Utilize este identificador para referenciar este registo: http://hdl.handle.net/10400.21/3043
Título: CCTα and CCTδ chaperonin subunits are essential and required for cilia assembly and maintenance in Tetrahymena
Autor: Seixas, Cecília
Cruto, Teresa
Tavares, Alexandra
Gaertig, Jacek
Soares, Helena
Palavras-chave: Amino acid substitution/genetics
Axoneme/metabolism
Axoneme/pathology
Chaperonin containing TCP-1/metabolism
Cilia/metabolism
Epitopes/metabolism
Gene Knockout techniques
Microtubules/metabolism
Mutation/genetics
Protein subunits/metabolism
Recombinant fusion proteins
Temperature
Tetrahymena
Zygote
Data: Mai-2010
Editora: PLoS
Citação: Seixas C, Cruto T, Tavares A, Gaertig J, Soares H. CCTα and CCTδ chaperonin subunits are essential and required for cilia assembly and maintenance in Tetrahymena. PLoS One. 2010;5(5):e10704.
Resumo: 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 (CCTalpha to CCTzeta). 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 CCTalpha and CCTdelta subunits in the ciliate Tetrahymena. Cells lacking the zygotic expression of either CCTalpha or CCTdelta 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 CCTalpha rescued the gene knockout phenotype and localized primarily to the tips of cilia. A mutation in CCTalpha, G346E, at a residue also present in the related protein implicated in the Bardet Biedel Syndrome, BBS6, also caused defects in cilia and impaired CCTalpha 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.
Peer review: yes
URI: http://hdl.handle.net/10400.21/3043
ISSN: 1932-6203
Versão do Editor: http://www.plosone.org/article/info%3Adoi%2F10.1371%2Fjournal.pone.0010704
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