Proteins of Oxygen-Binding and Energy Metabolism in Muscles of Antarctic Fishes: Evolutionary Adjustments to Life at Cold Temperature
April 1, 2000-May 31, 2003
Level of Access
The suborder Notothenoidei is the dominant fish group of the Southern Ocean surrounding Antarctica, both in terms of number of species and biomass. For about fourteen million years, these highly successful fish evolved under stable thermal conditions that result in body temperatures of about zero degrees centigrade throughout their life histories. Evolution this cold environment has led to unusual physiological and biochemical characteristics. In some cases, the characteristics contribute to overcoming constraints of cold temperature on biological processes. In other instances, mutations that probably would have been lethal in warmer, less oxygen-rich environments than the Southern Ocean have been retained in Antarctic fishes. This research project focuses on three major objectives that exploit these unusual conditions to identify mechanisms compatible with normal cellular function at cold temperature and to gain unique insights into the physiological roles of key intracellular proteins. The three lines of study proposed are the molecular basis for the failure of the myoglobin encoding gene to be expressed in certain Antarctic notothenioid fishes, the basis of the substrate specificity of the enzyme fatty acyl-CoA synthetase that is involved in the catabolism of fatty acids, and the functional roles played by different isoforms of creatine phosphokinase in locomotory muscle of Antarctic fish. Results from this study will not only provide insight into the evolutionary biology of the Antarctic notothenioid fishes, but will elucidate important general principles that are applicable to widely different taxa beyond the Antarctic.
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Sidell, Bruce and Vayda, Michael E., "Proteins of Oxygen-Binding and Energy Metabolism in Muscles of Antarctic Fishes: Evolutionary Adjustments to Life at Cold Temperature" (2003). University of Maine Office of Research Administration: Grant Reports. 104.
Other Collaborators or Contacts
Dr. Stuart Egginton, Department of Physiology, University of Birmingham, England