The 2'-5' oligoadenylate synthetases form a well conserved family of interferon induced proteins, presumably present throughout the mammalian class. Using the Expressed Sequence Tag databases, we have identified a novel member of this family. This protein, which we named p59 2'-5' oligoadenylate synthetase-like protein (p59OASL), shares a highly conserved N-terminal domain with the known forms of 2'-5' oligoadenylate synthetases, but differs completely in its C-terminal part. The C-terminus of p59OASL is formed of two domains of ubiquitin-like sequences. Here we present the characterisation of a full-length cDNA clone, the genomic sequence and the expression pattern of this gene. We have addressed the evolution of the 2'-5' oligoadenylate synthetase gene family, in the light of both this new member and new 2'-5' oligoadenylate synthetase sequence data from other species, which have recently appeared in the databases.
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We would like to thank the following people: Anette Bejder for excellent help with the RACE experiment and Lars Aagaard for giving invaluable help in using the Phylip package and for many fruitful discussions, Niels Ole Kjeldgaard and Tracey Flint for critical reading of the manuscript and many valuable comments, Andrew King at the Sanger Centre (Cambridge, UK) and R. D. Cox, Welcome Trust Centre for Human Genetics (Oxford, UK) for valuable help with the genomic sequence and finally Cecilia Rosada Kjeldsen for helpful discussion. This work was supported by the Danish Natural Science Research Council (BIOTEK 3 program), The Danish Cancer Society and the Karen Elise Jensen’s Foundation.