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. 1978 Mar;5(3):825-33.
doi: 10.1093/nar/5.3.825.

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

V Cameron, D Soltis, O C Uhlenbeck
Free PMC article

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

V Cameron et al. Nucleic Acids Res. 1978 Mar.
Free PMC article

Abstract

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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References

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    1. Nucleic Acids Res. 1977 Jan;4(1):85-98 - PubMed
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