Evidence map›Paper›PMID 11593009›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2001

Functional analysis of mutant and wild-type Drosophila origin recognition complex.

I Chesnokov, D Remus, M Botchan

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed
3.9field-weighted citation impact, top 6% 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

58 citing papers in PubMed, 124 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Orc6 is a component of the replication fork and enables efficient mismatch repair.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  6. Article
  7. Article
  8. HumanizedGenetics · 2020
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. 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
  14. Review
  15. Mechanisms and regulation of DNA replication initiation in eukaryotes.Critical reviews in biochemistry and molecular biology · 2017
    Review
  16. Article
  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

3 authors at 2 institutions in 1 country.

I ChesnokovDepartment of Molecular and Cell Biology, Division of Biochemistry and Molecular Biology, University of California, Berkeley, CA 94720, USA.
D Remus
M Botchan
University of California, Berkeley · USCold Spring Harbor Laboratory · US

Funding

TRANSFORMATION OF CELLS BY SV-40 VIRUSR01CA030490 · NCI · UNIVERSITY OF CALIFORNIA BERKELEY · PI BERGER, JAMES M., BOTCHAN, MICHAEL R. · 1985 to 2020
$5.1M
REGULATORY INTERACTIONS BETWEEN TUMOR VIRUSES AND CELLSR37CA030490 · NCI · UNIVERSITY OF CALIFORNIA BERKELEY · PI BOTCHAN, MICHAEL R. · 1988 to 2014
$4.8M
DNA replication and cytokinesisR01GM097052 · NIGMS · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI CHESNOKOV, IGOR N · 2011 to 2014
$1.1M
NCI NIH HHS CA-30490NCI NIH HHS R01 CA030490NCI NIH HHS R37 CA030490NIGMS NIH HHS R01 GM097052
6 · The paper itself

Abstract

The origin recognition complex (ORC) is the DNA replication initiator protein in eukaryotes. We have reconstituted a functional recombinant Drosophila ORC and compared activities of the wild-type and several mutant ORC variants. Drosophila ORC is an ATPase, and our studies show that the ORC1 subunit is essential for ATP hydrolysis and for ATP-dependent DNA binding. Moreover, DNA binding by ORC reduces its ATP hydrolysis activity. In vitro, ORC binds to chromatin in an ATP-dependent manner, and this process depends on the functional AAA(+) nucleotide-binding domain of ORC1. Mutations in the ATP-binding domain of ORC1 are unable to support cell-free DNA replication. However, mutations in the putative ATP-binding domain of either the ORC4 or ORC5 subunits do not affect either of these functions. We also provide evidence that the Drosophila ORC6 subunit is directly required for all of these activities and that a large pool of ORC6 is present in the cytoplasm, cytologically proximal to the cell membrane. Studies reported here provide the first functional dissection of a metazoan initiator and highlight the basic conserved and divergent features among Drosophila and budding yeast ORC complexes.

Indexed as

DNA ReplicationAdenosine TriphosphatasesAdenosine TriphosphateAnimalsCell MembraneCell NucleusDNADNA-Binding ProteinsDrosophila melanogasterDrosophila ProteinsHydrolysisMembrane ProteinsMutagenesisNuclear ProteinsOrigin Recognition ComplexAdenosine TriphosphatasesAdenosine TriphosphateDNADNA-Binding ProteinsDrosophila ProteinsMembrane ProteinsNuclear ProteinsOrc1 protein, DrosophilaOrc4 protein, DrosophilaOrigin Recognition Complex

Identifiers

PMID11593009
PMCPMC59756
OpenAlexW1970515182

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.