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Interactions of poly(ADP-ribose) with nuclear proteins
F R Althaus1, S Bachmann, L Höfferer
1University of Zürich-Tierspital, Institute of Pharmacology and Toxicology, Switzerland.
Biochimie
|January 1, 1995
Summary
Poly(ADP-ribosyl)ation non-covalently binds histones, modulating DNA repair. Polymer size and branching dictate binding specificity, explaining histone shuttle mechanisms in DNA excision repair.
Area of Science:
- Molecular Biology
- Biochemistry
- Genetics
Background:
- The role of poly(ADP-ribosyl)ation in DNA repair is not fully understood.
- Current models emphasize covalent modification of target proteins.
Purpose of the Study:
- Investigate non-covalent interactions of ADP-ribose polymers with nuclear proteins.
- Determine the role of these interactions in DNA excision repair.
Main Methods:
- Studied non-covalent binding of ADP-ribose polymers to nuclear proteins, focusing on histones.
- Analyzed the influence of polymer size and branching on binding affinity.
Main Results:
- ADP-ribose polymers exhibit specific, strong non-covalent interactions with histones.
- Binding affinity is dependent on polymer size and branching.
- These interactions explain the specificity of the histone shuttle mechanism.
Conclusions:
- Non-covalent interactions, not just covalent modification, are crucial for poly(ADP-ribosyl)ation in DNA repair.
- Polymer characteristics regulate histone targeting during DNA repair in mammalian cells.