Evidence map›Paper›PMID 19081065›Full record

ArticleStructure (London, England : 1993)2008

Structural basis for DNA binding by replication initiator Mcm10.

Eric M Warren, Sivaraja Vaithiyalingam, Justin Haworth, Briana Greer, Anja-Katrin Bielinsky, Walter J Chazin, Brandt F Eichman

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

43 citing papers in PubMed, 62 citations in OpenAlex.

  1. Article
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  5. Mechanism of eukaryotic origin unwinding is a dual helicase DNA shearing process.Proceedings of the National Academy of Sciences of the United States of America · 2023
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  12. Review
  13. 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
  14. Article
  15. Article
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  18. Review
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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

7 authors at 2 institutions in 1 country.

Eric M WarrenDepartment of Biological Sciences, Vanderbilt University, Nashville, TN 37232, USA.
Sivaraja Vaithiyalingam
Justin Haworth
Briana Greer
Anja-Katrin Bielinsky
Walter J Chazin
Brandt F Eichman
Vanderbilt University · USUniversity of Minnesota · US

Funding

Structural Biology Facility CoreP30ES000267 · NIEHS · VANDERBILT UNIVERSITY · PI GUENGERICH, F PETER · 1985 to 2014
$20.3M
MOLECULAR BIOPHYSICS TRAINING PROGRAM AT VANDERBILTT32GM008320 · NIGMS · VANDERBILT UNIVERSITY · PI CHAZIN, WALTER J. · 1989 to 2023
$7.9M
Structural Basis for RPA Functions in DNA ProcessingR01GM065484 · NIGMS · VANDERBILT UNIVERSITY · PI CHAZIN, WALTER J. · 2003 to 2015
$3.9M
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
NIEHS NIH HHS P30 ES000267NIGMS NIH HHS R01 GM065484NIGMS NIH HHS R01 GM074917NIGMS NIH HHS R01 GM080570NIGMS NIH HHS T32 GM008320
6 · The paper itself

Abstract

Mcm10 is an essential eukaryotic DNA replication protein required for assembly and progression of the replication fork. The highly conserved internal domain (Mcm10-ID) has been shown to physically interact with single-stranded (ss) DNA, DNA polymerase alpha, and proliferating cell nuclear antigen (PCNA). The crystal structure of Xenopus laevis Mcm10-ID presented here reveals a DNA binding architecture composed of an oligonucleotide/oligosaccharide-fold followed in tandem by a variant and highly basic zinc finger. NMR chemical shift perturbation and mutational studies of DNA binding activity in vitro reveal how Mcm10 uses this unique surface to engage ssDNA. Corresponding mutations in Saccharomyces cerevisiae result in increased sensitivity to replication stress, demonstrating the functional importance of DNA binding by this region of Mcm10 to replication. In addition, mapping Mcm10 mutations known to disrupt PCNA, polymerase alpha, and DNA interactions onto the crystal structure provides insight into how Mcm10 might coordinate protein and DNA binding within the replisome.

Indexed as

DNA ReplicationAmino Acid MotifsAmino Acid SequenceAnimalsBinding SitesBiophysical PhenomenaDNADNA-Binding ProteinsDNA Mutational AnalysisDNA Polymerase IMinichromosome Maintenance ProteinsModels, BiologicalModels, MolecularMolecular Sequence DataMutationNuclear Magnetic Resonance, BiomolecularDNADNA-Binding ProteinsDNA Polymerase IMcm10 protein, XenopusMinichromosome Maintenance ProteinsProliferating Cell Nuclear AntigenSaccharomyces cerevisiae Proteins

Identifiers

PMID19081065
PMCPMC2636851
OpenAlexW2165914686

What OpenQuestion holds

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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.