ArticleProceedings of the National Academy of Sciences of the United States of America2013
Protein cold adaptation strategy via a unique seven-amino acid domain in the icefish (Chionodraco hamatus) PEPT1 transporter.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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13 citing papers in PubMed, 28 citations in OpenAlex.
- Temperature regulated nutrient sensing and metabolism of amino acids in juvenile turbot (Marine life science & technology · 2025Article
- Molecular Fingerprint of Cold Adaptation in Antarctic Icefish PepT1 (Biomolecules · 2025Article
- Molecular determinants for cold adaptation in an Antarctic NaProceedings of the National Academy of Sciences of the United States of America · 2023Article
- Adaptation of Antarctic Icefish Vision to Extreme Environments.Molecular biology and evolution · 2023Article
- Cold-Active Lipases and Esterases: A Review on Recombinant Overexpression and Other Essential Issues.International journal of molecular sciences · 2022Review
- The "www" ofMembranes · 2022Review
- Comparative transcriptomics of ice-crawlers demonstrates cold specialization constrains niche evolution in a relict lineage.Evolutionary applications · 2021Article
- Effects of Short-Term Fasting on mRNA Expression of Ghrelin and the Peptide Transporters PepT1 and 2 in Atlantic Salmon (Frontiers in physiology · 2021Article
- The peptide transporter 1a of the zebrafishGenes & nutrition · 2019Article
- Di- and tripeptide transport in vertebrates: the contribution of teleost fish models.Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology · 2017Review
- Continental-level population differentiation and environmental adaptation in the mushroom Suillus brevipes.Molecular ecology · 2017Article
- Complete mitochondrial genome of the Antarctic crocodile icefish,Mitochondrial DNA. Part B, Resources · 2016Article
- Teleost fish models in membrane transport research: the PEPT1(SLC15A1) H+-oligopeptide transporter as a case study.The Journal of physiology · 2014Review
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Authors and funding
8 authors at 2 institutions in 2 countries.
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No grant is acknowledged in the PubMed record.
Abstract
Adaptation of organisms to extreme environments requires proteins to work at thermodynamically unfavorable conditions. To adapt to subzero temperatures, proteins increase the flexibility of parts of, or even the whole, 3D structure to compensate for the lower thermal kinetic energy available at low temperatures. This may be achieved through single-site amino acid substitutions in regions of the protein that undergo large movements during the catalytic cycle, such as in enzymes or transporter proteins. Other strategies of cold adaptation involving changes in the primary amino acid sequence have not been documented yet. In Antarctic icefish (Chionodraco hamatus) peptide transporter 1 (PEPT1), the first transporter cloned from a vertebrate living at subzero temperatures, we came upon a unique principle of cold adaptation. A de novo domain composed of one to six repeats of seven amino acids (VDMSRKS), placed as an extra stretch in the cytosolic COOH-terminal region, contributed per se to cold adaptation. VDMSRKS was in a protein region uninvolved in transport activity and, notably, when transferred to the COOH terminus of a warm-adapted (rabbit) PEPT1, it conferred cold adaptation to the receiving protein. Overall, we provide a paradigm for protein cold adaptation that relies on insertion of a unique domain that confers greater affinity and maximal transport rates at low temperatures. Due to its ability to transfer a thermal trait, the VDMSRKS domain represents a useful tool for future cell biology or biotechnological applications.
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