Isolation and characterization of two mutant forms of T4 polynucleotide kinase. Journal Article uri icon



  • The purification of polynucleotide kinase from Escherichia coli infected by two different mutants in the T4 polynucleotide kinase (pseT) gene is described. The pseT 1 enzyme has virtually no 3' specific phosphatase activity and normal polynucleotide kinase activity. The pseT 47 enzyme has very little phosphatase activity and no kinase activity. However, enzyme isolated from a pseT 1, pseT 47 mixed infection appears to contain heterodimers with considerably more phosphatase activity. Thus, the pseT 47 mutation partially inactivates the phosphatase and totally inactivates the kinase. A study of the action of polynucleotide kinase on plasmid DNAs nicked to give a 3'-phosphate and a 5'-hydroxyl indicates that although the enzyme can catalyze both the removal of the 3'-phosphate and the insertion of a 5'-phosphate, there is no evidence for a concerted reaction involving both activities on the same polypeptide chain.

publication date

  • October 10, 1982

Date in CU Experts

  • March 13, 2015 12:57 PM

Full Author List

  • Soltis DA; Uhlenbeck OC

author count

  • 2

Other Profiles

International Standard Serial Number (ISSN)

  • 0021-9258

Additional Document Info

start page

  • 11332

end page

  • 11339


  • 257


  • 19