title: Protein cold adaptation strategy via a unique seven-amino acid domain in the icefish (Chionodraco hamatus) PEPT1 transporter.
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.
authors.affiliation: Laboratory of General Physiology, Department of Biological and Environmental Sciences and Technologies, University of Salento, I-73100 Lecce, Italy.
authors.forename: Antonia
authors.initials: A
authors.lastname: Rizzello
authors.forename: Alessandro
authors.initials: A
authors.lastname: Romano
authors.forename: Gabor
authors.initials: G
authors.lastname: Kottra
authors.forename: Raffaele
authors.initials: R
authors.lastname: Acierno
authors.forename: Carlo
authors.initials: C
authors.lastname: Storelli
authors.forename: Tiziano
authors.initials: T
authors.lastname: Verri
authors.forename: Hannelore
authors.initials: H
authors.lastname: Daniel
authors.forename: Michele
authors.initials: M
authors.lastname: Maffia
mesh_terms: D000220:Adaptation, Biological / Q000502:physiology*; D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D003001:Cloning, Molecular; D016000:Cluster Analysis; D003080:Cold Temperature; D008958:Models, Molecular; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D018408:Patch-Clamp Techniques; D000074011:Peptide Transporter 1; D010473:Perciformes / Q000502:physiology*; D010802:Phylogeny; D017434:Protein Structure, Tertiary / Q000235:genetics / Q000502:physiology; D060888:Real-Time Polymerase Chain Reaction; D020133:Reverse Transcriptase Polymerase Chain Reaction; D017422:Sequence Analysis, DNA; D027981:Symporters / Q000235:genetics / Q000502:physiology*
chemical_list: D000074011:Peptide Transporter 1; D027981:Symporters