Evidence map›Paper›PMID 15601841›Full record

ArticleMolecular and cellular biology2005

Nse2, a component of the Smc5-6 complex, is a SUMO ligase required for the response to DNA damage.

Emily A Andrews, Jan Palecek, John Sergeant, Elaine Taylor, Alan R Lehmann, Felicity Z Watts

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 151 papers.

0numbers the graph read from it
0cells of the map it votes in
151citing papers in PubMed
5.0field-weighted citation impact, top 4% 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

151 citing papers in PubMed, 230 citations in OpenAlex.

  1. Article
  2. Review
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  8. Review
  9. RecessiveDiagnostics (Basel, Switzerland) · 2025
    Article
  10. In Vitro SUMOylation Assays with a DNA-Sensitive Multi-subunit E3 Ligase.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Genome control by SMC complexes.Nature reviews. Molecular cell biology · 2023
    Review
  20. Article

91 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

6 authors at 1 institution in 1 country.

Emily A AndrewsGenome Damage and Stability Centre, School of Life Sciences, University of Sussex, Falmer, Brighton BN1 9RQ, United Kingdom.
Jan Palecek
John Sergeant
Elaine Taylor
Alan R Lehmann
Felicity Z Watts
University of Sussex · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Schizosaccharomyces pombe SMC proteins Rad18 (Smc6) and Spr18 (Smc5) exist in a high-M(r) complex which also contains the non-SMC proteins Nse1, Nse2, Nse3, and Rad62. The Smc5-6 complex, which is essential for viability, is required for several aspects of DNA metabolism, including recombinational repair and maintenance of the DNA damage checkpoint. We have characterized Nse2 and show here that it is a SUMO ligase. Smc6 (Rad18) and Nse3, but not Smc5 (Spr18) or Nse1, are sumoylated in vitro in an Nse2-dependent manner, and Nse2 is itself autosumoylated, predominantly on the C-terminal part of the protein. Mutations of C195 and H197 in the Nse2 RING-finger-like motif abolish Nse2-dependent sumoylation. nse2.SA mutant cells, in which nse2.C195S-H197A is integrated as the sole copy of nse2, are viable, whereas the deletion of nse2 is lethal. Smc6 (Rad18) is sumoylated in vivo: the sumoylation level is increased upon exposure to DNA damage and is drastically reduced in the nse2.SA strain. Since nse2.SA cells are sensitive to DNA-damaging agents and to exposure to hydroxyurea, this implicates the Nse2-dependent sumoylation activity in DNA damage responses but not in the essential function of the Smc5-6 complex.

Indexed as

DNA DamageAmino Acid SequenceBlotting, WesternCell Cycle ProteinsCell SurvivalChromosomal Proteins, Non-HistoneDNA RepairDose-Response Relationship, RadiationEnzyme InhibitorsGene DeletionHydroxyureaKineticsMolecular Sequence DataMutationPlasmidsProtein BindingCell Cycle ProteinsChromosomal Proteins, Non-HistoneEnzyme InhibitorsHydroxyureaNse2 protein, S pombeSchizosaccharomyces pombe ProteinsSmc5 protein, S pombesmc6 protein, S pombe

Identifiers

PMID15601841
PMCPMC538766
OpenAlexW2100419900

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.