Evidence map›Paper›PMID 10567589›Full record

ArticleMolecular and cellular biology1999

Characterization of a fission yeast SUMO-1 homologue, pmt3p, required for multiple nuclear events, including the control of telomere length and chromosome segregation.

K Tanaka, J Nishide, K Okazaki, H Kato, O Niwa, T Nakagawa, H Matsuda, M Kawamukai, Y Murakami

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 85 papers.

0numbers the graph read from it
0cells of the map it votes in
85citing papers in PubMed
3.6field-weighted citation impact, top 7% 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

85 citing papers in PubMed, 191 citations in OpenAlex.

  1. The SUMO Pathway.Methods in molecular biology (Clifton, N.J.) · 2025
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  5. Smc5/6 Complex Promotes Rad3Molecular and cellular biology · 2022
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  7. Article
  8. Article
  9. Article
  10. Review
  11. SUMOlock reveals a more complete Aspergillus nidulans SUMOylome.Fungal genetics and biology : FG & B · 2019
    Article
  12. Suppressor screening reveals common kleisin-hinge interaction in condensin and cohesin, but different modes of regulation.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

25 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

9 authors at 3 institutions in 3 countries.

K TanakaDepartment of Applied Bioscience and Biotechnology, Faculty of Life and Environmental Science, Shimane University, Matsue 690-8504, Japan. ktanaka@life.shimane-u.ac.jp
J Nishide
K Okazaki
H Kato
O Niwa
T Nakagawa
H Matsuda
M Kawamukai
Y Murakami
Kazusa DNA Research Institute · JPKyoto University · JPShimane University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Unlike ubiquitin, the ubiquitin-like protein modifier SUMO-1 and its budding yeast homologue Smt3p have been shown to be more important for posttranslational protein modification than for protein degradation. Here we describe the identification of the SUMO-1 homologue of fission yeast, which we show to be required for a number of nuclear events including the control of telomere length and chromosome segregation. A disruption of the pmt3(+) gene, the Schizosaccharomyces pombe homologue of SMT3, was not lethal, but mutant cells carrying the disrupted gene grew more slowly. The pmt3Delta cells showed various phenotypes such as aberrant mitosis, sensitivity to various reagents, and high-frequency loss of minichromosomes. Interestingly, we found that pmt3(+) is required for telomere length maintenance. Loss of Pmt3p function caused a striking increase in telomere length. When Pmt3p synthesis was restored, the telomeres became gradually shorter. This is the first demonstration of involvement of one of the Smt3p/SUMO-1 family proteins in telomere length maintenance. Fusion of Pmt3p to green fluorescent protein (GFP) showed that Pmt3p was predominantly localized as intense spots in the nucleus. One of the spots was shown to correspond to the spindle pole body (SPB). During prometaphase- and metaphase, the bright GFP signals at the SPB disappeared. These observations suggest that Pmt3p is required for kinetochore and/or SPB functions involved in chromosome segregation. The multiple functions of Pmt3p described here suggest that several nuclear proteins are regulated by Pmt3p conjugation.

Indexed as

Chromosome SegregationSchizosaccharomyces pombe ProteinsSmall Ubiquitin-Related Modifier ProteinsTelomereAmino Acid SequenceAnimalsBase SequenceCell NucleusChromosomes, FungalDNA, FungalFungal ProteinsHumansMolecular Sequence DataPhenotypeRepressor ProteinsSchizosaccharomycesDNA, FungalFungal ProteinsPmt3 protein, S pombeRepressor ProteinsSchizosaccharomyces pombe ProteinsSmall Ubiquitin-Related Modifier ProteinsSUMO-1 ProteinSUMO2 protein, humanSUMO3 protein, humanUbiquitins

Identifiers

PMID10567589
PMCPMC85006
OpenAlexW1864629140

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.