Expression and structure of stress chaperon hsp90 in terrestrial decapods, <i>Coenobita</i> (Anomura: Coenobitidae) and <i>Chiromantes</i> (Brachyura: Sesarmidae)

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  • Gusev Oleg
    Laboratory of Behavior, Evolution, and Environment, Graduate School of Natural Science and Technology, Okayama University
  • Ziegler Tracy A.
    Nicholas School of the Environment and Earth Sciences, Duke University Marine Laboratory
  • Saigusa Masayuki
    Laboratory of Behavior, Evolution, and Environment, Graduate School of Natural Science and Technology, Okayama University

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<p>This study describes aspects of the biology of heat shock proteins 90kDa (hsp90) in terrestrial decapods, Coenobita purpureus, C. brevimanus (Anomura: Coenobitidae) and Chiromantes haematocheir (Brachyura: Sesarmidae). These species possess highly developed terrestrial adaptations on both morphological and physiological levels. We have analyzed the pattern of expression for the gene coding hsp90: molecular chaperon in both embryos and the muscle tissues of adults of these species in response to heat stress. While the minimum temperature for initiation of the synthesis of excess of hsp90 mRNA was different between embryos and adults from the different climatic regions, the range of resistance to high temperature shock was nearly the same (6-7℃). Furthermore, the structure of the stress-factor binding domain in hsp90 coding gene showed convergent patterns by possessing a conservative amino acid sequence in decapods experiencing the same annual temperature regimes in the subtropical, temperate and boreal climatic regions.</p>

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