Evidence map›Paper›PMID 21502537›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2011

Structural analysis of human Orc6 protein reveals a homology with transcription factor TFIIB.

Shixuan Liu, Maxim Balasov, Hongfei Wang, Lijie Wu, Igor N Chesnokov, Yingfang Liu

Abstract readComparative Study
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

40 citing papers in PubMed, 59 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. ORChestra coordinates the replication and repair music.BioEssays : news and reviews in molecular, cellular and developmental biology · 2023
    Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. HumanizedGenetics · 2020
    Article
  14. Article
  15. Article
  16. 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
  17. Review
  18. Article
  19. A structural view of the initiators for chromosome replication.Current opinion in structural biology · 2018
    Review
  20. Conformational control and DNA-binding mechanism of the metazoan origin recognition complex.Proceedings of the National Academy of Sciences of the United States of America · 2018
    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 2 countries.

Shixuan LiuNational Laboratory of Biological Macromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China.
Maxim Balasov
Hongfei Wang
Lijie Wu
Igor N Chesnokov
Yingfang Liu
Chinese Academy of Sciences · CNInstitute of Biophysics · CNUniversity of Alabama at Birmingham · US

Funding

The Role of origin Recognition Complex in the Cell CycleR01GM069681 · NIGMS · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI CHESNOKOV, IGOR N · 2005 to 2009
$1.6M
DNA replication and cytokinesisR01GM097052 · NIGMS · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI CHESNOKOV, IGOR N · 2011 to 2014
$1.1M
NIGMS NIH HHS GM69681NIGMS NIH HHS GM69681-S1NIGMS NIH HHS GM97052NIGMS NIH HHS R01 GM069681NIGMS NIH HHS R01 GM097052
6 · The paper itself

Abstract

The Origin Recognition Complex (ORC) is a six-subunit protein important for the initiation of DNA replication in eukaryotic cells. Orc6 is the smallest and the least conserved among ORC subunits. It is required for the DNA replication but also has a function in cytokinesis in metazoan species, however, the mechanisms of Orc6 action in these processes are not clear. Here we report a structure of the middle domain of human Orc6. This domain has an overall fold similar to the corresponding helical domain of transcription factor TFIIB. Based on these findings, a model of Orc6 binding to DNA is produced. We have identified amino acids of Orc6 which are directly involved in DNA binding. Alterations of these amino acids abolish DNA binding ability of Orc6 and also result in reduced levels of DNA replication in vitro and in cultured cells. Our data indicate that Orc6 is one of the DNA binding subunits of ORC in metazoan species. We propose that Orc6 may participate in positioning of ORC at the origins of DNA replication similar to the role of TFIIB in positioning transcription preinitiation complex at the promoter.

Indexed as

Models, MolecularProtein BindingProtein ConformationAmino Acid SequenceAnimalsBromodeoxyuridineChromatography, GelCloning, MolecularCrystallizationDNA ReplicationDrosophilaElectrophoresis, Polyacrylamide GelGreen Fluorescent ProteinsHumansMolecular Sequence DataOrigin Recognition ComplexBromodeoxyuridineGreen Fluorescent ProteinsOrigin Recognition ComplexTranscription Factor TFIIB

Identifiers

PMID21502537
PMCPMC3088625
OpenAlexW2001222878

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.