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Main Authors: Bogan, Samuel N, Surendran, Nathan, Hotaling, Scott, Desvignes, Thomas, Bista, Iliana, Lins, Luana S F, Eilertsen, Mari H, Le François, Nathalie R, Algayer, Tait, Hamilton, Scott L, Frandsen, Paul B, Hoffmann, Federico G, Kelley, Joanna L
Format: Artículo científico
Language:en
Published: Molecular biology and evolution 2025
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Online Access:https://pubmed.ncbi.nlm.nih.gov/41065271/
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author Bogan, Samuel N
Surendran, Nathan
Hotaling, Scott
Desvignes, Thomas
Bista, Iliana
Lins, Luana S F
Eilertsen, Mari H
Le François, Nathalie R
Algayer, Tait
Hamilton, Scott L
Frandsen, Paul B
Hoffmann, Federico G
Kelley, Joanna L
author_facet Bogan, Samuel N
Surendran, Nathan
Hotaling, Scott
Desvignes, Thomas
Bista, Iliana
Lins, Luana S F
Eilertsen, Mari H
Le François, Nathalie R
Algayer, Tait
Hamilton, Scott L
Frandsen, Paul B
Hoffmann, Federico G
Kelley, Joanna L
Bogan, Samuel N
Surendran, Nathan
Hotaling, Scott
Desvignes, Thomas
Bista, Iliana
Lins, Luana S F
Eilertsen, Mari H
Le François, Nathalie R
Algayer, Tait
Hamilton, Scott L
Frandsen, Paul B
Hoffmann, Federico G
Kelley, Joanna L
collection PubMed - marine biology
contents Temperature and Pressure Shaped the Evolution of Antifreeze Proteins in Polar and Deep Sea Zoarcoid Fishes. Bogan, Samuel N Surendran, Nathan Hotaling, Scott Desvignes, Thomas Bista, Iliana Lins, Luana S F Eilertsen, Mari H Le François, Nathalie R Algayer, Tait Hamilton, Scott L Frandsen, Paul B Hoffmann, Federico G Kelley, Joanna L Animals Evolution, Molecular Fishes Antifreeze Proteins Phylogeny Temperature Fish Proteins Antifreeze proteins (AFPs) have enabled teleost fishes to repeatedly colonize polar seas. Four AFP types have convergently evolved in several fish lineages. AFPs inhibit ice crystal growth and lower tissue freezing point. In lineages with AFPs, species inhabiting colder environments may possess more AFP copies. Elucidating how differences in AFP copy number evolve is challenging due to the genes' tandem array structure and consequently poor resolution of these repetitive regions. Here, we explore the evolution of type III AFPs (AFP III) in the globally distributed suborder Zoarcoidei, leveraging six new long-read genome assemblies. Zoarcoidei has fewer genomic resources relative to other polar fish clades while it is one of the few groups of fishes adapted to both the Arctic and Southern Oceans. Combining these new assemblies with additional long-read genomes available for Zoarcoidei, we conducted a comprehensive phylogenetic test of AFP III evolution and modeled the effects of thermal habitat and depth on AFP III gene family evolution. We confirm a single origin of AFP III via neofunctionalization of the enzyme sialic acid synthase B. We also show that AFP copy number increased under low temperature but decreased with depth, potentially because pressure lowers freezing point. Associations between the environment and AFP III copy number were driven by duplications of paralogs that were translocated out of the ancestral locus at which AFP III arose. Our results reveal novel environmental effects on AFP evolution and demonstrate the value of high-quality genomic resources for studying how structural genomic variation shapes convergent adaptation.
format Artículo científico
id pubmed_41065271
institution PubMed
language en
publishDate 2025
publisher Molecular biology and evolution
record_format pubmed
spellingShingle Temperature and Pressure Shaped the Evolution of Antifreeze Proteins in Polar and Deep Sea Zoarcoid Fishes.
Bogan, Samuel N
Surendran, Nathan
Hotaling, Scott
Desvignes, Thomas
Bista, Iliana
Lins, Luana S F
Eilertsen, Mari H
Le François, Nathalie R
Algayer, Tait
Hamilton, Scott L
Frandsen, Paul B
Hoffmann, Federico G
Kelley, Joanna L
Animals
Evolution, Molecular
Fishes
Antifreeze Proteins
Phylogeny
Temperature
Fish Proteins
Temperature and Pressure Shaped the Evolution of Antifreeze Proteins in Polar and Deep Sea Zoarcoid Fishes. Bogan, Samuel N Surendran, Nathan Hotaling, Scott Desvignes, Thomas Bista, Iliana Lins, Luana S F Eilertsen, Mari H Le François, Nathalie R Algayer, Tait Hamilton, Scott L Frandsen, Paul B Hoffmann, Federico G Kelley, Joanna L Animals Evolution, Molecular Fishes Antifreeze Proteins Phylogeny Temperature Fish Proteins Antifreeze proteins (AFPs) have enabled teleost fishes to repeatedly colonize polar seas. Four AFP types have convergently evolved in several fish lineages. AFPs inhibit ice crystal growth and lower tissue freezing point. In lineages with AFPs, species inhabiting colder environments may possess more AFP copies. Elucidating how differences in AFP copy number evolve is challenging due to the genes' tandem array structure and consequently poor resolution of these repetitive regions. Here, we explore the evolution of type III AFPs (AFP III) in the globally distributed suborder Zoarcoidei, leveraging six new long-read genome assemblies. Zoarcoidei has fewer genomic resources relative to other polar fish clades while it is one of the few groups of fishes adapted to both the Arctic and Southern Oceans. Combining these new assemblies with additional long-read genomes available for Zoarcoidei, we conducted a comprehensive phylogenetic test of AFP III evolution and modeled the effects of thermal habitat and depth on AFP III gene family evolution. We confirm a single origin of AFP III via neofunctionalization of the enzyme sialic acid synthase B. We also show that AFP copy number increased under low temperature but decreased with depth, potentially because pressure lowers freezing point. Associations between the environment and AFP III copy number were driven by duplications of paralogs that were translocated out of the ancestral locus at which AFP III arose. Our results reveal novel environmental effects on AFP evolution and demonstrate the value of high-quality genomic resources for studying how structural genomic variation shapes convergent adaptation.
title Temperature and Pressure Shaped the Evolution of Antifreeze Proteins in Polar and Deep Sea Zoarcoid Fishes.
topic Animals
Evolution, Molecular
Fishes
Antifreeze Proteins
Phylogeny
Temperature
Fish Proteins
url https://pubmed.ncbi.nlm.nih.gov/41065271/