Molecular characterization and induction of heat shock protein 90 in the Antarctic bivalve Laternula elliptica
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...
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ftpubmed:oai:pubmedcentral.nih.gov:2728271 2023-05-15T13:33:18+02:00 Molecular characterization and induction of heat shock protein 90 in the Antarctic bivalve Laternula elliptica Kim, Meesun Ahn, In-Young Kim, Hakjun Cheon, Jina Park, Hyun 2008-11-06 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2728271 http://www.ncbi.nlm.nih.gov/pubmed/18987993 https://doi.org/10.1007/s12192-008-0090-9 en eng Springer Netherlands http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2728271 http://www.ncbi.nlm.nih.gov/pubmed/18987993 http://dx.doi.org/10.1007/s12192-008-0090-9 © Cell Stress Society International 2008 Original Paper Text 2008 ftpubmed https://doi.org/10.1007/s12192-008-0090-9 2013-09-02T15:49:48Z 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. Text Antarc* Antarctic PubMed Central (PMC) Antarctic The Antarctic Cell Stress and Chaperones 14 4 363 370 |
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Original Paper |
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Original Paper Kim, Meesun Ahn, In-Young Kim, Hakjun Cheon, Jina Park, Hyun Molecular characterization and induction of heat shock protein 90 in the Antarctic bivalve Laternula elliptica |
topic_facet |
Original Paper |
description |
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. |
format |
Text |
author |
Kim, Meesun Ahn, In-Young Kim, Hakjun Cheon, Jina Park, Hyun |
author_facet |
Kim, Meesun Ahn, In-Young Kim, Hakjun Cheon, Jina Park, Hyun |
author_sort |
Kim, Meesun |
title |
Molecular characterization and induction of heat shock protein 90 in the Antarctic bivalve Laternula elliptica |
title_short |
Molecular characterization and induction of heat shock protein 90 in the Antarctic bivalve Laternula elliptica |
title_full |
Molecular characterization and induction of heat shock protein 90 in the Antarctic bivalve Laternula elliptica |
title_fullStr |
Molecular characterization and induction of heat shock protein 90 in the Antarctic bivalve Laternula elliptica |
title_full_unstemmed |
Molecular characterization and induction of heat shock protein 90 in the Antarctic bivalve Laternula elliptica |
title_sort |
molecular characterization and induction of heat shock protein 90 in the antarctic bivalve laternula elliptica |
publisher |
Springer Netherlands |
publishDate |
2008 |
url |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2728271 http://www.ncbi.nlm.nih.gov/pubmed/18987993 https://doi.org/10.1007/s12192-008-0090-9 |
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Antarctic The Antarctic |
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Antarctic The Antarctic |
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Antarc* Antarctic |
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Antarc* Antarctic |
op_relation |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2728271 http://www.ncbi.nlm.nih.gov/pubmed/18987993 http://dx.doi.org/10.1007/s12192-008-0090-9 |
op_rights |
© Cell Stress Society International 2008 |
op_doi |
https://doi.org/10.1007/s12192-008-0090-9 |
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Cell Stress and Chaperones |
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14 |
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4 |
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370 |
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