Cold Body Temperature as an Evolutionary Shaping Force in the Physiology of Antarctic Fishes

• Main Author: Sidell, Bruce
• Format: Text
• Language: unknown
• Published: DigitalCommons@UMaine 2006
• Subjects: Notothenioid fishes; Fatty acyl CoA synthetase; Parvalbumin; Ecology and Evolutionary Biology; Antarctic; Antarc*; Antarctica
• Online Access: https://digitalcommons.library.umaine.edu/orsp_reports/197; https://digitalcommons.library.umaine.edu/cgi/viewcontent.cgi?article=1207&context=orsp_reports

Notothenioid fishes that dominate the fish fauna surrounding Antarctica have been evolving for 10-14 million years at a nearly constant body temperature of ~0C throughout their life histories. As a result, this group of animals is uniquely suited to studies aimed at understanding and identifying features of physiology and biochemistry that result from the process of evolution at cold body temperature. This project has three major objectives aimed at examining adaptations for life in cold environments: 1. Identify the amino acid substitutions in the fatty acid-binding pocket of fatty acyl CoA synthetase (FACS) that explain its substrate specificity. Fatty acids are a major fuel of energy metabolism in Antarctic fishes. FACS catalyzes the condensation of CoASH and fatty acids to fatty acyl CoA esters, a step required for subsequent metabolism of these important compounds. This research may permit us to resolve the specific amino acid substitutions that explain both substrate specificity and preservation of catalytic rate of notothenioid FACS at cold physiological temperatures.2. Produce a rigorous biochemical and biophysical characterization of the intracellular calcium-binding protein, parvalbumin, from white axial musculature of Antarctic fishes. Parvalbumin plays a pivotal role in facilitating the relaxation phase of fast-contracting muscles and is a likely site of strong selective pressure. Preliminary data strongly indicate that the protein from Antarctic fishes has been modified to ensure function at cold temperature. A suite of physical techniques will be used to determine dissociation constants of Antarctic fish parvalbumins for calcium and magnesium and unidirectional rate constants of ion-dissociation from the protein. Full-length cDNA clones for Antarctic fish parvalbumin(s) will permit deduction of primary amino acid sequence These data will yield insight into structural elements that permit the protein from notothenioid fishes to function at very cold body temperature.3. Conduct a broad survey of the ...