A poly(dT)-stimulated ATPase activity associated with simian virus 40 large T antigen

Autor:	D Giacherio, Lowell P. Hager
Rok vydání:	1979
Předmět:	chemistry.chemical_classification SV40 large T antigen Ribonucleotide Activator (genetics) Cell Biology Biology Biochemistry Molecular biology Deoxyribonucleotide chemistry.chemical_compound Enzyme chemistry Polynucleotide Specific activity Molecular Biology DNA
Zdroj:	Journal of Biological Chemistry. 254:8113-8116
ISSN:	0021-9258
DOI:	10.1016/s0021-9258(19)86859-x
Popis:	Highly purified SV40 large T antigen exhibits an ATPase activity which can be stimulated approximately 7-fold by the DNA homopolymer poly(dT). The poly(dT)-stimulated enzyme can hydrolyze various ribonucleotide and deoxyribonucleotide triphosphates, with ATP and dATP serving as the best substrates. Purified large T antigen hydrolyzes ATP to ADP and Pi, with a maximum specific activity of 13.5 mumol of inorganic phosphate released per h per mg of protein. Of the various natural and synthetic polynucleotides tested, poly(dT) was by far the best activator. Long chain poly(dT) molecules are much more effective activators than are short chain length oligo(dT) molecules. The highly purified large T antigen contains no detectable protein kinase activity.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::1703ca91e3d41a77cc32c414f8849de1 https://doi.org/10.1016/s0021-9258(19)86859-x Zobrazit plný text záznamu