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Evolution of the 2′-5′-Oligoadenylate Synthetase Family in Eukaryotes and Bacteria

Journal of Molecular Evolution volume 69, Article number: 612 (2009) Cite this article

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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Abbreviations

OAS:

2′-5′-Oligoadenylate synthetase.

OASL:

2′-5′-Oligoadenylate synthetase like.

2-5A:

2′-5′-Oligoadenylates.

IFN:

Interferon

RNaseL:

Ribonuclease L

EST:

Expressed sequence tag

BLAST:

Basic local alignment search tool

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Acknowledgments

We thank the technical assistance from Lotte Quist. We thank Shawn Iadonato and Christina Scherer Kineta Inc, Seattle, WA, USA and Mia Schødt Dickow for help and stimulating discussions and Mikkel Heide Schierup for critical reading of the manuscript. Niels Larsen has helped us with definition of motifs and discussions on molecular evolution. Peter Funch is thanked for a highly appreciated discussion of this manuscript using his expertise in phylogenetics and systematics. The work was initially supported by a grant from the Danish Natural Science Council and the Carlsberg Foundation. The work was supported by the Estonian Science Foundation (Grant no. 7421).

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Affiliations

  1. Department of Molecular Biology, University of Aarhus, C.F. Mollers Allé 3, 8000, Aarhus, Denmark

    Karina Hansen Kjaer, Jesper Buchhave Poulsen, Pia Moeller Martensen & Just Justesen

  2. Department of Gene Technology, Tallinn University of Technology, Tallinn, Estonia

    Tõnu Reintamm & Merike Kelve

  3. Department of Benthic Ecology and Biodiversity, Centre d’Estudis Avancats de Blanes, CSIC, Blanes, Spain

    Emilie Saby

  4. Mads Clausen Institute, University of Southern Denmark, Alsion 2, Sønderborg, Denmark

    Just Justesen

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  1. Karina Hansen Kjaer
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  2. Jesper Buchhave Poulsen
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  7. Just Justesen
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Correspondence to Just Justesen.

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Kjaer, K.H., Poulsen, J.B., Reintamm, T. et al. Evolution of the 2′-5′-Oligoadenylate Synthetase Family in Eukaryotes and Bacteria. J Mol Evol 69, 612 (2009). https://doi.org/10.1007/s00239-009-9299-1

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  • DOI: https://doi.org/10.1007/s00239-009-9299-1

Keywords

  • Oligoadenylate synthetase
  • CCA-adding enzyme
  • Evolution
  • Interferon
  • Phylogeny