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Histone shuttling by poly(ADP-ribosylation).

C A Realini¹, F R Althaus

¹Institute of Pharmacology and Biochemistry, University of Zürich-Tierspital, Switzerland.

The Journal of Biological Chemistry

|September 15, 1992

Summary

Two nuclear enzymes, poly(ADP-ribose) polymerase and poly(ADP-ribose) glycohydrolase, cooperate in a histone shuttle mechanism. This process facilitates chromatin unfolding during DNA repair by temporarily removing histones from DNA.

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Area of Science:

Molecular Biology
Biochemistry
Genetics

Background:

Nuclear enzymes play crucial roles in DNA metabolism and chromatin regulation.
Histone dynamics are essential for processes like DNA replication and repair.
Poly(ADP-ribosylation) is a post-translational modification involved in various cellular processes.

Purpose of the Study:

To investigate the cooperative function of poly(ADP-ribose) polymerase and poly(ADP-ribose) glycohydrolase.
To elucidate the mechanism of histone-DNA interaction mediated by these enzymes.
To understand the role of this enzymatic system in chromatin remodeling during DNA repair.

Main Methods:

Reconstituted in vitro system to analyze reaction intermediates.
Electrophoretic mobility assays to monitor DNA and histone complex changes.
Nuclease digestion assays to assess DNA accessibility.

Main Results:

Poly(ADP-ribose) polymerase activation leads to ADP-ribose polymer formation, attracting histones.
Histones dissociate from DNA, making it susceptible to nuclease digestion.
Poly(ADP-ribose) glycohydrolase degrades polymers, allowing histone reassociation with DNA.
The system functions as a histone shuttle, facilitating transient histone displacement.

Conclusions:

The poly(ADP-ribosylation) system acts as a catalyst for nucleosomal unfolding.
This mechanism is compatible with chromatin remodeling during DNA excision repair.
Enzymatic cooperation enables dynamic histone-DNA interactions crucial for genome stability.

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