Beyond the Identification of Transcribed Sequences:
Functional, Evolutionary and Expression Analysis
12th International Workshop
October 25-28, 2002
Washington, DC


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Identification and Characterization of a Novel Thermostable RNA ligase

T. Blondal,2  O. Fridjonsson, 1  S. Hjorleifsdottir, 1  A. Ævarsson, 1  S. Skirnisdottir,1  A.G. Hermannsdottir, 1  G.O. Hreggvidsson, 1,3 Albert Vernon Smith2 and J.K. Kristjansson1,3
1 Prokaria ltd. Gylfaflot 5, 101 Reyjavik, Iceland, 2 DeCode Genetics Inc, Reykjavik Iceland, 3 University of Iceland, Grensasvegur 12, 107 Reykjavik, Iceland
Telephone: +345 5701900
Fax: +354 5701902
Email: thorarinn@decode.is

T4-RNA-ligase has the ability to ligate single stranded nucleic acids. It catalyses intra- and inter-molecular formation of phosphodiester bonds between 5'-phosphate and 3'-hydroxyl termini of single-stranded RNA or DNA, in an ATP dependent manner.  This enzyme is increasingly being used in various molecular biology applications, especailly in RNA-based protocols for retrieving genes or gene fragments (such as RACE). Furthermore it has use in single gene specific primer  PCR methods for retrieving flanking regions of gene fragments and for modifications of  5’-ends of single stranded nucleic acids. RNA-ligases of this type have only been found in T4-like phages, but recently a homologous gene has been  identified in the plant virus Autographa californica.

We report the identification of  a thermostable RNA ligase in the genome of a T4-like phage, RM 378 that infects  the thermophilic bacterium Rhodothermus marinus. The gene has been cloned and expressed in high quantities and purified. Properties of this enzyme will be reported.



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