Evidence map›Paper›PMID 23894664›Full record

ArticlePloS one2013

Mcm10 self-association is mediated by an N-terminal coiled-coil domain.

Wenyue Du, Ajeetha Josephrajan, Suraj Adhikary, Timothy Bowles, Anja-Katrin Bielinsky, Brandt F Eichman

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.0field-weighted citation impact, top 24% 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

13 citing papers in PubMed, 18 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Mcm10 has potent strand-annealing activity and limits translocase-mediated fork regression.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Crystal structures of MBP fusion proteins.Protein science : a publication of the Protein Society · 2016
    Review
  11. Article
  12. MCM10: one tool for all-Integrity, maintenance and damage control.Seminars in cell & developmental biology · 2014
    Review
  13. 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 2 institutions in 1 country.

Wenyue DuDepartment of Biological Sciences, Vanderbilt University, Nashville, Tennessee, USA.
Ajeetha Josephrajan
Suraj Adhikary
Timothy Bowles
Anja-Katrin Bielinsky
Brandt F Eichman
Vanderbilt University · USUniversity of Minnesota · US

Funding

Understanding the biological function of Mcm10 in yeastR01GM074917 · NIGMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI BIELINSKY, ANJA-KATRIN · 2005 to 2019
$3.7M
Structural mechanisms of Mcm10 in DNA replicationR01GM080570 · NIGMS · VANDERBILT UNIVERSITY · PI EICHMAN, BRANDT F · 2007 to 2010
$1.1M
NIGMS NIH HHS R01 GM074917NIGMS NIH HHS R01 GM080570
6 · The paper itself

Abstract

Minichromosome maintenance protein 10 (Mcm10) is an essential eukaryotic DNA-binding replication factor thought to serve as a scaffold to coordinate enzymatic activities within the replisome. Mcm10 appears to function as an oligomer rather than in its monomeric form (or rather than as a monomer). However, various orthologs have been found to contain 1, 2, 3, 4, or 6 subunits and thus, this issue has remained controversial. Here, we show that self-association of Xenopus laevis Mcm10 is mediated by a conserved coiled-coil (CC) motif within the N-terminal domain (NTD). Crystallographic analysis of the CC at 2.4 Å resolution revealed a three-helix bundle, consistent with the formation of both dimeric and trimeric Mcm10 CCs in solution. Mutation of the side chains at the subunit interface disrupted in vitro dimerization of both the CC and the NTD as monitored by analytical ultracentrifugation. In addition, the same mutations also impeded self-interaction of the full-length protein in vivo, as measured by yeast-two hybrid assays. We conclude that Mcm10 likely forms dimers or trimers to promote its diverse functions during DNA replication.

Indexed as

Models, MolecularAmino Acid SequenceAnimalsDNA ReplicationMinichromosome Maintenance ProteinsMutationProtein MultimerizationProtein Structure, TertiarySequence AlignmentXenopus laevisMcm10 protein, XenopusMinichromosome Maintenance Proteins

Identifiers

PMID23894664
PMCPMC3720919
OpenAlexW2066983187

What OpenQuestion holds

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LicenceCC BY
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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.