Evidence map›Paper›PMID 18662997›Full record

ArticleMolecular and cellular biology2008

Subunit organization of Mcm2-7 and the unequal role of active sites in ATP hydrolysis and viability.

Matthew L Bochman, Stephen P Bell, Anthony Schwacha

Abstract read
In one paragraph

Article in Molecular and cellular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 80 papers.

0numbers the graph read from it
0cells of the map it votes in
80citing papers in PubMed
–field-weighted citation impact
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

80 citing papers in PubMed.

  1. MCM8-9 helicase activity protects primordial germ cell development to prevent premature ovarian insufficiency.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
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  10. Review
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  12. CMG helicase can use ATPγS to unwind DNA: Implications for the rate-limiting step in the reaction mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  13. Mechanisms of hexameric helicases.Critical reviews in biochemistry and molecular biology · 2021
    Review
  14. Article
  15. Review
  16. Article
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  18. Article
  19. Article
  20. Article

20 more citing papers are in PubMed but not listed here.

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.

Matthew L BochmanDepartment of Biological Sciences, University of Pittsburgh, Pittsburgh, Pennsylvania 15260, USA.
Stephen P Bell
Anthony Schwacha

Funding

MCM PROTEIN FUNCTION DURING EUKARYOTIC DNA REPLICATIONR01GM058701 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI BELL, STEPHEN P. · 1999 to 2002
$562k
Howard Hughes Medical InstituteNIGMS NIH HHS GM58701
6 · The paper itself

Abstract

The Mcm2-7 (minichromosome maintenance) complex is a toroidal AAA(+) ATPase and the putative eukaryotic replicative helicase. Unlike a typical homohexameric helicase, Mcm2-7 contains six distinct, essential, and evolutionarily conserved subunits. Precedence to other AAA(+) proteins suggests that Mcm ATPase active sites are formed combinatorially, with Walker A and B motifs contributed by one subunit and a catalytically essential arginine (arginine finger) contributed by the adjacent subunit. To test this prediction, we used copurification experiments to identify five distinct and stable Mcm dimer combinations as potential active sites; these subunit associations predict the architecture of the Mcm2-7 complex. Through the use of mutant subunits, we establish that at least three sites are active for ATP hydrolysis and have a canonical AAA(+) configuration. In isolation, these five active-site dimers have a wide range of ATPase activities. Using Walker B and arginine finger mutations in defined Mcm subunits, we demonstrate that these sites similarly make differential contributions toward viability and ATP hydrolysis within the intact hexamer. Our conclusions predict a structural discontinuity between Mcm2 and Mcm5 and demonstrate that in contrast to other hexameric helicases, the six Mcm2-7 active sites are functionally distinct.

Indexed as

Adenosine TriphosphateAmino Acid MotifsBinding SitesCell Cycle ProteinsChromosomal Proteins, Non-HistoneDimerizationDNA HelicasesFungal ProteinsMultienzyme ComplexesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAdenosine TriphosphateCell Cycle ProteinsChromosomal Proteins, Non-HistoneDNA HelicasesFungal ProteinsMCM2 protein, S cerevisiaeMCM5 protein, humanMultienzyme ComplexesSaccharomyces cerevisiae Proteins

Identifiers

PMID18662997
PMCPMC2547011

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.