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M409211200v1
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Papers In Press, published online ahead of print December 2, 2004
J. Biol. Chem, 10.1074/jbc.M409211200
Submitted on August 11, 2004
Revised on November 30, 2004
Accepted on December 2, 2004

Characterization of a 5' polynucleotide kinase-3' phosphatase from bacteriophage RM378

Thorarinn Blondal, Sigridur Hjorleifsdottir, Arnthor Aevarsson, Olafur H. Fridjonsson, Sigurlaug Skirnisdottir, Jon Oskar Wheat, Anna Gudny Hermannsdottir, Gudmundur O. Hreggvidsson, Albert Vernon Smith, and Jakob K. Kristjansson

Prokaria Ltd., Reykjavik 112

Corresponding Author: thorarinn{at}prokaria.com

A polynucleotide kinase from the thermophilic bacteriophage RM378 that infects the thermophilic eubacterium Rhodothermus marinus was identified, expressed and purified. This polynucleotide kinase demonstrated to have a 5’ kinase domain as well as a 3’ phosphohydrolase domain. The RM378 polynucleotide kinase had limited sequence similarity to the 5’ kinase domain of the T4 bacteriophage polynucleotide kinase, but apparent homology was not evident within the 3’ phosphohydrolase domain. The domain order of RM378 polynucleotide kinase was reversed relative to that of T4 polynucleotide kinase. The RM378 phosphohydrolase domain displayed some sequence similarity with the bacterial poly(A) polymerase family including a HD motif, characteristic of the diverse superfamily of metal dependent HD phosphohydrolases. The RM378 polynucleotide kinase was biochemically characterized and shown to possess 5’ kinase activity on RNA and single- and double-stranded DNA at elevated temperatures. It also showed phosphohydrolase activity on 2’-3’ cyclic-adenosine monophosphate. This description of the RM378 polynucleotide kinase, along with the recently described RM378 RNA ligase, suggest that the RM378 bacteriophage has to counter similar antiphage mechanism in R. marinus as the T4 phage has to counter in Escherichia coli.


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