CCTδ colocalizes with actin and β-tubulin: Insight into its involvement in the cytoskeleton formation of the intracellular parasite Nosema bombycis.
CCT
Chaperonin
Immunolocalization
Nosema bombycis
RNAi
Journal
Journal of invertebrate pathology
ISSN: 1096-0805
Titre abrégé: J Invertebr Pathol
Pays: United States
ID NLM: 0014067
Informations de publication
Date de publication:
09 2021
09 2021
Historique:
received:
24
04
2021
revised:
27
06
2021
accepted:
05
07
2021
pubmed:
14
7
2021
medline:
30
11
2021
entrez:
13
7
2021
Statut:
ppublish
Résumé
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.
Identifiants
pubmed: 34256048
pii: S0022-2011(21)00113-0
doi: 10.1016/j.jip.2021.107646
pii:
doi:
Substances chimiques
Actins
0
Fungal Proteins
0
Tubulin
0
Chaperonin Containing TCP-1
EC 3.6.1.-
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
107646Informations de copyright
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