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© Research
Publication : The Journal of biological chemistry

Purification and characterization of DNA-dependent ATPase II from Escherichia coli

Team: Archived: Group: Evelyne Richet
Member: Evelyne Richet
Scientific Fields
Diseases
Organisms
Applications
Technique

Published in The Journal of biological chemistry - 25 Oct 1978

Richet E, Kohiyama M

Link to Pubmed [PMID] – 151684

J. Biol. Chem. 1978 Oct;253(20):7490-5

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.