Journal
PLOS ONE
Volume 5, Issue 5, Pages -Publisher
PUBLIC LIBRARY SCIENCE
DOI: 10.1371/journal.pone.0010704
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Funding
- Fundacao para a Ciencia a Tecnologia [PRAXIS XXI/P/BIA/10097/98, PTDC/BIA-BDE/73163/2006]
- NSF [MBC-033965]
- IEFP
- [SFRH/BD/5176/2001]
- Fundação para a Ciência e a Tecnologia [PTDC/BIA-BDE/73163/2006, SFRH/BD/5176/2001] Funding Source: FCT
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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 (CCT alpha to CCT zeta). CCT complex mediates the folding, of a wide range of newly synthesised proteins including tubulin (alpha, beta and gamma) and actin, as quantitatively major substrates. Methodology/Principal Findings: We disrupted the genes encoding CCT alpha and CCT delta subunits in the ciliate Tetrahymena. Cells lacking the zygotic expression of either CCT alpha or CCT delta 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 CCT alpha rescued the gene knockout phenotype and localized primarily to the tips of cilia. A mutation in CCT alpha, G346E, at a residue also present in the related protein implicated in the Bardet Biedel Syndrome, BBS6, also caused defects in cilia and impaired CCT alpha 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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