Dehydrogenase Complex

Identifiers

PMID10869431
PMCPMC16620
OpenAlexW2084900854

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.