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Nucleic Acids Research, 1978, Vol. 5, No. 3 825-833
© 1978

Articles

Polynucleotide kinase from a T4 mutant which lacks the 3' phosphatase activity

Vicki Cameron, Daniel Soltis and C. Uhienbeck

Departments of Biochemistry and Chemistry, University of Illinois Urbana, IL 61801, USA

Received December 29, 1977. Polynucleotide kinase from E. coli infected with the PseT 1 mutant of bacteriophage T4 has been isolated. The PseT 1 enzyme purifies similarly to normal polynucleotide kinase and effectively transfers the {gamma} phosphate of ATP to the 5' terminal hydroxyl of DNA and RNA. The PseT 1 and normal enzymes require similar magnesium ion concentrations, have the same pH optima and are both inhibited by inorganic phosphate. However, the PseT 1 enzyme is totally lacking the 3' phosphatase activity associated with normal polynucleotide kinase. The PseT 1 enzyme is a useful tool for the preparation of oligonucleotides with 3' and 5' terminal phosphates for use as susbstrates for RNA ligase.


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