Histone shuttling by poly ADP-ribosylation |
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Authors: | Felix R Althaus Liane Höfferer Hanna E Kleczkowska Maria Malanga Hanspeter Naegeli Phyllis L Panzeter Claudio A Realini |
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Institution: | (1) Institute of Pharmacology and Toxicology, University of Zürich-Tierspital, Winterthurerstrasse 260, CH-8057 Zürich, Switzerland |
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Abstract: | The enzymes poly(ADP-ribose)polymerase and poly(ADP-ribose) glycohydrolase may cooperate to drive a histone shuttle mechanism in chromatin. The mechanism is triggered by binding of the N-terminal zinc-finger domain of the polymerase to DNA strand breaks, which activates the catalytic activities residing in the C-terminal domain. The polymerase converts into a protein carrying multiple ADP-ribose polymers which displace histones from DNA by specifically targeting the histone tails responsible for DNA condensation. As a result, the domains surrounding DNA strand breaks become accessible to other proteins. Poly(ADP0ribose) glycohydrolase attacks ADP-ribose polymers in a specific order and thereby releases histones for reassociation with DNA. Increasing evidence from different model systems suggests that histone shuttling participates in DNA repairin vivo as a catalyst for nucleosomal unfolding. |
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Keywords: | poly(ADP-ribose)polymerase poly(ADP-ribose) glycohydrolase DNA repair chromatin nucleosomal unfolding NAD+ |
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