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- W2126338081 abstract "In human cells appropriate mono-methylation of histone H4 lysine20 by PrSet7/SET8 is important for the correct transcription of specific genes, and timely progression through the cell cycle. Over-methylation appears to be prevented through the interaction of PrSet7 with PCNA, which targets PrSet7 destruction via the CRL4cdt2 pathway, however the factors involved in positive regulation of its histone methylation remain undefined. Here we present biochemical and genetic evidence for a previously undocumented interaction between dPrSet7 and DNA polymerase-alpha in Drosophila. Depletion of the polymerase reduces H4K20 mono-methylation suggesting that it is required for the expression of dPrSet7 histone methylation activity. We also show that the interaction between PCNA and PrSet7 is conserved in Drosophila, but is only detectable in chromatin fractions. Consistent with this, S2 cells show a significant loss of chromatin bound dPrSet7 protein as S phase progresses. Based on these data we suggest that interaction with the DNA polymerase represents an important route for the expression of PrSet7 histone methylase activity, by allowing loading of dPrSet7 onto chromatin or its subsequent activation." @default.
- W2126338081 created "2016-06-24" @default.
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- W2126338081 date "2014-01-01" @default.
- W2126338081 modified "2023-10-16" @default.
- W2126338081 title "DNA polymerase alpha interacts with PrSet7 and mediates H4K20 monomethylation in Drosophila" @default.
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- W2126338081 doi "https://doi.org/10.1242/jcs.144501" @default.
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