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  • Title: Histone shuttling by poly ADP-ribosylation.
    Author: Althaus FR, Höfferer L, Kleczkowska HE, Malanga M, Naegeli H, Panzeter PL, Realini CA.
    Journal: Mol Cell Biochem; 1994 Sep; 138(1-2):53-9. PubMed ID: 7898476.
    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(ADP-ribose)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 repair in vivo as a catalyst for nucleosomal unfolding.
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