Evidence map›Paper›PMID 18846224›Full record

ArticlePLoS genetics2008

Cooperation of sumoylated chromosomal proteins in rDNA maintenance.

Yoshimitsu Takahashi, Stanimir Dulev, Xianpeng Liu, Natalie Jasmin Hiller, Xiaolan Zhao, Alexander Strunnikov

Open access · goldAbstract read
In one paragraph

Article in PLoS genetics, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
1.8field-weighted citation impact, top 16% 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

45 citing papers in PubMed, 66 citations in OpenAlex.

  1. Article
  2. Article
  3. Multifaceted roles of SUMO in DNA metabolism.Nucleus (Austin, Tex.) · 2024
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Review
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Review
  16. The SUMO Pathway in Mitosis.Advances in experimental medicine and biology · 2017
    Review
  17. Article
  18. Article
  19. The Epigenetic Pathways to Ribosomal DNA Silencing.Microbiology and molecular biology reviews : MMBR · 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

6 authors at 5 institutions in 2 countries.

Yoshimitsu TakahashiLaboratory of Gene Regulation and Development, National Institute of Child Health and Human Development, NIH, Bethesda, MD, USA.
Stanimir Dulev
Xianpeng Liu
Natalie Jasmin Hiller
Xiaolan Zhao
Alexander Strunnikov
Memorial Sloan Kettering Cancer Center · USEunice Kennedy Shriver National Institute of Child Health and Human Development · USNational Institutes of Health · USPlovdiv University · BGRockefeller University · US

Funding

The Rtt107 interactome structures and functionsR01GM080670 · NIGMS · SLOAN-KETTERING INST CAN RESEARCH · PI ZHAO, XIAOLAN · 2007 to 2021
$4.5M
Intramural NIH HHSNIGMS NIH HHS GM080670NIGMS NIH HHS R01 GM080670
6 · The paper itself

Abstract

SUMO is a posttranslational modifier that can modulate protein activities, interactions, and localizations. As the GFP-Smt3p fusion protein has a preference for subnucleolar localization, especially when deconjugation is impaired, the nucleolar role of SUMO can be the key to its biological functions. Using conditional triple SUMO E3 mutants, we show that defects in sumoylation impair rDNA maintenance, i.e., the rDNA segregation is defective and the rDNA copy number decreases in these mutants. Upon characterization of sumoylated proteins involved in rDNA maintenance, we established that Top1p and Top2p, which are sumoylated by Siz1p/Siz2p, most likely collaborate with substrates of Mms21p to maintain rDNA integrity. Cohesin and condensin subunits, which both play important roles in rDNA stability and structures, are potential substrates of Mms21, as their sumoylation depends on Mms21p, but not Siz1p and Siz2p. In addition, binding of cohesin and condensin to rDNA is altered in the mms21-CH E3-deficient mutant.

Indexed as

Chromosomal Proteins, Non-HistoneDNA, FungalDNA, RibosomalDNA TopoisomerasesGenes, FungalMutationNuclear ProteinsProtein Processing, Post-TranslationalSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSmall Ubiquitin-Related Modifier ProteinsSUMO-1 ProteinUbiquitin-Protein LigasesChromosomal Proteins, Non-HistoneDNA, FungalDNA, RibosomalDNA TopoisomerasesMms21 protein, S cerevisiaeNuclear ProteinsSaccharomyces cerevisiae ProteinsSiz1 protein, S cerevisiaeSiz2 protein, S cerevisiaeSmall Ubiquitin-Related Modifier ProteinsSUMO-1 ProteinUbiquitin-Protein Ligases

Identifiers

PMID18846224
PMCPMC2563031
OpenAlexW2047071185

What OpenQuestion holds

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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.