Evidence map›Paper›PMID 10756203›Full record

ArticleNucleic acids research2000

Fission yeast hrp1, a chromodomain ATPase, is required for proper chromosome segregation and its overexpression interferes with chromatin condensation.

E J Yoo, Y H Jin, Y K Jang, P Bjerling, M Tabish, S H Hong, K Ekwall, S D Park

Open access · bronzeAbstract read
In one paragraph

Article in Nucleic acids research, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.1field-weighted citation impact, top 23% 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

11 citing papers in PubMed, 36 citations in OpenAlex.

  1. mRNA stability in the nucleus.Journal of Zhejiang University. Science. B · 2014
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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

8 authors at 3 institutions in 3 countries.

E J YooDepartment of Molecular Biology and Research Center for Cell Differentiation, Seoul National University, Seoul, Republic of Korea.
Y H Jin
Y K Jang
P Bjerling
M Tabish
S H Hong
K Ekwall
S D Park
Karolinska Institutet · SESeoul National University · KRNational Institutes of Health · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Hrp1 of Schizosaccharomyces pombe is a member of the CHD protein family, characterized by a chromodomain, a Myb-like telobox-related DNA-binding domain and a SNF2-related helicase/ATPase domain. CHD proteins are thought to be required for modification of the chromatin structure in transcription, but the exact roles of CHD proteins are not known. Here we examine the sub-cellular localization and biochemical activity of Hrp1 and the phenotypes of hrp1 Delta and Hrp1-overexpressing strains. Fluorescence microscopy revealed that Hrp1 protein is targeted to the nucleus. We found that Hrp1 exhibited DNA-dependent ATPase activity, stimulated by both single- and double-stranded DNA. Overexpression of Hrp1 caused slow cell growth accompanied by defective chromosome condensation in anaphase resulting in a 'cut' (celluntimelytorn) phenotype and chromosome loss. The hrp1 Delta mutation also caused abnormal anaphase and mini-chromosome loss phenotypes. Electron micrographs demonstrated that aberrantly shaped nucleoli appeared in Hrp1-overexpressing cells. Therefore, these results suggest that Hrp1 may play a role in mitotic chromosome segregation and maintenance of chromatin structure by utilizing the energy from ATP hydrolysis.

Indexed as

Chromosome SegregationmRNA Cleavage and Polyadenylation FactorsSaccharomyces cerevisiae ProteinsAdenosine TriphosphatasesAdenosine TriphosphateAnaphaseCell NucleolusCell NucleusChromatinChromosomes, FungalDNAFluorescent Antibody Technique, IndirectGene DeletionGene Expression Regulation, FungalHydrolysisMitosisAdenosine TriphosphatasesAdenosine TriphosphateChromatinDNAHRP1 protein, S cerevisiaemRNA Cleavage and Polyadenylation FactorsRibonucleoproteinsRNA-Binding ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID10756203
PMCPMC103280
OpenAlexW2118170309

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.