| First Author | Kumar S | Year | 2000 |
| Journal | Mol Biol Evol | Volume | 17 |
| Issue | 5 | Pages | 738-50 |
| PubMed ID | 10779534 | Mgi Jnum | J:61960 |
| Mgi Id | MGI:1855821 | Doi | 10.1093/oxfordjournals.molbev.a026352 |
| Citation | Kumar S, et al. (2000) Expansion and molecular evolution of the interferon-induced 2'-5' oligoadenylate synthetase gene family. Mol Biol Evol 17(5):738-50 |
| abstractText | 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. |
