Abstract
The access to DNA within nucleosomes is greatly restricted for most enzymes and trans-acting factors that bind DNA. We report here that human DNA ligase I, which carries out the final step of Okazaki fragment processing and of many DNA repair pathways, can access DNA that is wrapped about the surface of a nucleosome in vitro and carry out its enzymatic function with high efficiency. In addition, we find that ligase activity is not affected by the binding of linker histone (H1) but is greatly influenced by the disposition of the core histone tail domains. These results suggest that the window of opportunity for human DNA ligase I may extend well beyond the first stages of chromatin reassembly after DNA replication or repair.
Original language | English (US) |
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Pages (from-to) | 5492-5501 |
Number of pages | 10 |
Journal | EMBO Journal |
Volume | 19 |
Issue number | 20 |
DOIs | |
State | Published - Oct 16 2000 |
Externally published | Yes |
Keywords
- Chromatin
- Gene regulation
- Human DNA ligase
- Nucleosome
ASJC Scopus subject areas
- General Neuroscience
- Molecular Biology
- General Biochemistry, Genetics and Molecular Biology
- General Immunology and Microbiology