Evidence map›Paper›PMID 18704118›Full record

ArticleEMBO reports2008

Rtt101 and Mms1 in budding yeast form a CUL4(DDB1)-like ubiquitin ligase that promotes replication through damaged DNA.

Iram Waris Zaidi, Gwénaël Rabut, Ana Poveda, Hartmut Scheel, Johan Malmström, Helle Ulrich, Kay Hofmann, Philippe Pasero, Matthias Peter, Brian Luke

Open access · greenAbstract readComparative Study
In one paragraph

Article in EMBO reports, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 papers.

0numbers the graph read from it
0cells of the map it votes in
69citing papers in PubMed
5.7field-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

69 citing papers in PubMed, 98 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. The Ubiquitin-like Proteins ofBiomolecules · 2023
    Review
  8. Article
  9. Article
  10. Biomolecules · 2021
    Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Review
  16. Review
  17. Human CRL4Oncotarget · 2017
    Article
  18. Review
  19. Article
  20. Article

9 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

10 authors at 5 institutions in 4 countries.

Iram Waris ZaidiInstitute of Biochemistry, Swiss Federal Institute of Technology Zurich (ETH), ETH Hoenggerberg, 8093 Zurich, Switzerland.
Gwénaël Rabut
Ana Poveda
Hartmut Scheel
Johan Malmström
Helle Ulrich
Kay Hofmann
Philippe Pasero
Matthias Peter
Brian Luke
ETH Zurich · CHMiltenyi Biotec (Germany) · DECancer Research UK · GBCentre National de la Recherche Scientifique · FRInstitut de Génétique Humaine · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In budding yeast the cullin Rtt101 promotes replication fork progression through natural pause sites and areas of DNA damage, but its relevant subunits and molecular mechanism remain poorly understood. Here, we show that in budding yeast Mms1 and Mms22 are functional subunits of an Rtt101-based ubiquitin ligase that associates with the conjugating-enzyme Cdc34. Replication forks in mms1Delta, mms22Delta and rtt101Delta cells are sensitive to collisions with drug-induced DNA lesions, but not to transient pausing induced by nucleotide depletion. Interaction studies and sequence analysis have shown that Mms1 resembles human DDB1, suggesting that Rtt101(Mms1) is the budding yeast counterpart of the mammalian CUL4(DDB1) ubiquitin ligase family. Rtt101 interacts in an Mms1-dependent manner with the putative substrate-specific adaptors Mms22 and Crt10, the latter being a regulator of expression of ribonucleotide reductase. Taken together, our data suggest that the Rtt101(Mms1) ubiquitin ligase complex might be required to reorganize replication forks that encounter DNA lesions.

Indexed as

Anaphase-Promoting Complex-CyclosomeCullin ProteinsDNA-Binding ProteinsDNA DamageDNA ReplicationHumansProtein SubunitsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitin-Conjugating EnzymesUbiquitin-Protein Ligase ComplexesUbiquitin-Protein LigasesAnaphase-Promoting Complex-CyclosomeCDC34 protein, humanCDC34 protein, S cerevisiaeCullin ProteinsDDB1 protein, humanDNA-Binding ProteinsMms1 protein, S cerevisiaeMms22 protein, S cerevisiaeProtein SubunitsRTT101 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitin-Conjugating EnzymesUbiquitin-Protein Ligase ComplexesUbiquitin-Protein Ligases

Identifiers

PMID18704118
PMCPMC2572122
OpenAlexW2055776712

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.