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Histone shuttle driven by the automodification cycle of poly(ADP‐ribose) polymerase
Author(s) -
Althaus Felix R.,
Höfferer Liane,
Kleczkowska Hanna E.,
Malanga Maria,
Naegeli Hanspeter,
Panzeter Phyllis,
Realini Claudio
Publication year - 1993
Publication title -
environmental and molecular mutagenesis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1
H-Index - 87
eISSN - 1098-2280
pISSN - 0893-6692
DOI - 10.1002/em.2850220417
Subject(s) - polymerase , poly adp ribose polymerase , histone , dna repair , chromatin , dna polymerase , microbiology and biotechnology , histone h2a , dna , biology , biochemistry , nucleotide excision repair , helicase , proliferating cell nuclear antigen , dna clamp , chemistry , gene , rna , reverse transcriptase
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. © 1993 Wiley‐Liss, Inc.