Evidence map›Paper›PMID 19181665›Full record

ArticleThe Journal of biological chemistry2009

Poly(ADP-ribose) Polymerase 1 Interacts with Nuclear Respiratory Factor 1 (NRF-1) and Plays a Role in NRF-1 Transcriptional Regulation.

Mohammad B Hossain, Ping Ji, Ramakrishnan Anish, Raymond H Jacobson, Shinako Takada

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

28 citing papers in PubMed, 57 citations in OpenAlex.

  1. To Break or Not to Break: The Role of TOP2B in Transcription.International journal of molecular sciences · 2023
    Review
  2. Article
  3. Article
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  5. Article
  6. Article
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  9. Review
  10. Article
  11. Review
  12. Article
  13. Estrogens regulate life and death in mitochondria.Journal of bioenergetics and biomembranes · 2017
    Review
  14. Article
  15. Review
  16. Transcriptional roles of PARP1 in cancer.Molecular cancer research : MCR · 2014
    Review
  17. PARP inhibition delays progression of mitochondrial encephalopathy in mice.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2014
    Article
  18. Mitochondrial stress signaling promotes cellular adaptations.International journal of cell biology · 2014
    Review
  19. Article
  20. Visualization of a DNA-PK/PARP1 complex.Nucleic acids research · 2012
    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

5 authors at 1 institution in 1 country.

Mohammad B HossainDepartment of Biochemistry and Molecular Biology, Genes and Development Program of the Graduate School of Biomedical Sciences, The University of Texas M. D. Anderson Cancer Center, Houston, Texas 77030, USA.
Ping Ji
Ramakrishnan Anish
Raymond H Jacobson
Shinako Takada
The University of Texas Health Science Center at Houston · US

Funding

Regulatory mechanisms of HBV X gene TranscriptionR01AI057504 · NIAID · UNIVERSITY OF TX MD ANDERSON CAN CTR · PI KLEIN, WILLIAM H. · 2005 to 2009
$1.6M
The TFIID Complex-Biophysical &Structural StudiesR01GM069769 · NIGMS · UNIVERSITY OF TX MD ANDERSON CAN CTR · PI TAKADA, SHINAKO · 2004 to 2008
$1.4M
NIAID NIH HHS AI057504NIGMS NIH HHS GM069769
6 · The paper itself

Abstract

Nuclear respiratory factor 1 (NRF-1) is one of the key transcriptional activators for nuclear-coded genes involved in mitochondrial biogenesis and function as well as for many housekeeping genes. A transcriptional co-activator PGC-1 and its related family member PRC have previously been shown to interact with NRF-1 and co-activate NRF-1. We show here that NRF-1 can also directly interact with poly(ADP-ribose) polymerase 1 (PARP-1) and co-purify the PARP-1.DNA-PK.Ku80.Ku70.topoisomerase IIbeta-containing protein complex. Our in vitro binding experiments show that DNA-binding/dimerization domain of NRF-1 and the N-terminal half of PARP-1, which contains two Zinc fingers and the auto-modification domain, are responsible for the interaction, and that this interaction occurs with or without PARP-1 poly(ADP-ribosyl)ation (PARylation). DNA-bound NRF-1 can form a complex with PARP-1, suggesting that NRF-1 can recruit the PARP-1.DNA-PK.Ku80.Ku70.topoisomerase IIbeta-containing protein complex to the promoter. PARP-1 can also PARylate the DNA-binding domain of NRF-1 and negatively regulate NRF-1.PARP-1 interaction. Transient transfection and chromatin immunoprecipitation experiments suggest that PARP-1 plays a role during transcriptional activation by NRF-1. Our finding identifies a new aspect of transcriptional regulation used by NRF-1.

Indexed as

AnimalsAntigens, NuclearDNA-Activated Protein KinaseDNA-Binding ProteinsDNA Topoisomerases, Type IIHeLa CellsHumansKu AutoantigenMiceMultiprotein ComplexesNuclear ProteinsNuclear Respiratory Factor 1Poly (ADP-Ribose) Polymerase-1Poly(ADP-ribose) PolymerasesPromoter Regions, GeneticProtein Structure, TertiaryAntigens, NuclearDNA-Activated Protein KinaseDNA-Binding ProteinsDNA Topoisomerases, Type IIKu AutoantigenMultiprotein ComplexesNRF1 protein, humanNrf1 protein, mouseNuclear ProteinsNuclear Respiratory Factor 1PARP1 protein, humanParp1 protein, mousePoly (ADP-Ribose) Polymerase-1Poly(ADP-ribose) PolymerasesPRKDC protein, humanPrkdc protein, mouseXrcc6 protein, humanXrcc6 protein, mouse

Identifiers

PMID19181665
PMCPMC2659221
OpenAlexW2091606631

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.