Evidence map›Paper›PMID 19015240›Full record

ArticleMolecular and cellular biology2009

DNA-binding and -bending activities of SAP30L and SAP30 are mediated by a zinc-dependent module and monophosphoinositides.

Keijo M Viiri, Janne Jänis, Trevor Siggers, Taisto Y K Heinonen, Jarkko Valjakka, Martha L Bulyk, Markku Mäki, Olli Lohi

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed, 1 pooled it
1.5field-weighted citation impact, top 18% 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

36 citing papers in PubMed, 1 synthesis or guideline pooled it, 63 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. When PIPFrontiers in cell and developmental biology · 2022
    Review
  12. Article
  13. Article
  14. Article
  15. The nuclear phosphoinositide response to stress.Cell cycle (Georgetown, Tex.) · 2020
    Review
  16. Article
  17. Article
  18. Review
  19. Review
  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

8 authors at 4 institutions in 2 countries.

Keijo M ViiriPaediatric Research Centre, University of Tampere Medical School and Tampere University Hospital, 33520 Tampere, Finland.
Janne Jänis
Trevor Siggers
Taisto Y K Heinonen
Jarkko Valjakka
Martha L Bulyk
Markku Mäki
Olli Lohi
Tampere University Hospital · FITampere University · FIBrigham and Women's Hospital · USHarvard–MIT Division of Health Sciences and Technology · US

Funding

Universal, Compact Combinatorial Microarrays for DNA Binding Site DiscoveryR01HG003985 · NHGRI · BRIGHAM AND WOMEN'S HOSPITAL · PI BULYK, MARTHA L · 2006 to 2017
$4.9M
NHGRI NIH HHS R01 HG003985
6 · The paper itself

Abstract

Deacetylation of histones is carried out by a corepressor complex in which Sin3A is an essential scaffold protein. Two proteins in this complex, the Sin3A-associated proteins SAP30L and SAP30, have previously been suggested to function as linker molecules between various corepressors. In this report, we demonstrate new functions for human SAP30L and SAP30 by showing that they can associate directly with core histones as well as naked DNA. A zinc-coordinating structure is necessary for DNA binding, one consequence of which is bending of the DNA. We provide evidence that a sequence motif previously shown to be a nuclear localization signal is also a phosphatidylinositol (PI)-binding element and that binding of specific nuclear monophosphoinositides regulates DNA binding and chromatin association of SAP30L. PI binding also decreases the repression activity of SAP30L and affects its translocation from the nucleus to the cytoplasm. Our results suggest that SAP30L and SAP30 play active roles in recruitment of deacetylating enzymes to nucleosomes, and mediate key protein-protein and protein-DNA interactions involved in chromatin remodeling and transcription.

Indexed as

Amino Acid SequenceCell LineChromatinDNAElectrophoretic Mobility Shift AssayHistone DeacetylasesHistonesHumansMolecular Sequence DataNuclear Localization SignalsNuclear ProteinsNucleosomesPhosphatidylinositolsPoint MutationProtein Array AnalysisProtein ConformationChromatinDNAHistone DeacetylasesHistonesNuclear Localization SignalsNuclear ProteinsNucleosomesPhosphatidylinositolsSAP30L protein, humanSAP30 protein, humanZinc

Identifiers

PMID19015240
PMCPMC2612513
OpenAlexW2087513381

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.