Spermine stimulates RNA-dependent reverse transcriptase activity.
The polyamine spermine can not replace Mg2+ in the reactions catalyzed by avian myeloblastosis virus reverse transcriptase. In the presence of suboptimal Mg2+ concentrations, spermine enhanced the reverse transcriptase activities with viral 70 S RNA and synthetic polyriboadenylic acid as templates, about 4-fold and 2-fold, respectively. A similar effect occurred in the polyriboadenylic acid-directed reaction using Mn2+ as divalent cation. On the other hand, no stimulation by spermine was observed with activated DNA and polydeoxyadenylic acid as template in the reactions catalyzed by reverse transcriptase.
Aoyama
H
H
Departamento de Bioquímica, Universidade Estadual de Campinas, São Paulo, Brasil.
D001354:Avian Leukosis Virus / Q000201:enzymology*; D009189:Avian Myeloblastosis Virus / Q000201:enzymology* / Q000235:genetics; D002413:Cations, Divalent; D004247:DNA / Q000096:biosynthesis; D008274:Magnesium / Q000494:pharmacology; D011067:Poly dA-dT / Q000378:metabolism; D012367:RNA, Viral / Q000378:metabolism; D012194:RNA-Directed DNA Polymerase / Q000378:metabolism*; D013096:Spermine / Q000494:pharmacology*; D013698:Templates, Genetic
D002413:Cations, Divalent; D012367:RNA, Viral; D011067:Poly dA-dT; D013096:Spermine; D004247:DNA; D012194:RNA-Directed DNA Polymerase; D008274:Magnesium