Evidence map›Paper›PMID 19608746›Full record

ArticleThe Journal of biological chemistry2009

Physical interactions between Mcm10, DNA, and DNA polymerase alpha.

Eric M Warren, Hao Huang, Ellen Fanning, Walter J Chazin, Brandt F Eichman

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

38 citing papers in PubMed, 64 citations in OpenAlex.

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  17. 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
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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

5 authors at 1 institution in 1 country.

Eric M WarrenDepartment of Biological Sciences, Vanderbilt University, Nashville, Tennessee 37232, USA.
Hao Huang
Ellen Fanning
Walter J Chazin
Brandt F Eichman
Vanderbilt University · US

Funding

Tumor Immunology and Microenvironment Research ProgramP30CA068485 · NCI · VANDERBILT UNIVERSITY MEDICAL CENTER · PI STACIE B DUSETZINA · 1995 to 2026
$172.8M
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
CONTROL OF SIMIAN VIRUS 40 AND CELLULAR DNA REPLICATIONR01GM052948 · NIGMS · VANDERBILT UNIVERSITY · PI FRIEDMAN, KATHERINE LOUISE · 1995 to 2013
$6.1M
Structural Basis for RPA Functions in DNA ProcessingR01GM065484 · NIGMS · VANDERBILT UNIVERSITY · PI CHAZIN, WALTER J. · 2003 to 2015
$3.9M
Structural mechanisms of Mcm10 in DNA replicationR01GM080570 · NIGMS · VANDERBILT UNIVERSITY · PI EICHMAN, BRANDT F · 2007 to 2010
$1.1M
NCI NIH HHS P30 CA068485NIEHS NIH HHS P30 ES000267NIGMS NIH HHS R01 GM052948NIGMS NIH HHS R01 GM065484NIGMS NIH HHS R01 GM080570NIGMS NIH HHS R01 GM52948NIGMS NIH HHS R01 GM65484NIGMS NIH HHS T32 GM008320NIGMS NIH HHS T32 GM08320
6 · The paper itself

Abstract

Mcm10 is an essential eukaryotic protein required for the initiation and elongation phases of chromosomal replication. Specifically, Mcm10 is required for the association of several replication proteins, including DNA polymerase alpha (pol alpha), with chromatin. We showed previously that the internal (ID) and C-terminal (CTD) domains of Mcm10 physically interact with both single-stranded (ss) DNA and the catalytic p180 subunit of pol alpha. However, the mechanism by which Mcm10 interacts with pol alpha on and off DNA is unclear. As a first step toward understanding the structural details for these critical intermolecular interactions, x-ray crystallography and NMR spectroscopy were used to map the binary interfaces between Mcm10-ID, ssDNA, and p180. The crystal structure of an Mcm10-ID*ssDNA complex confirmed and extended our previous evidence that ssDNA binds within the oligonucleotide/oligosaccharide binding-fold cleft of Mcm10-ID. We show using NMR chemical shift perturbation and fluorescence spectroscopy that p180 also binds to the OB-fold and that ssDNA and p180 compete for binding to this motif. In addition, we map a minimal Mcm10 binding site on p180 to a small region within the p180 N-terminal domain (residues 286-310). These findings, together with data for DNA and p180 binding to an Mcm10 construct that contains both the ID and CTD, provide the first mechanistic insight into how Mcm10 might use a handoff mechanism to load and stabilize pol alpha within the replication fork.

Indexed as

Amino Acid MotifsBinding SitesCell Cycle ProteinsCrystallography, X-RayDNA Polymerase IDNA, Single-StrandedHumansMinichromosome Maintenance ProteinsNuclear Magnetic Resonance, BiomolecularProtein BindingCell Cycle ProteinsDNA Polymerase IDNA, Single-StrandedMCM10 protein, humanMinichromosome Maintenance Proteins

Identifiers

PMID19608746
PMCPMC2782055
OpenAlexW2129585221

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.