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The oligoadenylate synthetase family: an ancient protein family with multiple antiviral activities.
- Source :
-
Journal of interferon & cytokine research : the official journal of the International Society for Interferon and Cytokine Research [J Interferon Cytokine Res] 2011 Jan; Vol. 31 (1), pp. 41-7. Date of Electronic Publication: 2010 Dec 12. - Publication Year :
- 2011
-
Abstract
- 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.
- Subjects :
- 2',5'-Oligoadenylate Synthetase chemistry
2',5'-Oligoadenylate Synthetase genetics
Animals
Endoribonucleases chemistry
Endoribonucleases metabolism
Enzyme Activation
Host-Pathogen Interactions
Humans
Protein Conformation
RNA Stability
RNA, Double-Stranded metabolism
RNA, Viral metabolism
2',5'-Oligoadenylate Synthetase metabolism
Gene Expression Regulation, Enzymologic
Interferons metabolism
Virus Diseases metabolism
Virus Inactivation
Subjects
Details
- Language :
- English
- ISSN :
- 1557-7465
- Volume :
- 31
- Issue :
- 1
- Database :
- MEDLINE
- Journal :
- Journal of interferon & cytokine research : the official journal of the International Society for Interferon and Cytokine Research
- Publication Type :
- Academic Journal
- Accession number :
- 21142819
- Full Text :
- https://doi.org/10.1089/jir.2010.0107