Evidence map›Paper›PMID 16489218›Full record

ArticleGenetics2006

Cotransport of the heterodimeric small subunit of the Saccharomyces cerevisiae ribonucleotide reductase between the nucleus and the cytoplasm.

Xiuxiang An, Zhen Zhang, Kui Yang, Mingxia Huang

Open access · bronzeAbstract read
In one paragraph

Article in Genetics, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

19 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
  2. Genes · 2021
    Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Conserved electron donor complex Dre2-Tah18 is required for ribonucleotide reductase metallocofactor assembly and DNA synthesis.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Functional dissection of a HECT ubiquitin E3 ligase.Molecular & cellular proteomics : MCP · 2008
    Article
  15. Article
  16. Article
  17. Role of the C terminus of the ribonucleotide reductase large subunit in enzyme regeneration and its inhibition by Sml1.Proceedings of the National Academy of Sciences of the United States of America · 2007
    Article
  18. Article
  19. 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

4 authors at 2 institutions in 1 country.

Xiuxiang AnDepartment of Biochemistry and Molecular Genetics, University of Colorado Health Sciences Center, Aurora, Colorado 80045, USA.
Zhen Zhang
Kui Yang
Mingxia Huang
University of Colorado Anschutz Medical Campus · USUniversity of Colorado Health · US

Funding

Function and Regulation of DNA Damage Response GenesR01CA095207 · NCI · UNIVERSITY OF COLORADO DENVER · PI HUANG, MINGXIA · 2003 to 2007
$1.3M
NCI NIH HHS CA-095207NCI NIH HHS R01 CA095207
6 · The paper itself

Abstract

Ribonucleotide reductase (RNR) catalyzes the rate-limiting step in de novo deoxyribonucleotide biosynthesis and is essential in DNA replication and repair. Cells have evolved complex mechanisms to modulate RNR activity during normal cell cycle progression and in response to genotoxic stress. A recently characterized mode of RNR regulation is DNA damage-induced RNR subunit redistribution. The RNR holoenzyme consists of a large subunit, R1, and a small subunit, R2. The Saccharomyces cerevisiae R2 is an Rnr2:Rnr4 heterodimer. Rnr2 generates a diferric-tyrosyl radical cofactor required for catalysis; Rnr4 facilitates cofactor assembly and stabilizes the resulting holo-heterodimer. Upon DNA damage, Rnr2 and Rnr4 undergo checkpoint-dependent, nucleus-to-cytoplasm redistribution, resulting in colocalization of R1 and R2. Here we present evidence that Rnr2 and Rnr4 are transported between the nucleus and the cytoplasm as one protein complex. Tagging either Rnr2 or Rnr4 with a nuclear export sequence causes cytoplasmic localization of both proteins. Moreover, mutations at the Rnr2:Rnr4 heterodimer interface can affect the localization of both proteins without disrupting the heterodimeric complex. Finally, the relocalization of Rnr4 appears to involve both active export and blockage of nuclear import. Our findings provide new insights into the mechanism of DNA damage-induced RNR subunit redistribution.

Indexed as

Biological Transport, ActiveCell NucleusCytoplasmDimerizationDNA DamageGene ExpressionMutationNuclear Export SignalsProtein TransportRibonucleotide ReductasesSaccharomyces cerevisiaeNuclear Export SignalsRibonucleotide Reductases

Identifiers

PMID16489218
PMCPMC1461425
OpenAlexW2101976185

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.