Evidence map›Paper›PMID 8670844›Full record

ArticleThe EMBO journal1996

Identification of two DNA-binding sites on the globular domain of histone H5.

F A Goytisolo, S E Gerchman, X Yu, C Rees, V Graziano, V Ramakrishnan, J O Thomas

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.

0numbers the graph read from it
0cells of the map it votes in
56citing papers in PubMed
6.0field-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

56 citing papers in PubMed, 151 citations in OpenAlex.

  1. Review
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  8. Identification and characterization of histones inNAR genomics and bioinformatics · 2021
    Article
  9. Article
  10. The mechanistic basis for chromatin regulation by pioneer transcription factors.Wiley interdisciplinary reviews. Systems biology and medicine · 2019
    Review
  11. Article
  12. Article
  13. Review
  14. Review
  15. Linker histones: novel insights into structure-specific recognition of the nucleosome.Biochemistry and cell biology = Biochimie et biologie cellulaire · 2017
    Review
  16. Article
  17. Article
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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.

F A GoytisoloCambridge Centre for Molecular Recognition and Department of Biochemistry, University of Cambridge, UK.
S E Gerchman
X Yu
C Rees
V Graziano
V Ramakrishnan
J O Thomas
University of Cambridge · GB

Funding

STRUCTURAL STUDIES ON LINKER HISTONES AND CHROMATINR01GM042796 · NIGMS · UNIVERSITY OF UTAH · PI RAMAKRISHNAN, VENKATRAMAN · 1989 to 1999
–
NIGMS NIH HHS GM42796Wellcome Trust
6 · The paper itself

Abstract

The nature of the complexes of histones H1 and H5 and their globular domains (GH1 and GH5) with DNA suggested two DNA-binding sites which are likely to be the basis of the preference of H1 and H5 for the nucleosome, compared with free DNA. More recently the X-ray and NMR structures of GH5 and GH1, respectively, have identified two basic clusters on opposite sides of the domains as candidates for these sites. Removal of the positive charge at either location by mutagenesis impairs or abolishes the ability of GH5 to assemble cooperatively in 'tramline' complexes containing two DNA duplexes, suggesting impairment or loss of its ability to bind two DNA duplexes. The mutant forms of GH5 also fail to protect the additional 20 bp of nucleosomal DNA that are characteristically protected by H1, H5 and wild-type recombinant GH5. They still bind to H1/H5-depleted chromatin, but evidently inappropriately. These results confirm the existence of, and identify the major components of, two DNA-binding sites on the globular domain of histone H5, and they strongly suggest that both binding sites are required to position the globular domain correctly on the nucleosome.

Indexed as

Amino Acid SequenceAnimalsBinding SitesChromatinCircular DichroismDNADNA-Binding ProteinsHistonesHumansMicroscopy, ElectronMolecular Sequence DataMutagenesis, Site-DirectedNucleosomesProtein ConformationSequence Homology, Amino AcidChromatinDNADNA-Binding ProteinsHistonesNucleosomes

Identifiers

PMID8670844
PMCPMC451906
OpenAlexW1601865702

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.