Purification and characterization of DNA-dependent ATPase II from Escherichia coli.
A new DNA-dependent ATPase was isolated and purified from soluble extracts of Escherichia coli. This enzyme, called ATPase II, has a molecular weight of 86,000 and exists in a monomeric state. It degrades ATP (or dATP) to ADP (or dADP) and Pi in the presence of magnesium and requires a double-stranded polynucleotide as cofactor. A correlation between the efficiency as cofactor and the melting point of the polynucleotide has been found; the lower the melting temperature, the higher the stimulation of ATPase II. The enzyme binds to single-stranded DNA and poly[d(A-T)] copolymer, but not to the double-stranded circular DNA (Form I) of simian virus 40.
D000251:Adenosine Triphosphatases / Q000302:isolation & purification / Q000378:metabolism*; D002413:Cations, Divalent; D004247:DNA / Q000494:pharmacology; D004789:Enzyme Activation; D004926:Escherichia coli / Q000201:enzymology*; D007700:Kinetics; D008970:Molecular Weight; D011119:Polynucleotides / Q000494:pharmacology
D002413:Cations, Divalent; D011119:Polynucleotides; D004247:DNA; D000251:Adenosine Triphosphatases