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Published online 12 December 2005. doi:10.1083/jcb.200508184
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 171, Number 6, 1035-1044
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Article

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



Yuhua Shang, Che-Chia Tsao, and Martin A. Gorovsky

Department of Biology, University of Rochester, Rochester, NY 14627

Correspondence to Martin A. Gorovsky: goro{at}mail.rochester.edu

We have used in vitro mutagenesis and gene replacement to study the function of the nucleotide-binding domain (NBD) of {gamma}-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 {gamma}-tubulin is normally suppressed by a negative regulatory mechanism that acts through its NBD.

Abbreviations used in this paper: BB, basal body; GDP, guanosine diphosphate; KF, kinetodesmal fiber; ML, M loop; MT, microtubule; MTOC, MT-organizing center; NBD, nucleotide-binding domain; OA, oral apparatus.


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