Molecular cloning of silkworm Cdc37 and its interaction with Hsp90 chaperone

Jun Yamashita, Yoshitaka Miyagawa, Ryohei Sugahara, Hiroaki Mon, Hitoshi Mitsunobu, Jae Man Lee, Yutaka Kawaguchi, Takahiro Kusakabe

Research output: Contribution to journalArticlepeer-review

7 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)137-143
Number of pages7
JournalJournal of Insect Biotechnology and Sericology
Issue number3
Publication statusPublished - Oct 2007

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Applied Microbiology and Biotechnology
  • General Business,Management and Accounting
  • General Agricultural and Biological Sciences
  • Insect Science
  • Industrial and Manufacturing Engineering


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