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

研究成果: Contribution to journalArticle査読

7 被引用数 (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.

ジャーナルJournal of Insect Biotechnology and Sericology
出版ステータス出版済み - 10 1 2007

All Science Journal Classification (ASJC) codes

  • バイオテクノロジー
  • 応用微生物学とバイオテクノロジー
  • ビジネス、管理および会計(全般)
  • 農業および生物科学(全般)
  • 昆虫科学
  • 産業および生産工学


「Molecular cloning of silkworm Cdc37 and its interaction with Hsp90 chaperone」の研究トピックを掘り下げます。これらがまとまってユニークなフィンガープリントを構成します。