Evidence map›Paper›PMID 25870416›Full record

ArticleNucleic acids research2015

Linker histone partial phosphorylation: effects on secondary structure and chromatin condensation.

Rita Lopez, Bettina Sarg, Herbert Lindner, Salvador Bartolomé, Inma Ponte, Pedro Suau, Alicia Roque

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

22 citing papers in PubMed, 37 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Review
  7. Unraveling linker histone interactions in nucleosomes.Current opinion in structural biology · 2021
    Review
  8. Article
  9. Review
  10. Article
  11. Histone H1 Post-Translational Modifications: Update and Future Perspectives.International journal of molecular sciences · 2020
    Review
  12. Emergence of chromatin hierarchical loops from protein disorder and nucleosome asymmetry.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  13. International journal of molecular sciences · 2020
    Review
  14. Review
  15. Article
  16. Review
  17. Article
  18. Review
  19. Nuclear and nucleolar activity of linker histone variant H1.0.Cellular & molecular biology letters · 2016
    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

7 authors at 2 institutions in 2 countries.

Rita LopezDepartamento de Bioquímica y Biología Molecular, Facultad de Biociencias, Universidad Autónoma de Barcelona, 08193, Bellaterra, Barcelona, Spain.
Bettina SargDivision of Clinical Biochemistry, Biocenter, Innsbruck Medical University, A-6020, Innsbruck, Austria.
Herbert LindnerDivision of Clinical Biochemistry, Biocenter, Innsbruck Medical University, A-6020, Innsbruck, Austria.
Salvador BartoloméLaboratorio de Luminiscencia y Espectroscopia de Biomoléculas, Universidad Autónoma de Barcelona, 08193, Bellaterra, Barcelona, Spain.
Inma PonteDepartamento de Bioquímica y Biología Molecular, Facultad de Biociencias, Universidad Autónoma de Barcelona, 08193, Bellaterra, Barcelona, Spain.
Pedro SuauDepartamento de Bioquímica y Biología Molecular, Facultad de Biociencias, Universidad Autónoma de Barcelona, 08193, Bellaterra, Barcelona, Spain.
Alicia RoqueDepartamento de Bioquímica y Biología Molecular, Facultad de Biociencias, Universidad Autónoma de Barcelona, 08193, Bellaterra, Barcelona, Spain alicia.roque@uab.es.
Universitat Autònoma de Barcelona · ESInnsbruck Medical University · AT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Linker histones are involved in chromatin higher-order structure and gene regulation. We have successfully achieved partial phosphorylation of linker histones in chicken erythrocyte soluble chromatin with CDK2, as indicated by HPCE, MALDI-TOF and Tandem MS. We have studied the effects of linker histone partial phosphorylation on secondary structure and chromatin condensation. Infrared spectroscopy analysis showed a gradual increase of β-structure in the phosphorylated samples, concomitant to a decrease in α-helix/turns, with increasing linker histone phosphorylation. This conformational change could act as the first step in the phosphorylation-induced effects on chromatin condensation. A decrease of the sedimentation rate through sucrose gradients of the phosphorylated samples was observed, indicating a global relaxation of the 30-nm fiber following linker histone phosphorylation. Analysis of specific genes, combining nuclease digestion and qPCR, showed that phosphorylated samples were more accessible than unphosphorylated samples, suggesting local chromatin relaxation. Chromatin aggregation was induced by MgCl2 and analyzed by dynamic light scattering (DLS). Phosphorylated chromatin had lower percentages in volume of aggregated molecules and the aggregates had smaller hydrodynamic diameter than unphosphorylated chromatin, indicating that linker histone phosphorylation impaired chromatin aggregation. These findings provide new insights into the effects of linker histone phosphorylation in chromatin condensation.

Indexed as

AnimalsChickensChromatinCyclin-Dependent Kinase 2HistonesHumansMagnesium ChlorideMicrococcal NucleasePhosphorylationProtein Structure, SecondaryChromatinCyclin-Dependent Kinase 2HistonesMagnesium ChlorideMicrococcal Nuclease

Identifiers

PMID25870416
PMCPMC4482070
OpenAlexW2039405194

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.