| Autor: |
Evrin, Cecile, Maman, Joseph D, Diamante, Aurora, Pellegrini, Luca, Labib, Karim |
| Přispěvatelé: |
Pellegrini, Luca [0000-0002-9300-497X], Labib, Karim [0000-0001-8861-379X], Apollo - University of Cambridge Repository |
| Rok vydání: |
2018 |
| Předmět: |
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| DOI: |
10.17863/cam.33156 |
| Popis: |
The eukaryotic replisome disassembles parental chromatin at DNA replication forks, but then plays a poorly understood role in the re-deposition of the displaced histone complexes onto nascent DNA. Here, we show that yeast DNA polymerase α contains a histone-binding motif that is conserved in human Pol α and is specific for histones H2A and H2B. Mutation of this motif in budding yeast cells does not affect DNA synthesis, but instead abrogates gene silencing at telomeres and mating-type loci. Similar phenotypes are produced not only by mutations that displace Pol α from the replisome, but also by mutation of the previously identified histone-binding motif in the CMG helicase subunit Mcm2, the human orthologue of which was shown to bind to histones H3 and H4. We show that chromatin-derived histone complexes can be bound simultaneously by Mcm2, Pol α and the histone chaperone FACT that is also a replisome component. These findings indicate that replisome assembly unites multiple histone-binding activities, which jointly process parental histones to help preserve silent chromatin during the process of chromosome duplication. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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