Evidence map›Paper›PMID 21461783›Full record

ArticleCellular and molecular life sciences : CMLS2011

Different roles of the human Orc6 protein in the replication initiation process.

Andreas W Thomae, Jens Baltin, Dagmar Pich, Manuel J Deutsch, Máté Ravasz, Krisztina Zeller, Manfred Gossen, Wolfgang Hammerschmidt, Aloys Schepers

Abstract read
In one paragraph

Article in Cellular and molecular life sciences : CMLS, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed, 1 pooled it
–field-weighted citation impact
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

17 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. 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
  10. Sirtuin 5 Is Regulated by the SCFMolecular and cellular biology · 2021
    Article
  11. Expansion and Functional Diversification of TFIIB-Like Factors in Plants.International journal of molecular sciences · 2021
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Regulating DNA replication in eukarya.Cold Spring Harbor perspectives in biology · 2013
    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

9 authors.

Andreas W ThomaeDepartment of Gene Vectors, Helmholtz Zentrum München, German Research Center for Environmental Health, Munich, Germany.
Jens Baltin
Dagmar Pich
Manuel J Deutsch
Máté Ravasz
Krisztina Zeller
Manfred Gossen
Wolfgang Hammerschmidt
Aloys Schepers

Funding

Genetic Analysis of EBV's Immortalizing GenesR01CA070723 · NCI · UNIVERSITY OF WISCONSIN-MADISON · PI SUGDEN, WILLIAM M. · 1996 to 2017
$4.6M
NCI NIH HHS CA70723NCI NIH HHS R01 CA070723
6 · The paper itself

Abstract

In eukaryotes, binding of the six-subunit origin recognition complex (ORC) to DNA provides an interactive platform for the sequential assembly of pre-replicative complexes. This process licenses replication origins competent for the subsequent initiation step. Here, we analyze the contribution of human Orc6, the smallest subunit of ORC, to DNA binding and pre-replicative complex formation. We show that Orc6 not only interacts with Orc1-Orc5 but also with the initiation factor Cdc6. Biochemical and imaging experiments reveal that this interaction is required for licensing DNA replication competent. Furthermore, we demonstrate that Orc6 contributes to the interaction of ORC with the chaperone protein HMGA1a (high mobility group protein A1a). Binding of human ORC to replication origins is not specified at the level of DNA sequence and the functional organization of origins is poorly understood. We have identified HMGA1a as one factor that might direct ORC to AT-rich heterochromatic regions. The systematic analysis of the interaction between ORC and HMGA1a revealed that Orc6 interacts with the acidic C-terminus of HMGA1a and also with its AT-hooks. Both domains support autonomous replication if targeted to DNA templates. As such, Orc6 functions at different stages of the replication initiation process. Orc6 can interact with ORC chaperone proteins such as HMGA1a to facilitate chromatin binding of ORC and is also an essential factor for pre-RC formation.

Indexed as

DNA ReplicationReplication OriginCell Cycle ProteinsHEK293 CellsHMGA1a ProteinHumansNuclear ProteinsOrigin Recognition ComplexProtein IsoformsProtein SubunitsCDC6 protein, humanCell Cycle ProteinsHMGA1a ProteinNuclear ProteinsORC6 protein, humanOrigin Recognition ComplexProtein IsoformsProtein Subunits

Identifiers

PMID21461783
PMCPMC11114885

What OpenQuestion holds

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Registered trials

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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.