KMID : 0381120060280040361
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Genes and Genomics 2006 Volume.28 No. 4 p.361 ~ p.368
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Characterization of the Heat Shock Protein 60 and 10 Genes and their Bidirectional Promoter Region in Olive Flounder (Paralichthys olivaceus)
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Nam Bo-Hye
Kim Bong-Seok Kim Young-Ok Lee Sang-Jun Jee Young-Ju Lim Sang-Uk Cho Yong-Chul Chung Jae-Hun
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Abstract
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Heat shock protein (HSP) 60 and 10 are stress-inducible mitochondrial matrix proteins that form an important chaperonin complex for mitochondrial protein folding and function. Extensive studies on model fish species have revealed molecular chaperones, such as HSP90, HSP70, and low molecular weight HSP (16?47 kDa), but the study of chaperonins in fish has not yet been conducted. We present the full sequence of the HSP60 and HSP10 genes for the teleost olive flounder (Paralichthys olivaceus), which were found to be linked head-to-head comprising approximately 10 kb and consisting of 11 and 4 exons, respectively. Using a luciferase?reporter assay, we demonstrated that the region between the two genes functions as a bidirectional promoter. The nucleotide variations detected are localized in a putative CCAAT-box in the bidirectional promoter region, and analysis of the transcriptional activity of the promoter fragment with these variations showed that it affects transcriptional levels.
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KEYWORD
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HSP10, HSP60, bidirectional promoter, luciferase activity, Paralichthys olivaceus
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