Evidence map›Paper›PMID 17693398›Full record

ArticleThe Journal of biological chemistry2007

Binding and activation of DNA topoisomerase III by the Rmi1 subunit.

Chi-Fu Chen, Steven J Brill

Open access · hybridAbstract readComparative Study
In one paragraph

Article in The Journal of biological chemistry, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

54 citing papers in PubMed, 64 citations in OpenAlex.

  1. Article
  2. Mechanistic basis for relaxation of DNA supercoils by human topoisomerase IIIα-RMI1-RMI2.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Mechanism of Bloom syndrome complex assembly required for double Holliday junction dissolution and genome stability.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  7. Article
  8. Review
  9. The many lives of type IA topoisomerases.The Journal of biological chemistry · 2020
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. An Overview of the Molecular Mechanisms of Recombinational DNA Repair.Cold Spring Harbor perspectives in biology · 2015
    Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. The dissolution of double Holliday junctions.Cold Spring Harbor perspectives in biology · 2014
    Review
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

2 authors at 1 institution in 1 country.

Chi-Fu ChenDepartment of Molecular Biology and Biochemistry, Rutgers University, Piscataway, New Jersey 08854.
Steven J BrillDepartment of Molecular Biology and Biochemistry, Rutgers University, Piscataway, New Jersey 08854. Electronic address: brill@mbcl.rutgers.edu.
Rutgers, The State University of New Jersey · US

Funding

Genomic Stability and RecQ DNA Helicases in YeastR01GM071268 · NIGMS · RUTGERS THE ST UNIV OF NJ NEW BRUNSWICK · PI BRILL, STEVEN J. · 2004 to 2012
$2.5M
NIGMS NIH HHS R01 GM071268NIGMS NIH HHS R01GM072569
6 · The paper itself

Abstract

Rmi1 is a conserved oligonucleotide and oligosaccharide binding-fold protein that is associated with RecQ DNA helicase complexes from humans (BLM-TOP3 alpha) and yeast (Sgs1-Top3). Although human RMI1 stimulates the dissolution activity of BLM-TOP3 alpha, its biochemical function is unknown. Here we examined the role of Rmi1 in the yeast complex. Consistent with the similarity of top3Delta and rmi1Delta phenotypes, we find that a stable Top3.Rmi1 complex can be isolated from yeast cells overexpressing these two subunits. Compared with Top3 alone, this complex displays increased superhelical relaxation activity. The isolated Rmi1 subunit also stimulates Top3 activity in reconstitution experiments. In both cases elevated temperatures are required for optimal relaxation unless the substrate contains a single-strand DNA (ssDNA) bubble. Interestingly, Rmi1 binds only weakly to ssDNA on its own, but it stimulates the ssDNA binding activity of Top3 5-fold. Top3 and Rmi1 also cooperate to bind the Sgs1 N terminus and promote its interaction with ssDNA. These results demonstrate that Top3-Rmi1 functions as a complex and suggest that Rmi1 stimulates Top3 by promoting its interaction with ssDNA.

Indexed as

Carrier ProteinsDNA-Binding ProteinsDNA, FungalDNA, Single-StrandedDNA Topoisomerases, Type IHumansMultiprotein ComplexesNuclear ProteinsProtein BindingRecQ HelicasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsCarrier ProteinsDNA-Binding ProteinsDNA, FungalDNA, Single-StrandedDNA Topoisomerases, Type IMultiprotein ComplexesNuclear ProteinsRecQ HelicasesRMI1 protein, humanRmi1 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSGS1 protein, S cerevisiaeTOP3 protein, S cerevisiae

Identifiers

PMID17693398
PMCPMC2804875
OpenAlexW2076744932

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.