Isolation of a Complex between the P Protein of Phage lamba and the dnaB Protein of Escherichia coli

作者：Albrecht Klein, Erich Lanka, Heinz Georg Schuster · 发表于：European Journal of Biochemistry · 年份：1980 · DOI：10.1111/j.1432-1033.1980.tb04467.x · 被引用次数：58 · 研究领域：Cancer therapeutics and mechanisms、Enzyme Structure and Function、Bacteriophages and microbial interactions

P protein of phage lambda and dnaB protein of Escherichia coli were isolated from (a) bacteria containing an inducible lambda P gene on a plasmid, and (b) phage-lambda-infected bacteria. P protein from both sources copurifies with part of the dnaB protein during four purification steps. A highly purified preparation contains the multimeric dnaB and the P protein in a complex as revealed by glycerol gradient centrifugation. The complex is composed of two major polypeptides. Their molecular weights of 52 000 and 26 000 are identical to those previously determined for the dnaB and P polypeptides, respectively. The complex contains a DNA-dependent ribonucleoside triphosphatase activity which can be inactivated by anti-dnaB globulin. Both the dnaB complementing and the ribonucleoside triphosphatase activities are partially masked by the P protein as shown by their stimulation following a treatment with sodium chloride and N-ethylmaleimide.