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Symplectin evolved from multiple duplications in bioluminescent squid
The squid Sthenoteuthis oualaniensis, formerly Symplectoteuthis oualaniensis, generates light using the luciferin coelenterazine and a unique enzyme, symplectin. Genetic information is limited for bioluminescent cephalopod species, so many proteins, including symplectin, occur in public databases on...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
PeerJ Inc.
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5541922/ https://www.ncbi.nlm.nih.gov/pubmed/28785521 http://dx.doi.org/10.7717/peerj.3633 |
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author | Francis, Warren R. Christianson, Lynne M. Haddock, Steven H.D. |
author_facet | Francis, Warren R. Christianson, Lynne M. Haddock, Steven H.D. |
author_sort | Francis, Warren R. |
collection | PubMed |
description | The squid Sthenoteuthis oualaniensis, formerly Symplectoteuthis oualaniensis, generates light using the luciferin coelenterazine and a unique enzyme, symplectin. Genetic information is limited for bioluminescent cephalopod species, so many proteins, including symplectin, occur in public databases only as sequence isolates with few identifiable homologs. As the distribution of the symplectin/pantetheinase protein family in Metazoa remains mostly unexplored, we have sequenced the transcriptomes of four additional luminous squid, and make use of publicly available but unanalyzed data of other cephalopods, to examine the occurrence and evolution of this protein family. While the majority of spiralians have one or two copies of this protein family, four well-supported groups of proteins are found in cephalopods, one of which corresponds to symplectin. A cysteine that is critical for symplectin functioning is conserved across essentially all members of the protein family, even those unlikely to be used for bioluminescence. Conversely, active site residues involved in pantetheinase catalysis are also conserved across essentially all of these proteins, suggesting that symplectin may have multiple functions including hydrolase activity, and that the evolution of the luminous phenotype required other changes in the protein outside of the main binding pocket. |
format | Online Article Text |
id | pubmed-5541922 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | PeerJ Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-55419222017-08-07 Symplectin evolved from multiple duplications in bioluminescent squid Francis, Warren R. Christianson, Lynne M. Haddock, Steven H.D. PeerJ Biochemistry The squid Sthenoteuthis oualaniensis, formerly Symplectoteuthis oualaniensis, generates light using the luciferin coelenterazine and a unique enzyme, symplectin. Genetic information is limited for bioluminescent cephalopod species, so many proteins, including symplectin, occur in public databases only as sequence isolates with few identifiable homologs. As the distribution of the symplectin/pantetheinase protein family in Metazoa remains mostly unexplored, we have sequenced the transcriptomes of four additional luminous squid, and make use of publicly available but unanalyzed data of other cephalopods, to examine the occurrence and evolution of this protein family. While the majority of spiralians have one or two copies of this protein family, four well-supported groups of proteins are found in cephalopods, one of which corresponds to symplectin. A cysteine that is critical for symplectin functioning is conserved across essentially all members of the protein family, even those unlikely to be used for bioluminescence. Conversely, active site residues involved in pantetheinase catalysis are also conserved across essentially all of these proteins, suggesting that symplectin may have multiple functions including hydrolase activity, and that the evolution of the luminous phenotype required other changes in the protein outside of the main binding pocket. PeerJ Inc. 2017-07-31 /pmc/articles/PMC5541922/ /pubmed/28785521 http://dx.doi.org/10.7717/peerj.3633 Text en ©2017 Francis et al. http://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, reproduction and adaptation in any medium and for any purpose provided that it is properly attributed. For attribution, the original author(s), title, publication source (PeerJ) and either DOI or URL of the article must be cited. |
spellingShingle | Biochemistry Francis, Warren R. Christianson, Lynne M. Haddock, Steven H.D. Symplectin evolved from multiple duplications in bioluminescent squid |
title | Symplectin evolved from multiple duplications in bioluminescent squid |
title_full | Symplectin evolved from multiple duplications in bioluminescent squid |
title_fullStr | Symplectin evolved from multiple duplications in bioluminescent squid |
title_full_unstemmed | Symplectin evolved from multiple duplications in bioluminescent squid |
title_short | Symplectin evolved from multiple duplications in bioluminescent squid |
title_sort | symplectin evolved from multiple duplications in bioluminescent squid |
topic | Biochemistry |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5541922/ https://www.ncbi.nlm.nih.gov/pubmed/28785521 http://dx.doi.org/10.7717/peerj.3633 |
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