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DNA-dependent ATPase II from Bacillus cereus.

G Bánfalvi, S Csuzi, A Ohlbaum

    Biochimica Et Biophysica Acta
    |September 9, 1980
    PubMed
    Summary

    Researchers purified a novel DNA-dependent ATPase II from Bacillus cereus. This enzyme unwinds DNA using ATP, with single-stranded DNA being a more effective cofactor than double-stranded DNA.

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    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Enzymology

    Background:

    • DNA-dependent ATPases are crucial enzymes involved in various cellular processes, including DNA replication, repair, and recombination.
    • Understanding the specific functions and mechanisms of novel ATPases is essential for elucidating complex biological pathways.

    Purpose of the Study:

    • To purify and characterize a novel DNA-dependent ATPase from Bacillus cereus.
    • To investigate the enzyme's activity, substrate specificity, and DNA unwinding capabilities.

    Main Methods:

    • Purification of ATPase II from Bacillus cereus soluble extracts.
    • Enzymatic assays to measure ATP hydrolysis in the presence of Mg2+/Ca2+ and various DNA forms.
    • SDS-polyacrylamide gel electrophoresis for molecular weight determination.
    • Inhibition studies using specific chemical agents.

    Main Results:

    • A novel DNA-dependent ATPase, designated ATPase II, was purified to near homogeneity.
    • ATPase II catalyzes ATP hydrolysis, with single-stranded DNA being a more effective cofactor than double-stranded DNA.
    • The enzyme demonstrates DNA strand separation activity in the presence of ATP, though phosphohydrolysis can occur independently at higher ATP concentrations.
    • The enzyme's molecular weight was determined to be 84,000 Da.
    • ATPase II was inhibited by adenosine 5'-(beta, gamma-imido)-diphosphate, actinomycin D, and ethidium bromide, but not by nalidixic acid.

    Conclusions:

    • Bacillus cereus possesses a novel DNA-dependent ATPase (ATPase II) with DNA unwinding capabilities.
    • The enzyme's activity is modulated by DNA structure and ATP concentration.
    • ATPase II represents a potential target for further investigation into DNA metabolism and related cellular functions.

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