Mutational analyses reveal a novel function of the nucleotide-binding domain of γ-tubulin in the regulation of basal body biogenesis

We have used in vitro mutagenesis and gene replacement to study the function of the nucleotide-binding domain (NBD) of γ-tubulin in Tetrahymena thermophila. In this study, we show that the NBD has an essential function and that point mutations in two conserved residues lead to over-production and mi...

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Detalles Bibliográficos
Autores principales: Shang, Yuhua, Tsao, Che-Chia, Gorovsky, Martin A.
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 2005
Materias:
Research Articles
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2171320/
https://www.ncbi.nlm.nih.gov/pubmed/16344310
http://dx.doi.org/10.1083/jcb.200508184
Descripción
Sumario:We have used in vitro mutagenesis and gene replacement to study the function of the nucleotide-binding domain (NBD) of γ-tubulin in Tetrahymena thermophila. In this study, we show that the NBD has an essential function and that point mutations in two conserved residues lead to over-production and mislocalization of basal body (BB) assembly. These results, coupled with previous studies (Dammermann, A., T. Muller-Reichert, L. Pelletier, B. Habermann, A. Desai, and K. Oegema. 2004. Dev. Cell. 7:815–829; La Terra, S., C.N. English, P. Hergert, B.F. McEwen, G. Sluder, and A. Khodjakov. 2005. J. Cell Biol. 168:713–722), suggest that to achieve the precise temporal and spatial regulation of BB/centriole assembly, the initiation activity of γ-tubulin is normally suppressed by a negative regulatory mechanism that acts through its NBD.

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