CCTα and CCTδ chaperonin subunits are essential and required for cilia assembly and maintenance in Tetrahymena

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Abstract

Background: The eukaryotic cytosolic chaperonin CCT is a hetero-oligomeric complex formed by two rings connected back-to-back, each composed of eight distinct subunits (CCTα to CCTζ). CCT complex mediates the folding, of a wide range of newly synthesised proteins including tubulin (α, β and γ) and actin, as quantitatively major substrates. Methodology/Principal Findings: We disrupted the genes encoding CCTα and CCTδ subunits in the ciliate Tetrahymena. Cells lacking the zygotic expression of either CCTα or CCTδ showed a loss of cell body microtubules, failed to assemble new cilia and died within 2 cell cycles. We also show that loss of CCT subunit activity leads to axoneme shortening and splaying of tips of axonemal microtubules. An epitope-tagged CCTα rescued the gene knockout phenotype and localized primarily to the tips of cilia. A mutation in CCTα, G346E, at a residue also present in the related protein implicated in the Bardet Biedel Syndrome, BBS6, also caused defects in cilia and impaired CCTα localization in cilia. Conclusions/Significance: Our results demonstrate that the CCT subunits are essential and required for ciliary assembly and maintenance of axoneme structure, especially at the tips of cilia.

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Seixas, C., Cruto, T., Tavares, A., Gaertig, J., & Soares, H. (2010). CCTα and CCTδ chaperonin subunits are essential and required for cilia assembly and maintenance in Tetrahymena. PLoS ONE, 5(5). https://doi.org/10.1371/journal.pone.0010704

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