γS-Crystallin Proteins from the Antarctic Nototheniid Toothfish: A Model System for Investigating Differential Resistance to Chemical and Thermal Denaturation

• Main Authors: Kingsley, Carolyn N, Bierma, Jan C, Pham, Vyvy, Martin, Rachel W
• Format: Article in Journal/Newspaper
• Language: unknown
• Published: eScholarship, University of California 2014
• Subjects: Eye Disease and Disorders of Vision; Animals; Catfishes; Circular Dichroism; Escherichia coli; Fish Proteins; Humans; Models; Molecular; Nuclear Magnetic Resonance; Biomolecular; Perciformes; Protein Denaturation; Protein Stability; Protein Structure; Secondary; Scattering; Radiation; Sequence Homology; Sharks; Spectrometry; Fluorescence; Temperature; Urea; Zebrafish; gamma-Crystallins; Physical Sciences; Chemical Sciences; Engineering; Antarctic; The Antarctic; Antarc*; Antarctic Toothfish
• Online Access: https://escholarship.org/uc/item/3h75g84j

The γS1- and γS2-crystallins, structural eye lens proteins from the Antarctic toothfish (Dissostichus mawsoni), are homologues of the human lens protein γS-crystallin. Although γS1 has the higher thermal stability of the two, it is more susceptible to chemical denaturation by urea. The lower thermodynamic stability of both toothfish crystallins relative to human γS-crystallin is consistent with the current picture of how proteins from organisms endemic to perennially cold environments have achieved low-temperature functionality via greater structural flexibility. In some respects, the sequences of γS1- and γS2-crystallin are typical of psychrophilic proteins; however, their amino acid compositions also reflect their selection for a high refractive index increment. Like their counterparts in the human lens and those of mesophilic fish, both toothfish crystallins are relatively enriched in aromatic residues and methionine and exiguous in aliphatic residues. The sometimes contradictory requirements of selection for cold tolerance and high refractive index make the toothfish crystallins an excellent model system for further investigation of the biophysical properties of structural proteins.