Molecular characterization and expression analysis of heat shock proteins 40, 70 and 90 from kuruma shrimp <Emphasis Type="Italic">Marsupenaeus japonicus</Emphasis> |
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Authors: | Threechada Danwattananusorn Fernand F Fagutao Aiko Shitara Hidehiro Kondo Takashi Aoki Reiko Nozaki Ikuo Hirono |
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Institution: | (1) Laboratory of Genome Science, Tokyo University of Marine Science and Technology, Konan 4-5-7, Minato-ku, Tokyo 108-8477, Japan; |
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Abstract: | Heat shock proteins (HSPs) are proteins that are expressed more strongly when the cells are exposed to physiological and stressful
conditions. In this study, the full-length cDNAs of heat shock proteins 40 (MjHSP40), 70 (MjHSP70) and 90 (MjHSP90) were cloned from kuruma shrimp Marsupenaeus japonicus. The open reading frames (ORFs) of the cDNA clones have lengths of 1,191, 1,959 and 2,172 bp and encode 396, 652 and 723
amino acid residues, respectively. The predicted MjHSP40 amino acid sequence contains a J domain, a glycine/phenylalanine-rich region, and a central domain containing four repeats
of a CxxCxGxG motif, indicating that it is a type I HSP40 homolog. The signature sequences of the HSP70 and HSP90 gene families
are conserved in the MjHSP70 and MjHSP90 amino acid sequences. The deduced amino acid sequences of MjHSP70 and MjHSP90 share high identity with previously reported shrimp HSP70s and HSP90s, respectively. The expression of MjHSP90 mRNA increased at 32°C. Additionally, the expressions of MjHSP40, MjHSP70 and MjHSP90 mRNAs increased in defense-related tissues (i.e., hemocytes and lymphoid organ) when the shrimp were challenged with
white spot syndrome virus. |
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