Functional interaction of poly(ADP-ribose) with the 20S proteasome in vitro.

Abstract:

:The nuclear enzyme poly(ADP-ribosyl) transferase (pADPRT) catalyzes the formation of poly(ADP-ribose) from NAD+. Several nuclear proteins and pADPRT itself are targets for the modification by poly(ADP-ribosyl)ation. It is demonstrated here that poly(ADP-ribose) or pADPRT automodified with poly(ADP-ribose) interacts noncovalently with the 20S proteasome in vitro. The interaction of pADPRT with the 20S proteasome requires the long ADP-ribose polymers formed by automodification of the pADPRT with poly(ADP-ribose). As a result pADPRT automodified with short ADP-ribose oligomers is unable to associate with the 20S proteasome. The interaction with poly(ADP-ribose) causes a specific stimulation of the peptidase activity of the 20S proteasome. Modified pADPRT does not serve as a substrate for the degradation by the 20S proteasome. No covalent modification of the 20S proteasome by ADP-ribosylation was observed. The results may point to a functional relationship between pADPRT and the 20S proteasome in a pathway protecting the cell from oxidative damage.

authors

Mayer-Kuckuk P,Ullrich O,Ziegler M,Grune T,Schweiger M

doi

10.1006/bbrc.1999.0824

subject

Has Abstract

pub_date

1999-06-16 00:00:00

pages

576-81

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(99)90824-0

journal_volume

259

pub_type

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