ArticleJournal of molecular evolution2009
Evolution of the 2'-5'-oligoadenylate synthetase family in eukaryotes and bacteria.
Article in Journal of molecular evolution, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 50 citations in OpenAlex.
- The OAS-RNase L pathway: Insights from experiments of nature.Science immunology · 2026Review
- Review
- The canonical antiviral protein oligoadenylate synthetase 1 elicits antibacterial functions by enhancing IRF1 translation.Immunity · 2024Article
- Oligoadenylate synthetase 1 displays dual antiviral mechanisms in driving translational shutdown and protecting interferon production.Immunity · 2024Article
- Evolution of the Major Components of Innate Immunity in Animals.Journal of molecular evolution · 2024Review
- The Many Faces of Oligoadenylate Synthetases.Journal of interferon & cytokine research : the official journal of the International Society for Interferon and Cytokine Research · 2023Review
- Origin of the OAS-RNase L innate immune pathway before the rise of jawed vertebrates via molecular tinkering.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Differential Loss of OAS Genes Indicates Diversification of Antiviral Immunity in Mammals.Vaccines · 2023Article
- Article
- Alternative splicing coupled with transcript degradation modulates OAS1g antiviral activity.RNA (New York, N.Y.) · 2020Article
- Characteristics of Human OAS1 Isoform Proteins.Viruses · 2020Article
- RNA regulation of the antiviral protein 2'-5'-oligoadenylate synthetase.Wiley interdisciplinary reviews. RNA · 2019Review
- Recurrent Loss-of-Function Mutations Reveal Costs to OAS1 Antiviral Activity in Primates.Cell host & microbe · 2019Article
- Article
- Identification of 2'-5'-Oligoadenylate Synthetase-Like Gene in Goose: Gene Structure, Expression Patterns, and Antiviral Activity Against Newcastle Disease Virus.Journal of interferon & cytokine research : the official journal of the International Society for Interferon and Cytokine Research · 2016Article
- Enzyme assays for synthesis and degradation of 2-5As and other 2'-5' oligonucleotides.BMC biochemistry · 2015Article
- OASL-a new player in controlling antiviral innate immunity.Current opinion in virology · 2015Review
- Mitochondrial localization of the OAS1 p46 isoform associated with a common single nucleotide polymorphism.BMC cell biology · 2014Article
- Molecular evolutionary and structural analysis of the cytosolic DNA sensor cGAS and STING.Nucleic acids research · 2014Article
- Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The 2'-5'-oligoadenylate synthetase (OAS) belongs to a nucleotidyl transferase family that includes poly(A) polymerases and CCA-adding enzymes. In mammals and birds, the OAS functions in the interferon system but it is also present in an active form in sponges, which are devoid of the interferon system. In view of these observations, we have pursued the idea that OAS genes could be present in other metazoans and in unicellular organisms as well. We have identified a number of OAS1 genes in annelids, mollusks, a cnidarian, chordates, and unicellular eukaryotes and also found a family of proteins in bacteria that contains the five OAS-specific motifs. This indicates a specific relationship to OAS. The wide distribution of the OAS genes has made it possible to suggest how the OAS1 gene could have evolved from a common ancestor to choanoflagellates and metazoans. Furthermore, we suggest that the OASL may have evolved from an ancestor of cartilaginous fishes, and that the OAS2 and the OAS3 genes evolved from a mammalian ancestor. OAS proteins function in the interferon system in mammals. This system is only found in jawed vertebrates. We therefore suggest that the original function of OAS may differ from its function in the interferon system, and that this original function of OAS is preserved even in OAS genes that code for proteins, which do not have 2'-5'-oligoadenylate synthetase activity.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.