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

• Published in: Nucleic Acids Research
• Main Authors: Blondal, Thorarinn, Hjorleifsdottir, Sigridur H., Fridjonsson, Olafur F., Ævarsson, Arnthor, Skirnisdottir, Sigurlaug, Hermannsdottir, Anna Gudny, Hreggvidsson, Gudmundur O., Smith, Albert Vernon, Kristjansson, Jakob K.
• Format: Text
• Language: English
• Published: Oxford University Press 2003
• Subjects: Articles; Iceland
• Online Access: http://nar.oxfordjournals.org/cgi/content/short/31/24/7247; https://doi.org/10.1093/nar/gkg914

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.