2000 Volume 76 Issue 3 Pages 41-44
Most of eukaryotes, except for Saccharomyces cerevisiae, possess poly(ADP-ribose) polymerase (PARP, EC 2.4.2.30) activity. Poly(ADP-ribose) is described to be mainly degraded by poly(ADP- ribose) glycohydrolase (PARG) and also by phosphodiesterase I (PDEase, EC 3.1.4.1). To understand the function and metabolism of poly(ADP-ribose), the distribution of poly(ADP-ribose) degradation activity in various kinds of species was investigated. Poly(ADP-ribose) degradation activity was detected in extracts from various kinds of eukaryotes including Rattus norvegicus, Sarcophaga peregrina, Caenorhabditis elegans, Dictyostelium discoideurn, Tetrahymena thermophila, Tetrahymena pyrifornis, and Neurospora crassa. However, poly(ADP-ribose) degradation activity was not observed in Schizosaccharomyces pombe, and prokaryotes, namely Escherichia coli and Halobacterium volcanii. The main degradation products of [32P]poly(ADP-ribose), which were detected by the radioactivity, were ADP-ribose, phosphoribosyl-AMP and 5'-AMP at different ratios in each species. This suggests that PARG and PDEases are involved in the degradation of poly(ADP-ribose) at the initial step. Since poly(ADP-ribose) degradation due to PARG activity and PDEase activity, and poly(ADP-ribose) formation due to PARP activity were not detectable in Schizosaccharomyces pombe, Escherichia coli and Halobacterium volcanii, the presence of PARG as well as PDEase well correlates with that of PARP in various kinds of species.
