Evidence map›Paper›PMID 18660534›Full record

ArticleGenetics2008

Functional conservation of beta-hairpin DNA binding domains in the Mcm protein of Methanobacterium thermoautotrophicum and the Mcm5 protein of Saccharomyces cerevisiae.

Ronald P Leon, Marianne Tecklenburg, Robert A Sclafani

Open access · bronzeAbstract read
In one paragraph

Article in Genetics, 2008. 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
0.7field-weighted citation impact, top 31% 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, 27 citations in OpenAlex.

  1. Article
  2. Article
  3. Cryo-EM structure of Mcm2-7 double hexamer on DNA suggests a lagging-strand DNA extrusion model.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  4. Mechanisms and regulation of DNA replication initiation in eukaryotes.Critical reviews in biochemistry and molecular biology · 2017
    Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Insights into the MCM functional mechanism: lessons learned from the archaeal MCM complex.Critical reviews in biochemistry and molecular biology · 2010
    Review
  13. The Mcm complex: unwinding the mechanism of a replicative helicase.Microbiology and molecular biology reviews : MMBR · 2009
    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

3 authors at 1 institution in 1 country.

Ronald P LeonDepartment of Biochemistry and Molecular Genetics, School of Medicine, University of Colorado, Denver, Colorado 80045, USA.
Marianne Tecklenburg
Robert A Sclafani
University of Colorado Denver · US

Funding

University of Colorado Cancer Center Support Grant - Lung Cancer Patient-Derived Xenografts with Autologous Human Immune SystemsP30CA046934 · NCI · UNIVERSITY OF COLORADO DENVER · PI James V Degregori · 1988 to 2026
$117.0M
GENETIC &MOLECULAR ANALYSIS OF YEAST DNA REPLICATIONR01GM035078 · NIGMS · UNIVERSITY OF COLORADO DENVER · PI SCLAFANI, ROBERT A · 1985 to 2012
$3.4M
Analyzing the roles of Cdc7 and Mcm5 in DNA replicationF31GM070403 · NIGMS · UNIVERSITY OF COLORADO DENVER · PI LEON, RONALD P · 2003 to 2006
$99k
NCI NIH HHS P30 CA046934NIGMS NIH HHS F31 GM070403NIGMS NIH HHS GM-070403NIGMS NIH HHS GM-35078NIGMS NIH HHS R01 GM035078
6 · The paper itself

Abstract

Mcm proteins are an important family of evolutionarily conserved helicases required for DNA replication in eukaryotes. The eukaryotic Mcm complex consists of six paralogs that form a heterohexameric ring. Because the intact Mcm2-7 hexamer is inactive in vitro, it has been difficult to determine the precise function of the different subunits. The solved atomic structure of an archaeal minichromosome maintenance (MCM) homolog provides insight into the function of eukaryotic Mcm proteins. The N-terminal positively charged central channel in the archaeal molecule consists of beta-hairpin domains essential for DNA binding in vitro. Eukaryotic Mcm proteins also have beta-hairpin domains, but their function is unknown. With the archaeal atomic structure as a guide, yeast molecular genetics was used to query the function of the beta-hairpin domains in vivo. A yeast mcm5 mutant with beta-hairpin mutations displays defects in the G1/S transition of the cell cycle, the initiation phase of DNA replication, and in the binding of the entire Mcm2-7 complex to replication origins. A similar mcm4 mutation is synthetically lethal with the mcm5 mutation. Therefore, in addition to its known regulatory role, Mcm5 protein has a positive role in origin binding, which requires coordination by all six Mcm2-7 subunits in the hexamer.

Indexed as

Amino Acid MotifsAmino Acid SequenceArchaeal ProteinsBinding SitesCell Cycle ProteinsConserved SequenceDNADNA-Binding ProteinsDNA HelicasesModels, MolecularMolecular Sequence DataMutationProtein Structure, SecondaryProtein Structure, TertiarySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsArchaeal ProteinsCell Cycle ProteinsDNADNA-Binding ProteinsDNA HelicasesMCM5 protein, S cerevisiaeMCM protein, Methanobacterium thermoautotrophicumSaccharomyces cerevisiae Proteins

Identifiers

PMID18660534
PMCPMC2516056
OpenAlexW2046606987

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.