Endo-deoxyribonuclease from Streptomyces rimosus

From filtrates of an oxytetracycline-producing culture of Streptomyces rimosus a deoxyribonuclease was purified to homogeneity and determined to be a potent endo-DNase. It is a monomeric, basic protein (M_r 21 000; pI 9.5) stable in a broad pH range but unstable to higher temperature. The enzyme has an absolute requirement for Mg^{2 +} or Mn^{2 +}, and for its full activity requires free SH groups and a low-ionic-strength environment. Its N-terminal primary structure differs from that of other nucleases.