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PMID: 7898476 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Review

Histone shuttling by poly ADP-ribosylation.

Molecular and cellular biochemistry ·Vol. 138 ·No. 1-2 ·1994-09-00 ·Pages 53-9

Althaus FR, Höfferer L, Kleczkowska HE, Malanga M, Naegeli H, Panzeter PL, Realini CA

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.

MeSH Terms
Animals DNA/metabolism Glycoside Hydrolases/metabolism Histones/metabolism Humans Poly Adenosine Diphosphate Ribose/metabolism Poly(ADP-ribose) Polymerases/metabolism
Chemicals
Histones Poly Adenosine Diphosphate Ribose DNA Poly(ADP-ribose) Polymerases Glycoside Hydrolases poly ADP-ribose glycohydrolase
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
Althaus F R
University of Zürich-Tierspital, Institute of Pharmacology and Toxicology, Switzerland.
Höfferer L
Kleczkowska H E
Malanga M
Naegeli H
Panzeter P L
Realini C A
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Article Info
Journal
Molecular and cellular biochemistry
Abbr.
Mol Cell Biochem
ISSN
0300-8177
Published
1994-09-00
Pages
53-9
Language
English
Region
Netherlands
NLM ID
0364456
Subset
IM
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