Mcm10 Self-Association Is Mediated by an N-Terminal Coiled-Coil Domain
| Autor: | Ajeetha Josephrajan, Timothy M. Bowles, Anja Katrin Bielinsky, Suraj Adhikary, Brandt F. Eichman, Wenyue Du |
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| Jazyk: | angličtina |
| Rok vydání: | 2013 |
| Předmět: |
Macromolecular Assemblies
DNA Replication Models Molecular Protein subunit Xenopus Biophysics lcsh:Medicine Oligomer Biochemistry 03 medical and health sciences chemistry.chemical_compound Xenopus laevis 0302 clinical medicine Molecular cell biology Minichromosome maintenance DNA-binding proteins Animals Amino Acid Sequence lcsh:Science Biology 030304 developmental biology Coiled coil 0303 health sciences Multidisciplinary biology Minichromosome Maintenance Proteins lcsh:R DNA replication Proteins Protein interactions DNA biology.organism_classification Molecular biology Protein Structure Tertiary Nucleic acids chemistry Mutation MCM10 Protein structure Replisome lcsh:Q Protein Multimerization Sequence Alignment 030217 neurology & neurosurgery Research Article Structural proteins |
| Zdroj: | PLoS ONE PLoS ONE, Vol 8, Iss 7, p e70518 (2013) |
| ISSN: | 1932-6203 |
| Popis: | Minichromosome maintenance protein 10 (Mcm10) is an essential eukaryotic DNA-binding replication factor thought to serve as a scaffold to coordinate enzymatic activities within the replisome. Mcm10 appears to function as an oligomer rather than in its monomeric form (or rather than as a monomer). However, various orthologs have been found to contain 1, 2, 3, 4, or 6 subunits and thus, this issue has remained controversial. Here, we show that self-association of Xenopus laevis Mcm10 is mediated by a conserved coiled-coil (CC) motif within the N-terminal domain (NTD). Crystallographic analysis of the CC at 2.4 Å resolution revealed a three-helix bundle, consistent with the formation of both dimeric and trimeric Mcm10 CCs in solution. Mutation of the side chains at the subunit interface disrupted in vitro dimerization of both the CC and the NTD as monitored by analytical ultracentrifugation. In addition, the same mutations also impeded self-interaction of the full-length protein in vivo, as measured by yeast-two hybrid assays. We conclude that Mcm10 likely forms dimers or trimers to promote its diverse functions during DNA replication. |
| Databáze: | OpenAIRE |
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