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Article Abstract
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 CCTη of N. bombycis (NbCCTη) for the first time. Immunoprecipitations and mass spectrometry (IP-MS) of NbCCTη analysis showed that NbBip may interact with CCT subunits. Yeast two-hybrid assays validated that NbBip interacts with NbCCTη, as well as NbCCTα and NbCCTε. Furthermore, RNA interference on NbBip brought about radical expression of NbCCTα, NbCCTε, and NbCCTη, while RNAi on NbCCT subunits resulted in abnormal expression of NbBip. Immunofluorescence assay results showed that NbBip colocalized with NbCCTα and NbCCTη, and CCTη colocalized with Nbβ-tubulin and Nbactin in the parasite. Collectively, these findings suggest that NbBip may act as a crucial factor in the subunit-folding and assembly of CCT complex in N. bombycis.
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| http://dx.doi.org/10.1016/j.ijbiomac.2024.138971 | DOI Listing |
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