ArticlePloS one2013
Helical antifreeze proteins have independently evolved in fishes on four occasions.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 61 citations in OpenAlex.
- How to measure the activity of antifreeze proteins?Biophysical reviews · 2025Review
- Adaptation, diversification and ecological opportunity in the extremophile radiation ofProceedings. Biological sciences · 2025Article
- Convergent evolution of type I antifreeze proteins from four different progenitors in response to global cooling.BMC molecular and cell biology · 2024Article
- Diverse Origins of Near-Identical Antifreeze Proteins in Unrelated Fish Lineages Provide Insights Into Evolutionary Mechanisms of New Gene Birth and Protein Sequence Convergence.Molecular biology and evolution · 2024Article
- Polyproline type II helical antifreeze proteins are widespread in Collembola and likely originated over 400 million years ago in the Ordovician Period.Scientific reports · 2023Article
- The Spruce Budworm Genome: Reconstructing the Evolutionary History of Antifreeze Proteins.Genome biology and evolution · 2022Article
- Origin of an antifreeze protein gene in response to Cenozoic climate change.Scientific reports · 2022Article
- Structural diversity of marine anti-freezing proteins, properties and potential applications: a review.Bioresources and bioprocessing · 2022Review
- Transcriptomics of a Greenlandic Snailfish Reveals Exceptionally High Expression of Antifreeze Protein Transcripts.Evolutionary bioinformatics online · 2022Article
- Mainly on the Plane: Deep Subsurface Bacterial Proteins Bind and Alter Clathrate Structure.Crystal growth & design · 2020Article
- Antifreeze protein complements cryoprotective dehydration in the freeze-avoiding springtail Megaphorura arctica.Scientific reports · 2020Article
- Antifreeze protein dispersion in eelpouts and related fishes reveals migration and climate alteration within the last 20 Ma.PloS one · 2020Article
- Freeze Tolerance in Sculpins (Pisces; Cottoidea) Inhabiting North Pacific and Arctic Oceans: Antifreeze Activity and Gene Sequences of the Antifreeze Protein.Biomolecules · 2019Article
- Review
- afpCOOL: A tool for antifreeze protein prediction.Heliyon · 2018Article
- De Novo Gene Evolution of Antifreeze Glycoproteins in Codfishes Revealed by Whole Genome Sequence Data.Molecular biology and evolution · 2018Article
- Concentration-dependent oligomerization of an alpha-helical antifreeze polypeptide makes it hyperactive.Scientific reports · 2017Article
- Molecular Phylogenetics and the Perennial Problem of Homology.Journal of molecular evolution · 2016Review
- Modeling repetitive, non-globular proteins.Protein science : a publication of the Protein Society · 2016Review
- Rainbow smelt: the unusual case of cryoprotection by sustained glycerol production in an aquatic animal.Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology · 2015Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
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.
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Registered trials
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