Cell Stress and Chaperones

, Volume 14, Issue 4, pp 363–370 | Cite as

Molecular characterization and induction of heat shock protein 90 in the Antarctic bivalve Laternula elliptica

  • Meesun Kim
  • In-Young Ahn
  • Hakjun Kim
  • Jina Cheon
  • Hyun Park
Original Paper
First Online:
Received:
Accepted:

Abstract

Heat shock protein 90 (HSP90) is a highly conserved molecular chaperone that plays a key role in protein synthesis, folding, denaturation prevention, and signal transduction. We cloned the complete complementary DNA (cDNA) sequence of the Laternula elliptica HSP90. The full-length cDNA was 2,823 bp in size and contained an open reading frame of 2,190 bp that was translated into 729 amino acids with a calculated molecular weight of 83.4 kDa. The deduced amino acid sequence of HSP90 showed the highest homology to Haliotis tuberculata HSP90 (83%). Reverse-transcriptase polymerase chain reaction analysis revealed the presence of HSP90 transcripts in all of the tissues examined. We also studied the transcriptional expression pattern of HSP90 exposed to thermal stress with real-time polymerase chain reaction. The relative expression level of HSP90 messenger RNA was upregulated and peaked at 12 h in the digestive gland and at 24 h in the gills, then dropped progressively.

Keywords

Antarctic Heat shock protein 90 Laternula Thermal stress 
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Notes

Acknowledgments

This study was supported by a Status and Changes of Polar Indicator Species and Coastal/Terrestrial Ecosystems grant (PE08040) funded by the Korea Polar Research Institute (KOPRI) of the Korean Ocean Research & Development Institute (KORDI).

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Copyright information

© Cell Stress Society International 2008

Authors and Affiliations

  • Meesun Kim
    • 1
  • In-Young Ahn
    • 1
  • Hakjun Kim
    • 1
  • Jina Cheon
    • 1
  • Hyun Park
    • 1
  1. 1.Korea Polar Research Institute, Korea Ocean Research and Development Institute (KORDI)IncheonSouth Korea

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