Nucleic Acids Research, Vol 27, Issue 8 1900-1905, Copyright © 1999 by Oxford University Press
P Wang and NE Tumer
Ribosome-inactivating proteins (RIPs) are N-glycosylases that remove a
specific adenine from the sarcin/ricin loop of the large rRNA in a manner
analogous to N-glycosylases that are involved in DNA repair. Some RIPs have
been reported to remove adenines from single-stranded DNA and cleave
double-stranded supercoiled DNA. The molecular basis for the activity of
RIPs on double-stranded DNA is not known. Pokeweed antiviral protein (PAP),
a single-chain RIP from Phytolacca americana, cleaves supercoiled DNA into
relaxed and linear forms. Double-stranded DNA treated with PAP contains
apurinic/apyrimidinic (AP) sites due to the removal of adenine. Using an
active-site mutant of PAP (PAPx) which does not depurinate rRNA, we present
evidence that double-stranded DNA treated with PAPx does not contain AP
sites and is not cleaved. These results demonstrate for the first time that
PAP cleaves supercoiled double-stranded DNA using the same active site that
is required for depurination of rRNA.
ARTICLES
Pokeweed antiviral protein cleaves double-stranded supercoiled DNA using the same active site required to depurinate rRNA
Biotechnology Center and the Department of Plant Pathology, Foran Hall, Room 208, Cook College,Rutgers University, Dudley Road, New Brunswick, NJ 08903, USA.
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