Structure/function studies of dogfish α-crystallin, comparison with bovine α-crystallin

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dc.contributor.authorGhahghaei, Aen_AU
dc.contributor.authorRekas, Aen_AU
dc.contributor.authorCarver, JAen_AU
dc.contributor.authorAugusteyn, RCen_AU
dc.date.accessioned2010-01-21T23:15:49Zen_AU
dc.date.accessioned2010-04-30T05:04:05Zen_AU
dc.date.available2010-01-21T23:15:49Zen_AU
dc.date.available2010-04-30T05:04:05Zen_AU
dc.date.issued2009-11-20en_AU
dc.date.statistics2009-11-20en_AU
dc.description.abstractPurpose: α-Crystallin is the major protein of the mammalian lens where it contributes to the refractive properties needed for vision and possibly to the stability of the tissue. The aim of this study was to determine whether the properties of α-crystallin have changed during the course of evolution. Methods: Dogfish α-crystallin, which appeared over 420 million years ago, has been contrasted with bovine α-crystallin, which emerged around 160 million years later, by comparing their sizes, the microenvironments of their cysteine and tryptophan residues, their chaperone-like activities and the flexibility of their COOH-terminal extensions. Results: Dogfish α-crystallin consists of α A- and α B-polypeptides, in a 1: 5 ratio, and has a molecular mass of around 400 kDa. By contrast, the bovine protein is around 600-800 kDa in mass and has a 3: 1 subunit ratio. Cysteine residues in the proteins were equally accessible to reaction with 5,5'-dithiobis-(2-nitrobenzoic acid). Quenching of fluorescence with acrylamide indicated tryptophan residues in the two proteins were in similar environments. The chaperone activity of dogfish α-crystallin was comparable to that of bovine α-crystallin in preventing the heat-induced precipitation of β(L)-crystallin but the dogfish protein was three times more effective at preventing insulin precipitation after reduction at 37 degrees C. H-1 nuclear magnetic resonance spectroscopic studies showed that the last 17 amino acids of the dogfish α B polypeptide (V162-K178) have great conformational flexibility, are highly exposed to solvent and adopt little ordered conformation. This is comparable to, but slightly longer in length, than the COOH-terminal extension observed in mammalian alpha-crystallins. Conclusions: The structure and properties of α-crystallin have changed relatively little during the evolutionary period from the emergence of sharks and mammals. © US National Library of Medicine National Institutes of Healthen_AU
dc.identifier.citationGhahghaei, A., Rekas, A., Carver, J. A., & Augusteyn, R. C. (2009). Structure/function studies of dogfish alpha-crystallin, comparison with bovine alpha-crystallin. Molecular Vision, 15, 2411–2420. Retrieved from https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2785718/en_AU
dc.identifier.govdoc1263en_AU
dc.identifier.issn1090-0535en_AU
dc.identifier.journaltitleMolecular Visionen_AU
dc.identifier.pagination2411-2420en_AU
dc.identifier.urihttp://apo.ansto.gov.au/dspace/handle/10238/2749en_AU
dc.identifier.urihttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC2785718/en_AU
dc.identifier.volume15en_AU
dc.language.isoenen_AU
dc.publisherNational Center for Biotechnology Informationen_AU
dc.subjectCrystalline lensen_AU
dc.subjectCattleen_AU
dc.subjectFishesen_AU
dc.subjectProteinsen_AU
dc.subjectAmino acidsen_AU
dc.subjectEvolutionen_AU
dc.titleStructure/function studies of dogfish α-crystallin, comparison with bovine α-crystallinen_AU
dc.typeJournal Articleen_AU
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