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Human DNA ligase I efficiently seals nicks in nucleosomes
Author(s) -
Chafin David R.,
Vitolo Joseph M.,
Henricksen Leigh A.,
Bambara Robert A.,
Hayes Jeffrey J.
Publication year - 2000
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/19.20.5492
Subject(s) - dna ligase , biology , okazaki fragments , dna ligases , nucleosome , chromatin , histone , dna , microbiology and biotechnology , dna replication , ubiquitin ligase , dna clamp , linker dna , eukaryotic dna replication , biochemistry , ubiquitin , gene , reverse transcriptase , rna
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.