Journal article
Histone shuttling by poly ADP-ribosylation.
- Althaus FR University of Zürich-Tierspital, Institute of Pharmacology and Toxicology, Switzerland.
- Höfferer L
- Kleczkowska HE
- Malanga M
- Naegeli H
- Panzeter PL
- Realini CA
- 1994-09-01
Published in:
- Molecular and cellular biochemistry. - 1994
Animals
DNA
Glycoside Hydrolases
Histones
Humans
Poly Adenosine Diphosphate Ribose
Poly(ADP-ribose) Polymerases
English
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.
- Language
-
- English
- Open access status
- closed
- Identifiers
-
- DOI 10.1007/bf00928443
- PMID 7898476
- Persistent URL
- https://sonar.ch/global/documents/185548
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