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Article

Dpb4 promotes resection of DNA double-strand breaks and checkpoint activation by acting in two different protein complexes.

Nature communications - 6 Aug 2021

Casari Erika, Gobbini Elisa, Gnugnoli Marco, Mangiagalli Marco, Clerici Michela, Longhese Maria Pia

Abstract excerpt

Budding yeast Dpb4 (POLE3/CHRAC17 in mammals) is a highly conserved histone fold protein that is shared by two protein complexes: the chromatin remodeler ISW2/hCHRAC and the DNA polymerase ε (Pol ε) holoenzyme. In Saccharomyces cerevisiae, Dpb4 forms histone-like dimers with Dls1 in the ISW2 complex and with Dpb3 in the Pol ε complex. Here, we show that Dpb4 plays two functions in sensing and processing DNA...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 34362907
DOI: 10.1038/s41467-021-25090-9
PMCID: PMC8346560

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026.

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