ArticleThe Journal of biological chemistry2008
Domain architecture and biochemical characterization of vertebrate Mcm10.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed, 56 citations in OpenAlex.
- Multifaceted role of the DNA replication protein MCM10 in maintaining genome stability and its implication in human diseases.Cancer metastasis reviews · 2024Review
- Unwinding of a eukaryotic origin of replication visualized by cryo-EM.Nature structural & molecular biology · 2024Article
- XYLEM CYSTEINE PEPTIDASE 1 and its inhibitor CYSTATIN 6 regulate pattern-triggered immunity by modulating the stability of the NADPH oxidase RESPIRATORY BURST OXIDASE HOMOLOG D.The Plant cell · 2024Article
- Mechanism of eukaryotic origin unwinding is a dual helicase DNA shearing process.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Review
- Von Willebrand Factor Facilitates Intravascular Dissemination of MicrosporidiaFrontiers in cellular and infection microbiology · 2021Article
- The anti-parasitic agent suramin and several of its analogues are inhibitors of the DNA binding protein Mcm10.Open biology · 2019Article
- When proteins play tag: the dynamic nature of the replisome.Biophysical reviews · 2019Review
- Fine-tuning of the replisome: Mcm10 regulates fork progression and regression.Cell cycle (Georgetown, Tex.) · 2019Review
- Role of Cdc23/Mcm10 in generating the ribonucleotide imprint at the mat1 locus in fission yeast.Nucleic acids research · 2019Article
- Mcm10 has potent strand-annealing activity and limits translocase-mediated fork regression.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- The mechanism of eukaryotic CMG helicase activation.Nature · 2018Article
- Mcm10 promotes rapid isomerization of CMG-DNA for replisome bypass of lagging strand DNA blocks.eLife · 2017Article
- The Mcm2-7-interacting domain of human mini-chromosome maintenance 10 (Mcm10) protein is important for stable chromatin association and origin firing.The Journal of biological chemistry · 2017Article
- An intact Mcm10 coiled-coil interaction surface is important for origin melting, helicase assembly and the recruitment of Pol-α to Mcm2-7.Nucleic acids research · 2017Article
- Review
- An Mcm10 Mutant Defective in ssDNA Binding Shows Defects in DNA Replication Initiation.Journal of molecular biology · 2016Article
- Recruitment of Mcm10 to Sites of Replication Initiation Requires Direct Binding to the Minichromosome Maintenance (MCM) Complex.The Journal of biological chemistry · 2016Article
- Mcm10 coordinates the timely assembly and activation of the replication fork helicase.Nucleic acids research · 2016Article
- Cell-Cycle-Regulated Interaction between Mcm10 and Double Hexameric Mcm2-7 Is Required for Helicase Splitting and Activation during S Phase.Cell reports · 2015Article
Corrections and comments
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Authors and funding
10 authors at 3 institutions in 1 country.
Funding
Abstract
Mcm10 plays a key role in initiation and elongation of eukaryotic chromosomal DNA replication. As a first step to better understand the structure and function of vertebrate Mcm10, we have determined the structural architecture of Xenopus laevis Mcm10 (xMcm10) and characterized each domain biochemically. Limited proteolytic digestion of the full-length protein revealed N-terminal-, internal (ID)-, and C-terminal (CTD)-structured domains. Analytical ultracentrifugation revealed that xMcm10 self-associates and that the N-terminal domain forms homodimeric assemblies. DNA binding activity of xMcm10 was mapped to the ID and CTD, each of which binds to single- and double-stranded DNA with low micromolar affinity. The structural integrity of xMcm10-ID and CTD is dependent on the presence of bound zinc, which was experimentally verified by atomic absorption spectroscopy and proteolysis protection assays. The ID and CTD also bind independently to the N-terminal 323 residues of the p180 subunit of DNA polymerase alpha-primase. We propose that the modularity of the protein architecture, with discrete domains for dimerization and for binding to DNA and DNA polymerase alpha-primase, provides an effective means for coordinating the biochemical activities of Mcm10 within the replisome.
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Registered trials
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.