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Nucleic Acids Research, 2003, Vol. 31, No. 24 7247-7254
© 2003 Oxford University Press

Article

Discovery and characterization of a thermostable bacteriophage RNA ligase homologous to T4 RNA ligase 1

Thorarinn Blondal1,2,3, Sigridur H. Hjorleifsdottir1, Olafur F. Fridjonsson1, Arnthor Ævarsson1, Sigurlaug Skirnisdottir1, Anna Gudny Hermannsdottir1, Gudmundur O. Hreggvidsson1,2, Albert Vernon Smith3 and Jakob K. Kristjansson*,1,2

1 Prokaria Ltd, Gylfaflot 5, 101 Reykjavik, Iceland, 2 University of Iceland, 107 Reykjavik, Iceland and 3 deCode Genetics Inc., 112 Reykjavik, Iceland

*To whom correspondence should be addressed. Tel: +354 5707900; Fax: +354 5707901; Email: jakob.kristjansson{at}prokaria.com

Thermophilic viruses represent a novel source of genetic material and enzymes with great potential for use in biotechnology. We have isolated a number of thermophilic viruses from geothermal areas in Iceland, and by combining high throughput genome sequencing and state of the art bioinformatics we have identified a number of genes with potential use in biotechnology. We have also demonstrated the existence of thermostable counterparts of previously known bacteriophage enzymes. Here we describe a thermostable RNA ligase 1 from the thermophilic bacteriophage RM378 that infects the thermophilic eubacterium Rhodothermus marinus. The RM378 RNA ligase 1 has a temperature optimum of 60–64°C and it ligates both RNA and single-stranded DNA. Its thermostability and ability to work under conditions of high temperature where nucleic acid secondary structures are removed makes it an ideal enzyme for RNA ligase-mediated rapid amplification of cDNA ends (RLM-RACE), and other RNA and DNA ligation applications.


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