ArticleThe Journal of biological chemistry2015
DNA induces conformational changes in a recombinant human minichromosome maintenance complex.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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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.
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Who cites it
5 citing papers in PubMed, 9 citations in OpenAlex.
- Cryo-EM structure of human hexameric MCM2-7 complex.iScience · 2022Article
- Structure of an octameric form of the minichromosome maintenance protein from the archaeon Pyrococcus abyssi.Scientific reports · 2017Article
- Molecular architecture of the recombinant human MCM2-7 helicase in complex with nucleotides and DNA.Cell cycle (Georgetown, Tex.) · 2016Article
- An introduction to sample preparation and imaging by cryo-electron microscopy for structural biology.Methods (San Diego, Calif.) · 2016Article
- Structure of the eukaryotic MCM complex at 3.8 Å.Nature · 2015Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
ATP-dependent DNA unwinding activity has been demonstrated for recombinant archaeal homohexameric minichromosome maintenance (MCM) complexes and their yeast heterohexameric counterparts, but in higher eukaryotes such as Drosophila, MCM-associated DNA helicase activity has been observed only in the context of a co-purified Cdc45-MCM-GINS complex. Here, we describe the production of the recombinant human MCM (hMCM) complex in Escherichia coli. This protein displays ATP hydrolysis activity and is capable of unwinding duplex DNA. Using single-particle asymmetric EM reconstruction, we demonstrate that recombinant hMCM forms a hexamer that undergoes a conformational change when bound to DNA. Recombinant hMCM produced without post-translational modifications is functional in vitro and provides an important tool for biochemical reconstitution of the human replicative helicase.
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Registered trials
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