L. Barbieri et al., Polynucleotide : adenosine glycosidase activity of saporin-L1: effect on various forms of mammalian DNA, BBA-PROT ST, 1480(1-2), 2000, pp. 258-266
Citations number
56
Categorie Soggetti
Biochemistry & Biophysics
Journal title
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY
Saporin-L1 from the leaves of Saponaria officinalis belongs to a group of p
lant polynucleotide:adenosine glycosidases, known as ribosome-inactivating
proteins due to their property of depurinating the major rRNA. Previous exp
eriments indicated that saporin-L1 and other ribosome-inactivating proteins
depurinate also DNA [Barbieri et al. (1994) Nature 372, 324; and (1996) Bi
ochem. J. 319, 507-513]. Here we describe the effects of highly purified nu
clease-free saporin-L1 on mammalian nuclear and mitochondrial DNA. Saporin-
L1 had less activity on mitochondrial DNA than on nuclear DNA. A low, altho
ugh significant, depurination of both chromatin and whole nuclei was observ
ed. Mitochondrial nucleic acids are heavily depurinated in intact mitochond
ria, although the contribute of mtDNA to the deadenylation events is not kn
own. The kinetic constants for several substrates were determined. (C) 2000
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