Helical antifreeze proteins have independently evolved in fishes on four occasions.

Alanine-rich α-helical (type I) antifreeze proteins (AFPs) are produced by a variety of fish species from three different orders to protect against freezing in icy seawater. Interspersed amongst and within these orders are fishes making AFPs that are completely different in both sequence and structu...

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Autores principales:	Laurie A Graham, Rod S Hobbs, Garth L Fletcher, Peter L Davies
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2013
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/c8106c751847427c8c5c3c7e3e894a7d
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spelling	oai:doaj.org-article:c8106c751847427c8c5c3c7e3e894a7d2021-11-18T08:43:10ZHelical antifreeze proteins have independently evolved in fishes on four occasions.1932-620310.1371/journal.pone.0081285https://doaj.org/article/c8106c751847427c8c5c3c7e3e894a7d2013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24324684/?tool=EBIhttps://doaj.org/toc/1932-6203Alanine-rich α-helical (type I) antifreeze proteins (AFPs) are produced by a variety of fish species from three different orders to protect against freezing in icy seawater. Interspersed amongst and within these orders are fishes making AFPs that are completely different in both sequence and structure. The origin of this variety of types I, II, III and antifreeze glycoproteins (AFGPs) has been attributed to adaptation following sea-level glaciations that occurred after the divergence of most of the extant families of fish. The presence of similar types of AFPs in distantly related fishes has been ascribed to lateral gene transfer in the case of the structurally complex globular type II lectin-like AFPs and to convergent evolution for the AFGPs, which consist of a well-conserved tripeptide repeat. In this paper, we examine the genesis of the type I AFPs, which are intermediate in complexity. These predominantly α-helical peptides share many features, such as putative capping structures, Ala-richness and amphipathic character. We have added to the type I repertoire by cloning additional sequences from sculpin and have found that the similarities between the type I AFPs of the four distinct groups of fishes are not borne out at the nucleotide level. Both the non-coding sequences and the codon usage patterns are strikingly different. We propose that these AFPs arose via convergence from different progenitor helices with a weak affinity for ice and that their similarity is dictated by the propensity of specific amino acids to form helices and to align water on one side of the helix into an ice-like pattern.Laurie A GrahamRod S HobbsGarth L FletcherPeter L DaviesPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 8, Iss 12, p e81285 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Laurie A Graham Rod S Hobbs Garth L Fletcher Peter L Davies Helical antifreeze proteins have independently evolved in fishes on four occasions.
description	Alanine-rich α-helical (type I) antifreeze proteins (AFPs) are produced by a variety of fish species from three different orders to protect against freezing in icy seawater. Interspersed amongst and within these orders are fishes making AFPs that are completely different in both sequence and structure. The origin of this variety of types I, II, III and antifreeze glycoproteins (AFGPs) has been attributed to adaptation following sea-level glaciations that occurred after the divergence of most of the extant families of fish. The presence of similar types of AFPs in distantly related fishes has been ascribed to lateral gene transfer in the case of the structurally complex globular type II lectin-like AFPs and to convergent evolution for the AFGPs, which consist of a well-conserved tripeptide repeat. In this paper, we examine the genesis of the type I AFPs, which are intermediate in complexity. These predominantly α-helical peptides share many features, such as putative capping structures, Ala-richness and amphipathic character. We have added to the type I repertoire by cloning additional sequences from sculpin and have found that the similarities between the type I AFPs of the four distinct groups of fishes are not borne out at the nucleotide level. Both the non-coding sequences and the codon usage patterns are strikingly different. We propose that these AFPs arose via convergence from different progenitor helices with a weak affinity for ice and that their similarity is dictated by the propensity of specific amino acids to form helices and to align water on one side of the helix into an ice-like pattern.
format	article
author	Laurie A Graham Rod S Hobbs Garth L Fletcher Peter L Davies
author_facet	Laurie A Graham Rod S Hobbs Garth L Fletcher Peter L Davies
author_sort	Laurie A Graham
title	Helical antifreeze proteins have independently evolved in fishes on four occasions.
title_short	Helical antifreeze proteins have independently evolved in fishes on four occasions.
title_full	Helical antifreeze proteins have independently evolved in fishes on four occasions.
title_fullStr	Helical antifreeze proteins have independently evolved in fishes on four occasions.
title_full_unstemmed	Helical antifreeze proteins have independently evolved in fishes on four occasions.
title_sort	helical antifreeze proteins have independently evolved in fishes on four occasions.
publisher	Public Library of Science (PLoS)
publishDate	2013
url	https://doaj.org/article/c8106c751847427c8c5c3c7e3e894a7d
work_keys_str_mv	AT laurieagraham helicalantifreezeproteinshaveindependentlyevolvedinfishesonfouroccasions AT rodshobbs helicalantifreezeproteinshaveindependentlyevolvedinfishesonfouroccasions AT garthlfletcher helicalantifreezeproteinshaveindependentlyevolvedinfishesonfouroccasions AT peterldavies helicalantifreezeproteinshaveindependentlyevolvedinfishesonfouroccasions
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Helical antifreeze proteins have independently evolved in fishes on four occasions.

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