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Biological Sciences: Non-specific ‘pairing’ of DNA molecules by recombination enzyme of Bacillus subtilis

Abstract

ATP-dependent deoxyribonuclease(s) (ATP-DNase) is involved in the genetic recombination process in Escherichia coli1–3, Diplococcus pneumoniae4 and Bacillus subtilis5 and may also play an important part in DNA repair6–8, DNA replication9 and cell growth10. ATP-dependent or ATP-stimulated DNases have also been isolated and characterised in other microorganisms11–14. We reported the purification and properties of this enzyme in B. subtilis15,16 and noted that at the 600-fold purification level, the enzyme requires ATP for the hydrolysis of double stranded (ds) DNA, but not for single stranded (ss) DNA16. Since the activities on ds and ssDNA appear to reside in the same enzyme, we suggested the possibility that ATP consumption is somehow linked to the active unwinding of dsDNA before the DNase can hydrolyse phosphodiester bonds16. Recently, Friedman and Smith24 have also proposed an active role of ATP in dsDNA unwinding by Haemophilus influenzae enzyme, which is based on the structural feature of intermediate product DNA. To examine this possibility further, we tried to visualize the unwound portion of DNA and the DNA-enzyme complex by electron microscopy. Although the visual evidence is still ambiguous, an unexpected observation has been made. We report here the unusual property of B. subtilis ATP-DNase which apparently brings DNA molecules into close proximity or causes non-specific ‘pairing’ of dsDNA molecules.

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OHI, S., BASTIA, D. & SUEOKA, N. Biological Sciences: Non-specific ‘pairing’ of DNA molecules by recombination enzyme of Bacillus subtilis. Nature 248, 586–588 (1974). https://doi.org/10.1038/248586a0

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