Abstract
Poly(ADP-ribosyl)ation constitutes a novel type of posttranslational covalent modification of nuclear proteins. The synthesis of poly(ADP-ribose) is catalyzed by poly(ADP-ribose) synthetase (1). Recently, poly(ADP-ribose) groups on proteins were found to turn over rapidly in vivo (2, 3). The degradation of poly(ADP-ribose) is carried out by two different types of enzymes. ADP-ribosyl protein lyase cleaves the bond between mono(ADP-ribose) and protein (4). Another enzyme is poly(ADP-ribose) glycohydrolase, which is known to split the ribose-ribose glycosidic bond (5, 6). The glycohydrolase is the major enzyme responsible for polymer degradation in vivo (7). Therefore, the knowledge of its precise mode of action on poly(ADP-ribose) is important for elucidating not only the metabolism of poly(ADP-ribose) but also the biological functions of poly(ADP-ribosyl)ation. In the present study, we purified this glycohydrolase, and investigated its mode of action precisely.
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© 1989 Springer-Verlag New York Inc.
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Hatakeyama, K., Nemoto, Y., Ueda, K., Hayaishi, O. (1989). Poly(ADP-Ribose) Glycohydrolase and ADP-Ribosyl Group Turnover. In: Jacobson, M.K., Jacobson, E.L. (eds) ADP-Ribose Transfer Reactions. Springer, New York, NY. https://doi.org/10.1007/978-1-4615-8507-7_8
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DOI: https://doi.org/10.1007/978-1-4615-8507-7_8
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