• norsk
    • English
  • norsk 
    • norsk
    • English
  • Logg inn
Vis innførsel 
  •   Hjem
  • University of Bergen Library
  • Registrations from Cristin
  • Vis innførsel
  •   Hjem
  • University of Bergen Library
  • Registrations from Cristin
  • Vis innførsel
JavaScript is disabled for your browser. Some features of this site may not work without it.

Toxin-like neuropeptides in the sea anemone Nematostella unravel recruitment from the nervous system to venom

Sachkova, Maria; Landau, Morani; Surm, Joachim M.; Macrander, Jason; Singer, Shir A.; Reitzel, Adam M.; Moran, Yehu
Journal article, Peer reviewed
Accepted version
Thumbnail
Åpne
Accepted version (171.5Kb)
Permanent lenke
https://hdl.handle.net/11250/2762562
Utgivelsesdato
2020
Metadata
Vis full innførsel
Samlinger
  • Registrations from Cristin [5233]
  • Sars International Centre for Marine Molecular Biology [113]
Originalversjon
Proceedings of the National Academy of Sciences of the United States of America. 2020, 117(44), 27481-27492   10.1073/pnas.2011120117
Sammendrag
The sea anemone Nematostella vectensis (Anthozoa, Cnidaria) is a powerful model for characterizing the evolution of genes functioning in venom and nervous systems. Although venom has evolved independently numerous times in animals, the evolutionary origin of many toxins remains unknown. In this work, we pinpoint an ancestral gene giving rise to a new toxin and functionally characterize both genes in the same species. Thus, we report a case of protein recruitment from the cnidarian nervous to venom system. The ShK-like1 peptide has a ShKT cysteine motif, is lethal for fish larvae and packaged into nematocysts, the cnidarian venom-producing stinging capsules. Thus, ShK-like1 is a toxic venom component. Its paralog, ShK-like2, is a neuropeptide localized to neurons and is involved in development. Both peptides exhibit similarities in their functional activities: They provoke contraction in Nematostella polyps and are toxic to fish. Because ShK-like2 but not ShK-like1 is conserved throughout sea anemone phylogeny, we conclude that the two paralogs originated due to a Nematostella-specific duplication of a ShK-like2 ancestor, a neuropeptide-encoding gene, followed by diversification and partial functional specialization. ShK-like2 is represented by two gene isoforms controlled by alternative promoters conferring regulatory flexibility throughout development. Additionally, we characterized the expression patterns of four other peptides with structural similarities to studied venom components and revealed their unexpected neuronal localization. Thus, we employed genomics, transcriptomics, and functional approaches to reveal one venom component, five neuropeptides with two different cysteine motifs, and an evolutionary pathway from nervous to venom system in Cnidaria.
Utgiver
National Academy of Sciences
Tidsskrift
Proceedings of the National Academy of Sciences of the United States of America
Opphavsrett
Copyright 2020 The Authors

Kontakt oss | Gi tilbakemelding

Personvernerklæring
DSpace software copyright © 2002-2019  DuraSpace

Levert av  Unit
 

 

Bla i

Hele arkivetDelarkiv og samlingerUtgivelsesdatoForfattereTitlerEmneordDokumenttyperTidsskrifterDenne samlingenUtgivelsesdatoForfattereTitlerEmneordDokumenttyperTidsskrifter

Min side

Logg inn

Statistikk

Besøksstatistikk

Kontakt oss | Gi tilbakemelding

Personvernerklæring
DSpace software copyright © 2002-2019  DuraSpace

Levert av  Unit