Abstract
We wish to report a puzzling ATPase activity associated with the DNA restriction endonuclease from E. coli strain K1–3. This enzyme makes a limited number of double chain breaks in DNA molecules lacking the host-controlled modification imparted by strain K. Unmodified DNA molecules from bacteriophage λ, which serve as a convenient substrate, are broken into fragments with a weight average molecular weight of approximately 7 × 106, about one-fifth the size of the intact λ chromosome. The reaction requires Mg2+, ATP and S-adenosylmethionine (SAM).
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YUAN, R., HEYWOOD, J. & MESELSON, M. ATP Hydrolysis by Restriction Endonuclease from E. coli K. Nature New Biology 240, 42–43 (1972). https://doi.org/10.1038/newbio240042a0
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DOI: https://doi.org/10.1038/newbio240042a0
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