September 2002-August 2006
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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 pattern of cardiac myoglobin expression in the Suborder Notothenoidei. Previous work has indicated a variable pattern of presence or absence of the intracellular oxygen-binding protein, myoglobin (Mb), in hearts of one family of Antarctic notothenioid fishes (Channichthyidae; icefishes). Because Mb is of physiological value in species that express the protein, the observed pattern of interspecific expression has been attributed to unusually low niche competition in the Southern Ocean. This leads to the prediction that similar loss of cardiac Mb should be observed in other notothenioid taxa. This part of the project will survey for the presence and absence of cardiac Mb in as many notothenioid species as possible and, if Mb-lacking species are detected, will extend analyses to determine the mechanism(s) responsible for loss of its expression using molecular biological techniques.
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Sidell, Bruce, "Cold Body Temperature as an Evolutionary Shaping Force in the Physiology of Antarctic Fishes" (2006). University of Maine Office of Research and Sponsored Programs: Grant Reports. 197.