标题：Heat shock protein 90 maintains the stability and function of transcription factor Broad Z7 by interacting with its Broad-Complex-Tramtrack-Bric-a-brac domain
作者：Cai, M. -J.;Li, X. -R.;Pei, X. -Y.;Liu, W.;Wang, J. -X.;Zhao, X. -F.
作者机构：[Cai, M.-J] Shandong Provincial Key Laboratory of Animal Cells and Developmental Biology, School of Life Science, Shandong University, Jinan, 250100, 更多
通讯作者地址：[Zhao, XF]Shandong Univ, Sch Life Sci, Shandong Prov Key Lab Anim Cells & Dev Biol, Jinan 250100, Peoples R China.
来源：Insect Molecular Biology
关键词：Hsp90;BrZ7;BTB domain;middle domain;degradation
摘要：Heat shock protein 90 (Hsp90) is a highly conserved chaperone protein that interacts with various client proteins to mediate their folding and stability. The Broad-Complex-Tramtrack-Bric-a-brac (BTB) domain, also known as poxvirus and zinc finger (POZ) domain, exists widely in different proteins and is highly conserved. However, the stability mechanism of BTB domain-containing proteins has not been fully understood. Co-immunoprecipitation and a protein pull-down assay were performed to investigate the interaction between Hsp90 and the transcription factor Broad isoform Z7 (BrZ7) in vivo and in vitro. The middle domain of Hsp90 directly associated with the BTB domain of BrZ7. The Hsp90 inhibitor 17-(Allylamino)-17-demethoxygeldanamycin (17-AAG) interrupted the interaction between Hsp90 and BrZ7 and decreased the protein level of BrZ7 but did not affect the mRNA level of BrZ7. The addition of the proteasome inhibitor peptide aldehyde Cbz-leu-leu leucinal suppressed the 17-AAG-induced degradation of BrZ7. BTB domain deletion and 17-AAG treatment resulted in inhibition of BrZ7 function in gene expression in the 20-hydroxyecdysone and juvenile hormone pathways. These results reveal that the middle domain of Hsp90 associates with the BTB domain of BrZ7 to prevent BrZ7 degradation and maintain BrZ7 function in gene expression in the lepidopteran insect Helicoverpa armigera.