Functional Interaction of Poly(ADP-ribose) with the 20S Proteasome in Vitro

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• 作者：Mayer-Kuckuk ; Philipp ; Ullrich ; Oliver ; Ziegler ; Mathias ; Grune ; Tilman ; Schweiger ; Manfred
• 刊名：Biochemical and Biophysical Research Communications
• 出版年：1999
• 出版时间：June 16, 1999
• 年：1999
• 卷：259
• 期：3
• 页码：576-581
• 全文大小：148 K

文摘

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.