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J. Biol. Chem., Vol. 280, Issue 7, 5188-5194, February 18, 2005

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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||

From the Prokaria Limited. Gylfaflot 5, 112 Reyjavik, Iceland, the University of Iceland, Sturlugata 7, 101 Reykjavik, and ^¶GenThor Limited, Gardastraeti 11, 101 Reykjavik, Iceland

A polynucleotide kinase from the thermophilic bacteriophage RM378 that infects the thermophilic eubacterium Rhodothermus marinus was identified, expressed, and purified. This polynucleotide kinase was 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 the T4 polynucleotide kinase. The RM378 phosphohydrolase domain displayed some sequence similarity with the bacterial poly(A) polymerase family, including an 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, suggests that the RM378 bacteriophage has to counter a similar anti-phage mechanism in R. marinus as the one that the T4 phage has to counter in Escherichia coli.

Received for publication, August 11, 2004 , and in revised form, November 30, 2004.

^* The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBank^TM/EBI Data Bank with accession number(s) NC_004735.

^|| To whom correspondence should be addressed. Tel.: 35-5707900; Fax: 354-5707901; E-mail: jakob.kristjansson{at}prokaria.com.

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