Journal
JOURNAL OF INTERFERON AND CYTOKINE RESEARCH
Volume 31, Issue 1, Pages 41-47Publisher
MARY ANN LIEBERT, INC
DOI: 10.1089/jir.2010.0107
Keywords
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Funding
- Danish Cancer Society
- Danish Medical Research Council [22-04-0704]
- Novo Nordisk Foundation
- Carlsberg Foundation
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The 2'-5' oligoadenylate synthetases (OAS) are interferon-induced antiviral enzymes that recognize virally produced dsRNA and initiate RNA destabilization through activation of RNase L within infected cells. However, recent evidence points toward several RNase L-independent pathways, through which members of the OAS family can exert antiviral activity. The crystal structure of OAS led to a novel insight into the catalytic mechanism, and revealed a remarkable similarity between OAS, Polyadenosine polymerase, and the class I CCA-adding enzyme from Archeoglobus fulgidus. This, combined with a variety of bioinformatic data, leads to the definition of a superfamily of template independent polymerases and proved that the OAS family are ancient proteins, which probably arose as early as the beginning of metazoan evolution.
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