Molecular Cloning of Silkworm Cdc37 and its Interaction with Hsp90 Chaperone
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- Yamashita Jun
- Laboratory of Silkworm Sciences, Kyushu University Graduate School of Bioresource and Bioenvironmental Sciences
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- Miyagawa Yoshitaka
- Department of Developmental Biology, National Research Institute for Child Health and Development
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- Sugahara Ryohei
- Laboratory of Silkworm Sciences, Kyushu University Graduate School of Bioresource and Bioenvironmental Sciences
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- Mon Hiroaki
- Laboratory of Silkworm Sciences, Kyushu University Graduate School of Bioresource and Bioenvironmental Sciences
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- Mitsunobu Hitoshi
- Laboratory of Silkworm Sciences, Kyushu University Graduate School of Bioresource and Bioenvironmental Sciences
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- Man Lee Jae
- Laboratory of Silkworm Sciences, Kyushu University Graduate School of Bioresource and Bioenvironmental Sciences
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- Kawaguchi Yutaka
- Laboratory of Silkworm Sciences, Kyushu University Graduate School of Bioresource and Bioenvironmental Sciences
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- Kusakabe Takahiro
- Laboratory of Silkworm Sciences, Kyushu University Graduate School of Bioresource and Bioenvironmental Sciences
Bibliographic Information
- Other Title
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- Molecular cloning of silkworm Cdc37 and its interaction with Hsp90 chaperon
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Abstract
Hsp90-Cdc37 chaperone complex facilitates the folding and activation of numerous protein kinases. In this report, we have isolated a cDNA clone coding for the Bombyx mori Cdc37 homologue, BmCdc37, and determined its nucleotide sequence. Its mRNA encodes a polypeptide of 373 amino acid residues, which shares 52% amino acid identity with Drosophila melanogaster Cdc37. RT-PCR analysis revealed that the expression of BmCDC37 mRNA occurred mainly in the testis. Direct interaction of the HA-tagged BmCdc37 with endogenous BmHsp90 was demonstrated by co-immunoprecipitation assay from the cell lysates. Subcellular localization site of HA-BmHsp90 and HA-BmCdc37 was exclusively cytoplasmic. However, anomalous nuclear localization of DsRed-BmHsp90, probably due to interaction with EGFP-fused BmCdc37, was re-adjusted to cytoplasmic localization by heat stress. These results suggested that BmCdc37 interacts with BmHsp90 in vivo and tends to be transported to cytoplasm by stress-induced cellular mechanisms.<br>
Journal
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- Journal of Insect Biotechnology and Sericology
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Journal of Insect Biotechnology and Sericology 76 (3), 3_137-3_143, 2007
The Japanese Society of Sericultural Science
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Details 詳細情報について
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- CRID
- 1390282680173884160
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- NII Article ID
- 130004464136
- 10019767230
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- NII Book ID
- AA11558849
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- ISSN
- 18847978
- 13468073
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- NDL BIB ID
- 8969845
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- Text Lang
- en
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- Data Source
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- JaLC
- NDL
- CiNii Articles
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- Abstract License Flag
- Disallowed