AI Article Synopsis
- CCT is a molecular chaperone protein essential for folding newly synthesized proteins and consists of eight different subunits, with δ subunit playing a key role in cytoskeleton protein assembly.
- The study identifies NbCCTδ in the microsporidian Nosema bombycis, revealing a gene length of 1497 bp that encodes a 498 amino acid protein.
- NbCCTδ is expressed throughout N. bombycis' lifecycle, particularly during early proliferation, and is found to colocalize with actin and β-tubulin, suggesting its involvement in cytoskeleton formation and proliferation.
Article Abstract
The chaperonin-containing t-complex polypeptide 1 (CCT) is a molecular chaperone protein that is widely present in eukaryotic cytoplasm and can assist in the folding of newly synthesized proteins. The CCT complex consists of eight completely different subunits, among which the δ subunit plays an extremely important role in the folding and assembly of cytoskeleton proteins as an individual or complex with other subunits. In this study, we identified the CCTδ in the microsporidian Nosema bombycis (NbCCTδ) for the first time. The NbCCTδ gene contains a complete ORF of 1497 bp in length that encodes a 498 amino acid polypeptide. NbCCTδ is expressed throughout the entire lifecycle of N. bombycis and rather higher in early stage of proliferation. Indirect immunofluorescence results showed that NbCCTδ was colocalized with actin and β-tubulin during the proliferative and sporogonic phases of N. bombycis. RNA interference down-regulated the expression of the NbCCTδ gene. These results imply that NbCCTδ may participate in cytoskeleton formation and proliferation of N. bombycis.
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| http://dx.doi.org/10.1016/j.jip.2021.107646 | DOI Listing |
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