Evidence map›Paper›PMID 20489205›Full record

ArticleThe Journal of biological chemistry2010

Solution NMR structure of the C-terminal DNA binding domain of Mcm10 reveals a conserved MCM motif.

Patrick D Robertson, Benjamin Chagot, Walter J Chazin, Brandt F Eichman

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 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.1field-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

16 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Review
  7. Review
  8. Article
  9. MCM10: one tool for all-Integrity, maintenance and damage control.Seminars in cell & developmental biology · 2014
    Review
  10. Article
  11. Article
  12. Archaeology of eukaryotic DNA replication.Cold Spring Harbor perspectives in biology · 2013
    Review
  13. Enigmatic roles of Mcm10 in DNA replication.Trends in biochemical sciences · 2013
    Review
  14. Article
  15. Review
  16. Domain structure of the DEMETER 5-methylcytosine DNA glycosylase.Proceedings of the National Academy of Sciences of the United States of America · 2010
    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

4 authors at 2 institutions in 1 country.

Patrick D RobertsonDepartment of Biological Sciences, Vanderbilt University, Nashville, Tennessee 37232, USA.
Benjamin Chagot
Walter J Chazin
Brandt F Eichman
Joint Center for Structural Genomics · USVanderbilt University · US

Funding

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
NIGMS NIH HHS GM065484NIGMS NIH HHS GM080570NIGMS NIH HHS R01 GM065484NIGMS NIH HHS R01 GM080570
6 · The paper itself

Abstract

The eukaryotic DNA replication protein Mcm10 associates with chromatin in early S-phase and is required for assembly and function of the replication fork protein machinery. Xenopus laevis (X) Mcm10 binds DNA via a highly conserved internal domain (ID) and a C-terminal domain (CTD) that is unique to higher eukaryotes. Although the structural basis of the interactions of the ID with DNA and polymerase alpha is known, little information is available for the CTD. We have identified the minimal DNA binding region of the XMcm10-CTD and determined its three-dimensional structure by solution NMR. The CTD contains a globular domain composed of two zinc binding motifs. NMR chemical shift perturbation and mutational analysis show that ssDNA binds only to the N-terminal (CCCH-type) zinc motif, whose structure is unique to Mcm10. The second (CCCC-type) zinc motif is not involved in DNA binding. However, it is structurally similar to the CCCC zinc ribbon in the N-terminal oligomerization domain of eukaryotic and archaeal MCM helicases. NMR analysis of a construct spanning both the ID and CTD reveals that the two DNA binding domains are structurally independent in solution, supporting a modular architecture for vertebrate Mcm10. Our results provide insight in the action of Mcm10 in the replisome and support a model in which it serves as a central scaffold through coupling of interactions with partner proteins and the DNA.

Indexed as

Conserved SequenceNuclear Magnetic Resonance, BiomolecularAmino Acid MotifsAmino Acid SequenceAnimalsDNADNA-Binding ProteinsHumansMiceMinichromosome Maintenance ProteinsModels, MolecularMolecular Sequence DataProtein Structure, TertiaryXenopus laevisZincDNADNA-Binding ProteinsMcm10 protein, XenopusMinichromosome Maintenance ProteinsZinc

Identifiers

PMID20489205
PMCPMC2906287
OpenAlexW2107047202

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.