Evidence map›Paper›PMID 18647841›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2008

The architecture of the DNA replication origin recognition complex in Saccharomyces cerevisiae.

Zhiqiang Chen, Christian Speck, Patricia Wendel, Chunyan Tang, Bruce Stillman, Huilin Li

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

44 citing papers in PubMed, 76 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Structural mechanism of helicase loading onto replication origin DNA by ORC-Cdc6.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Mechanisms and regulation of DNA replication initiation in eukaryotes.Critical reviews in biochemistry and molecular biology · 2017
    Review
  12. Article
  13. Article
  14. Cryo-EM of dynamic protein complexes in eukaryotic DNA replication.Protein science : a publication of the Protein Society · 2017
    Review
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  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 3 institutions in 1 country.

Zhiqiang ChenBiology Department, Brookhaven National Laboratory, Upton, NY 11973, USA.
Christian Speck
Patricia Wendel
Chunyan Tang
Bruce Stillman
Huilin Li
Cold Spring Harbor Laboratory · USBrookhaven National Laboratory · USStony Brook University · US

Funding

VIRAL TRANSACTIVATIONP01CA013106 · NCI · COLD SPRING HARBOR LABORATORY · PI William Richard McCombie · 1985 to 2026
$116.8M
REGULATION OF DNA REPLICATIONR01GM045436 · NIGMS · COLD SPRING HARBOR LABORATORY · PI STILLMAN, BRUCE W. · 1991 to 2025
$15.8M
Structural mechanism of DNA replicationR35GM131754 · NIGMS · VAN ANDEL RESEARCH INSTITUTE · PI Huilin Li · 2019 to 2026
$6.0M
The Structural Basis of Eukaryotic Replication Origin Licensing by Cryo-EMR01GM074985 · NIGMS · BROOKHAVEN SCIENCE ASSOC-BROOKHAVEN LAB · PI LI, HUILIN · 2006 to 2010
$1.7M
Medical Research Council MC_U120085811NCI NIH HHS P01 CA013106NIGMS NIH HHS GM45436NIGMS NIH HHS GM74985NIGMS NIH HHS R01 GM045436NIGMS NIH HHS R01 GM074985NIGMS NIH HHS R35 GM131754
6 · The paper itself

Abstract

The origin recognition complex (ORC) is conserved in all eukaryotes. The six proteins of the Saccharomyces cerevisiae ORC that form a stable complex bind to origins of DNA replication and recruit prereplicative complex (pre-RC) proteins, one of which is Cdc6. To further understand the function of ORC we recently determined by single-particle reconstruction of electron micrographs a low-resolution, 3D structure of S. cerevisiae ORC and the ORC-Cdc6 complex. In this article, the spatial arrangement of the ORC subunits within the ORC structure is described. In one approach, a maltose binding protein (MBP) was systematically fused to the N or the C termini of the five largest ORC subunits, one subunit at a time, generating 10 MBP-fused ORCs, and the MBP density was localized in the averaged, 2D EM images of the MBP-fused ORC particles. Determining the Orc1-5 structure and comparing it with the native ORC structure localized the Orc6 subunit near Orc2 and Orc3. Finally, subunit-subunit interactions were determined by immunoprecipitation of ORC subunits synthesized in vitro. Based on the derived ORC architecture and existing structures of archaeal Orc1-DNA structures, we propose a model for ORC and suggest how ORC interacts with origin DNA and Cdc6. The studies provide a basis for understanding the overall structure of the pre-RC.

Indexed as

DNA ReplicationReplication OriginCarrier ProteinsCell Cycle ProteinsDNA, FungalImage Processing, Computer-AssistedImaging, Three-DimensionalImmunoprecipitationMaltose-Binding ProteinsMicroscopy, ElectronModels, MolecularMolecular ConformationProtein Structure, TertiarySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsCarrier ProteinsCDC6 protein, S cerevisiaeCell Cycle ProteinsDNA, FungalMaltose-Binding ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID18647841
PMCPMC2480615
OpenAlexW2146273596

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.