Evidence map›Paper›PMID 25136112›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2014

Automodification switches PARP-1 function from chromatin architectural protein to histone chaperone.

Uma M Muthurajan, Maggie R D Hepler, Aaron R Hieb, Nicholas J Clark, Michael Kramer, Tingting Yao, Karolin Luger

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 93 papers.

0numbers the graph read from it
0cells of the map it votes in
93citing papers in PubMed
5.5field-weighted citation impact, top 3% 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

93 citing papers in PubMed, 147 citations in OpenAlex.

  1. Article
  2. PARP1 Exhibits an Enzymatically Inactive Chromatin Binding Mode.bioRxiv : the preprint server for biology · 2026
    Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
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  10. Article
  11. Article
  12. Article
  13. Review
  14. Review
  15. PARP1 modulates METTL3 promoter chromatin accessibility and associated LPAR5 RNA mMolecular therapy : the journal of the American Society of Gene Therapy · 2023
    Article
  16. Role of NADCellular and molecular neurobiology · 2023
    Review
  17. Article
  18. Article
  19. Review
  20. Review

33 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

7 authors at 1 institution in 1 country.

Uma M MuthurajanDepartment of Biochemistry and Molecular Biology, and.
Maggie R D HeplerDepartment of Biochemistry and Molecular Biology, and.
Aaron R HiebDepartment of Biochemistry and Molecular Biology, and Howard Hughes Medical Institute, Colorado State University, Fort Collins, CO 80523-1870.
Nicholas J ClarkDepartment of Biochemistry and Molecular Biology, and.
Michael KramerDepartment of Biochemistry and Molecular Biology, and.
Tingting YaoDepartment of Biochemistry and Molecular Biology, and.
Karolin LugerDepartment of Biochemistry and Molecular Biology, and Howard Hughes Medical Institute, Colorado State University, Fort Collins, CO 80523-1870 kluger@lamar.colostate.edu.
Howard Hughes Medical Institute · US

Funding

project 3P01GM088409 · NIGMS · COLORADO STATE UNIVERSITY · PI NYBORG, JENNIFER K. · 2010 to 2014
$7.3M
Structure and Function of Nucleosome Assembly Protein 1R01GM067777 · NIGMS · UNIVERSITY OF COLORADO · PI LUGER, KAROLIN · 2003 to 2015
$3.7M
Regulation of a Deubiquitinating Enzyme in Proteolysis and Chromatin RemodelingR01GM098401 · NIGMS · COLORADO STATE UNIVERSITY · PI YAO, TINGTING · 2011 to 2021
$2.9M
Howard Hughes Medical InstituteNIGMS NIH HHS GM067777NIGMS NIH HHS GM088409NIGMS NIH HHS GM098401NIGMS NIH HHS P01 GM088409NIGMS NIH HHS R01 GM067777NIGMS NIH HHS R01 GM098401
6 · The paper itself

Abstract

Poly [ADP-ribose] polymerase 1 (PARP-1) is a highly abundant chromatin-associated enzyme. It catalyzes the NAD(+)-dependent polymerization of long chains of poly-ADP ribose (PAR) onto itself in response to DNA damage and other cues. More recently, the enzymatic activity of PARP-1 has also been implicated in the regulation of gene expression. The molecular basis for the functional switch from chromatin architectural protein to transcription factor and DNA damage responder, triggered by PARP-1 automodification, is unknown. Here, we show that unmodified PARP-1 engages in at least two high-affinity binding modes with chromatin, one of which does not involve free DNA ends, consistent with its role as a chromatin architectural protein. Automodification reduces PARP-1 affinity for intact chromatin but not for nucleosomes with exposed DNA ends. Automodified (AM) PARP-1 has the ability to sequester histones (both in vitro and in cells) and to assemble nucleosomes efficiently in vitro. This unanticipated nucleosome assembly activity of AM-PARP-1, coupled with the fast turnover of the modification, suggests a model in which DNA damage or transcription events trigger transient histone chaperone activity.

Indexed as

ChromatinDNA DamageDNA RepairFluorescence Resonance Energy TransferHistone ChaperonesHumansNucleosomesPoly (ADP-Ribose) Polymerase-1Poly(ADP-ribose) PolymerasesProtein BindingProtein Processing, Post-TranslationalTranscription, GeneticChromatinHistone ChaperonesNucleosomesPARP1 protein, humanPoly (ADP-Ribose) Polymerase-1Poly(ADP-ribose) Polymerasesdissociation constantHI-FI FRETlinker DNAposttranslational modification

Identifiers

PMID25136112
PMCPMC4156740
OpenAlexW2166071408

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.