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Molecular Biology and Evolution 17:738-750 (2000)
© 2000 Society for Molecular Biology and Evolution

Original Articles

Expansion and Molecular Evolution of the Interferon-Induced 2'–5' Oligoadenylate Synthetase Gene Family

Sudhir Kumar2,, Chandra Mitnik, Graziela Valente and Georgia Floyd-Smith

Department of Biology and Molecular and Cellular Biology Program, Arizona State University

Abstract

The mammalian 2'–5' oligoadenylate synthetases (2'–5'OASs) are enzymes that are crucial in the interferon-induced antiviral response. They catalyze the polymerization of ATP into 2'–5'-linked oligoadenylates which activate a constitutively expressed latent endonuclease, RNaseL, to block viral replication at the level of mRNA degradation. A molecular evolutionary analysis of available OAS sequences suggests that the vertebrate genes are members of a multigene family with its roots in the early history of tetrapods. The modern mammalian 2'–5'OAS genes underwent successive gene duplication events resulting in three size classes of enzymes, containing one, two, or three homologous domains. Expansion of the OAS gene family occurred by whole-gene duplications to increase gene content and by domain couplings to produce the multidomain genes. Evolutionary analyses show that the 2'–5'OAS genes in rodents underwent gene duplications as recently as 11 MYA and predict the existence of additional undiscovered OAS genes in mammals.


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