Restriction and modification in B. subtilis. Purification and general properties of a restriction endonuclease from strain R. |
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| Authors: | Sierd Bron Kenneth Murray Thomas A. Trautner |
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| Affiliation: | (1) Department of Molecular Biology, University of Edinburgh, Edinburgh, Scotland;(2) Department of Genetics, Biological Centre, Haren (Gn), The Netherlands;(3) Department of Molecular Biology, University of Edinburgh, EH9 3JR Edinburgh, Scotland;(4) Max-Planck-Institut für Molekulare Genetik, Ihnestr. 63-73, D-1000 Berlin 33, Germany |
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| Abstract: | Summary All Bacillus subtilis R-type strains showing the phenomena of restriction and modification contain an endonuclease that inactivates in vitro the biological activity of a variety of DNAs lacking R-specific modification, such as transfecting SPP1, SPO2 and  105 DNA, and transforming B. subtilis 168-type DNA. The corresponding DNAs carrying R-specific modification are resistant to the enzyme. The enzyme has been purified approximately 400-fold and is essentially free from contaminating double strand-directed unspecific exo-or endonuclease activity. Only Mg2+ is required as cofactor. The substrate DNAs are cleaved at specific sites. The double-stranded fragments produced from SPP1 DNA (molecular weight 2.5×107) have an average molecular weight of about 3×105. |
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