S. Nagasawa et al., Phylogenic distribution of poly(ADP-ribose) glycohydrolase and poly(ADP-ribose)-digesting phosphodiesterase, P JPN AC B, 76(3), 2000, pp. 41-44
Citations number
20
Categorie Soggetti
Multidisciplinary
Journal title
PROCEEDINGS OF THE JAPAN ACADEMY SERIES B-PHYSICAL AND BIOLOGICAL SCIENCES
Most of eukaryotes, except for Saccharomyces cerevisiae, possess poly(ADP-r
ibose) polymerase (PARP, EC 2.4.2.30) activity. Poly(ADP-ribose) is describ
ed to be mainly degraded by poly(ADP -ribose) glycohydrolase (PARG) and als
o by phosphodiesterase I (PDEase, EC 3.1.4.1). To understand the function a
nd metabolism of poly(ADP-ribose), the distribution of poly(ADP-ribose) deg
radation activity in various kinds of species mas investigated. Poly(ADP-ri
bose) degradation activity was detected in extracts from Various kinds of e
ukaryotes including Rattus norvegicus, Sarcophaga peregrina, Caenorhabditis
Dictyostelium discoideum, Tetrahymena thermophila, Tetrahymena pyriformis,
and Neurospora cl crassa. However, poly(ADP-ribose) degradation activity w
as not observed in Schizosaccharomyces pombe, and prokaryotes, namely Esche
richia coli and Halobacterium volcanii. The main degradation products of [P
-32]poly(ADP-ribose), which were detected by the radioactivity, were ADP-ri
bose, phosphoribosyl-AMP and 5'-AMP at different ratios in each species. Th
is suggests that PARG and PDEases are involved in the degradation of poly(A
DP-ribose) at the initial step. Since poly(ADP-ribose) degradation due to P
ARG activity and PDEase activity, and poly(ADP-ribose) formation due Co PAR
P activity were not detectable in Schizosaccharomyces pombe, Escherichia co
li and Halobacterium volcanii, the presence of PARG as well as PDEase well
correlates with that of PARP in various kinds of species.