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Histone shuttle driven by the automodification cycle of poly(ADP-ribose)polymerase.
- Source :
-
Environmental and molecular mutagenesis [Environ Mol Mutagen] 1993; Vol. 22 (4), pp. 278-82. - Publication Year :
- 1993
-
Abstract
- In mammalian cells, the incision step of DNA excision repair triggers a dramatic metabolic response in chromatin. The reaction starts with the binding of a zinc-finger protein, i.e. poly(ADP-ribose)polymerase to DNA nicks, activation of four resident catalytic activities leading to poly(ADP-ribose) synthesis, conversion of the polymerase into a protein modified with up to 28 variably sized ADP-ribose polymers, and rapid degradation of polymerase-bound polymers by poly(ADP-ribose)glycohydrolase. This automodification cycle catalyzes a transient and reversible dissociation of histones from DNA. Shuttling of histones on the DNA allows selected other proteins, such as DNA helicase A and topoisomerase I, to gain access to DNA. Histone shuttling in vitro mimics nucleosomal unfolding/refolding in vivo that accompanies the postincisional steps of DNA excision repair. Suppression of the automodification cycle in mammalian cells prevents nucleosomal unfolding and nucleotide excision repair.
Details
- Language :
- English
- ISSN :
- 0893-6692
- Volume :
- 22
- Issue :
- 4
- Database :
- MEDLINE
- Journal :
- Environmental and molecular mutagenesis
- Publication Type :
- Academic Journal
- Accession number :
- 8223511
- Full Text :
- https://doi.org/10.1002/em.2850220417