ArticleScientific reports2017
Structure of an octameric form of the minichromosome maintenance protein from the archaeon Pyrococcus abyssi.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed, 6 citations in OpenAlex.
- Assembly of a homohexameric minichromosome maintenance complex is dependent on ATP and DNA.The Journal of biological chemistry · 2026Article
- Cryo-EM structure of AAA + ATPase thorase reveals novel helical filament formation.Computational and structural biotechnology journal · 2025Article
- Potential Prospective Biomarkers for Non-small Cell Lung Cancer: Mini-Chromosome Maintenance Proteins.Frontiers in genetics · 2021Article
- The AAA + ATPase TorsinA polymerizes into hollow helical tubes with 8.5 subunits per turn.Nature communications · 2019Article
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
Cell division is a complex process that requires precise duplication of genetic material. Duplication is concerted by replisomes. The Minichromosome Maintenance (MCM) replicative helicase is a crucial component of replisomes. Eukaryotic and archaeal MCM proteins are highly conserved. In fact, archaeal MCMs are powerful tools for elucidating essential features of MCM function. However, while eukaryotic MCM2-7 is a heterocomplex made of different polypeptide chains, the MCM complexes of many Archaea form homohexamers from a single gene product. Moreover, some archaeal MCMs are polymorphic, and both hexameric and heptameric architectures have been reported for the same polypeptide. Here, we present the structure of the archaeal MCM helicase from Pyrococcus abyssi in its single octameric ring assembly. To our knowledge, this is the first report of a full-length octameric MCM helicase.
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