Evidence map›Paper›PMID 20335175›Full record

ArticleThe Journal of biological chemistry2010

Structure and mutagenesis studies of the C-terminal region of licensing factor Cdt1 enable the identification of key residues for binding to replicative helicase Mcm proteins.

Jungoo Jee, Takeshi Mizuno, Katsuhiko Kamada, Hidehito Tochio, Yasumasa Chiba, Ken-Ichiro Yanagi, Gentaro Yasuda, Hidekazu Hiroaki, Fumio Hanaoka, Masahiro Shirakawa

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. 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
1.5field-weighted citation impact, top 19% 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, 29 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. Mechanisms and regulation of DNA replication initiation in eukaryotes.Critical reviews in biochemistry and molecular biology · 2017
    Review
  9. The Temporal Regulation of S Phase Proteins During GAdvances in experimental medicine and biology · 2017
    Review
  10. Review
  11. Article
  12. Helicase loading at chromosomal origins of replication.Cold Spring Harbor perspectives in biology · 2013
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Prevention of DNA re-replication in eukaryotic cells.Journal of molecular cell biology · 2011
    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

10 authors at 6 institutions in 2 countries.

Jungoo JeeCenter for Priority Areas, Tokyo Metropolitan University, 1-1 Minami-Osawa, Hachioji, Tokyo 192-0397, Japan. jee-jungoo@tmu.ac.jp
Takeshi Mizuno
Katsuhiko Kamada
Hidehito Tochio
Yasumasa Chiba
Ken-Ichiro Yanagi
Gentaro Yasuda
Hidekazu Hiroaki
Fumio Hanaoka
Masahiro Shirakawa
RIKEN · JPKyoto University · JPAjinomoto (United States) · USGakushuin University · JPKobe University · JPTokyo Metropolitan University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In eukaryotes, DNA replication is fired once in a single cell cycle before cell division starts to maintain stability of the genome. This event is tightly controlled by a series of proteins. Cdt1 is one of the licensing factors and is involved in recruiting replicative DNA helicase Mcm2-7 proteins into the pre-replicative complex together with Cdc6. In Cdt1, the C-terminal region serves as a binding site for Mcm2-7 proteins, although the details of these interactions remain largely unknown. Here, we report the structure of the region and the key residues for binding to Mcm proteins. We determined the solution structure of the C-terminal fragment, residues 450-557, of mouse Cdt1 by NMR. The structure consists of a winged-helix domain and shows unexpected similarity to those of the C-terminal domain of Cdc6 and the central fragment of Cdt1, thereby implying functional and evolutionary relationships. Structure-based mutagenesis and an in vitro binding assay enabled us to pinpoint the region that interacts with Mcm proteins. Moreover, by performing in vitro binding and budding yeast viability experiments, we showed that approximately 45 residues located in the N-terminal direction of the structural region are equally crucial for recognizing Mcm proteins. Our data suggest the possibility that winged-helix domain plays a role as a common module to interact with replicative helicase in the DNA replication-licensing process.

Indexed as

AnimalsCell Cycle ProteinsDNA-Binding ProteinsDNA HelicasesMADS Domain ProteinsMiceMutagenesisNuclear Magnetic Resonance, BiomolecularNuclear ProteinsProtein BindingProtein Structure, SecondaryProtein Structure, TertiaryStructure-Activity RelationshipCDC6 protein, mouseCell Cycle ProteinsDNA-Binding ProteinsDNA HelicasesMADS Domain ProteinsNuclear ProteinsRis2 protein, mouse

Identifiers

PMID20335175
PMCPMC2871461
OpenAlexW2005381697

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.