Glucose-regulated protein 78 regulates the subunit-folding of the CCT complex by modulating gene expression and protein interaction in the microsporidian Nosema bombycis

文献类型： 外文期刊

第一作者： Xu, Sheng

作者： Xu, Sheng;Xiao, Shengyan;Qi, Jingru;Yao, Mingshuai;He, Ping;Wang, Runpeng;Wei, Erjun;Wang, Qiang;Zhang, Yiling;Tang, Xudong;Shen, Zhongyuan;Wang, Qiang;Zhang, Yiling;Tang, Xudong;Shen, Zhongyuan

作者机构：

关键词： Microsporidia; Nosema bombycis; CCT complex; Bip (GRP78); Interaction; Immunolocalization

期刊名称：INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES （ 影响因子：8.5； 五年影响因子：8.7 ）

ISSN： 0141-8130

年卷期： 2025 年 290 卷

页码：

收录情况： SCI

摘要： Chaperonin containing tailless complex polypeptide 1 (CCT) functions as a molecular chaperone and is essential for ensuring proper protein folding. Glucose-regulated protein 78 (GRP78/Bip), also a type of chaperone, not only assists in folding of proteins, but also facilitates the transportation of proteins into the endoplasmic reticulum (ER) via the Sec protein complex. In this study, we identified the CCT ) of N. bombycis (NbCCT )) for the first time. Immunoprecipitations and mass spectrometry (IP-MS) of NbCCT ) analysis showed that NbBip may interact with CCT subunits. Yeast two-hybrid assays validated that NbBip interacts with NbCCT ), as well as NbCCT alpha and NbCCTs. Furthermore, RNA interference on NbBip brought about radical expression of NbCCT alpha, NbCCT epsilon, and NbCCT eta, while RNAi on NbCCT subunits resulted in abnormal expression of NbBip. Immunofluorescence assay results showed that NbBip colocalized with NbCCT alpha and NbCCT ), and CCT ) colocalized with Nb beta-tubulin and Nbactin in the parasite. Collectively, these findings suggest that NbBip may act as a crucial factor in the subunitfolding and assembly of CCT complex in N. bombycis.

分类号：

  • 相关文献
作者其他论文 更多>>

微信小程序