Lateral transfer of a lectin-like antifreeze protein gene in fishes.

Fishes living in icy seawater are usually protected from freezing by endogenous antifreeze proteins (AFPs) that bind to ice crystals and stop them from growing. The scattered distribution of five highly diverse AFP types across phylogenetically disparate fish species is puzzling. The appearance of r...

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Autores principales:	Laurie A Graham, Stephen C Lougheed, K Vanya Ewart, Peter L Davies
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2008
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/379d603b8fd248eeada24e060d7ef4bb
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id	oai:doaj.org-article:379d603b8fd248eeada24e060d7ef4bb
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spelling	oai:doaj.org-article:379d603b8fd248eeada24e060d7ef4bb2021-11-25T06:11:42ZLateral transfer of a lectin-like antifreeze protein gene in fishes.1932-620310.1371/journal.pone.0002616https://doaj.org/article/379d603b8fd248eeada24e060d7ef4bb2008-07-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/18612417/?tool=EBIhttps://doaj.org/toc/1932-6203Fishes living in icy seawater are usually protected from freezing by endogenous antifreeze proteins (AFPs) that bind to ice crystals and stop them from growing. The scattered distribution of five highly diverse AFP types across phylogenetically disparate fish species is puzzling. The appearance of radically different AFPs in closely related species has been attributed to the rapid, independent evolution of these proteins in response to natural selection caused by sea level glaciations within the last 20 million years. In at least one instance the same type of simple repetitive AFP has independently originated in two distant species by convergent evolution. But, the isolated occurrence of three very similar type II AFPs in three distantly related species (herring, smelt and sea raven) cannot be explained by this mechanism. These globular, lectin-like AFPs have a unique disulfide-bonding pattern, and share up to 85% identity in their amino acid sequences, with regions of even higher identity in their genes. A thorough search of current databases failed to find a homolog in any other species with greater than 40% amino acid sequence identity. Consistent with this result, genomic Southern blots showed the lectin-like AFP gene was absent from all other fish species tested. The remarkable conservation of both intron and exon sequences, the lack of correlation between evolutionary distance and mutation rate, and the pattern of silent vs non-silent codon changes make it unlikely that the gene for this AFP pre-existed but was lost from most branches of the teleost radiation. We propose instead that lateral gene transfer has resulted in the occurrence of the type II AFPs in herring, smelt and sea raven and allowed these species to survive in an otherwise lethal niche.Laurie A GrahamStephen C LougheedK Vanya EwartPeter L DaviesPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 3, Iss 7, p e2616 (2008)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Laurie A Graham Stephen C Lougheed K Vanya Ewart Peter L Davies Lateral transfer of a lectin-like antifreeze protein gene in fishes.
description	Fishes living in icy seawater are usually protected from freezing by endogenous antifreeze proteins (AFPs) that bind to ice crystals and stop them from growing. The scattered distribution of five highly diverse AFP types across phylogenetically disparate fish species is puzzling. The appearance of radically different AFPs in closely related species has been attributed to the rapid, independent evolution of these proteins in response to natural selection caused by sea level glaciations within the last 20 million years. In at least one instance the same type of simple repetitive AFP has independently originated in two distant species by convergent evolution. But, the isolated occurrence of three very similar type II AFPs in three distantly related species (herring, smelt and sea raven) cannot be explained by this mechanism. These globular, lectin-like AFPs have a unique disulfide-bonding pattern, and share up to 85% identity in their amino acid sequences, with regions of even higher identity in their genes. A thorough search of current databases failed to find a homolog in any other species with greater than 40% amino acid sequence identity. Consistent with this result, genomic Southern blots showed the lectin-like AFP gene was absent from all other fish species tested. The remarkable conservation of both intron and exon sequences, the lack of correlation between evolutionary distance and mutation rate, and the pattern of silent vs non-silent codon changes make it unlikely that the gene for this AFP pre-existed but was lost from most branches of the teleost radiation. We propose instead that lateral gene transfer has resulted in the occurrence of the type II AFPs in herring, smelt and sea raven and allowed these species to survive in an otherwise lethal niche.
format	article
author	Laurie A Graham Stephen C Lougheed K Vanya Ewart Peter L Davies
author_facet	Laurie A Graham Stephen C Lougheed K Vanya Ewart Peter L Davies
author_sort	Laurie A Graham
title	Lateral transfer of a lectin-like antifreeze protein gene in fishes.
title_short	Lateral transfer of a lectin-like antifreeze protein gene in fishes.
title_full	Lateral transfer of a lectin-like antifreeze protein gene in fishes.
title_fullStr	Lateral transfer of a lectin-like antifreeze protein gene in fishes.
title_full_unstemmed	Lateral transfer of a lectin-like antifreeze protein gene in fishes.
title_sort	lateral transfer of a lectin-like antifreeze protein gene in fishes.
publisher	Public Library of Science (PLoS)
publishDate	2008
url	https://doaj.org/article/379d603b8fd248eeada24e060d7ef4bb
work_keys_str_mv	AT laurieagraham lateraltransferofalectinlikeantifreezeproteingeneinfishes AT stephenclougheed lateraltransferofalectinlikeantifreezeproteingeneinfishes AT kvanyaewart lateraltransferofalectinlikeantifreezeproteingeneinfishes AT peterldavies lateraltransferofalectinlikeantifreezeproteingeneinfishes
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Lateral transfer of a lectin-like antifreeze protein gene in fishes.

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