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MBC in Press, published online ahead of print December 25, 2002
Mol. Biol. Cell 10.1091/mbc.E02-01-0034

A more recent version of this article appeared on March 1, 2003
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Submitted on January 21, 2002
Revised on November 4, 2002
Accepted on November 27, 2002

Characterization of a new {gamma}TuRC subunit with WD repeats

Ruwanthi N. Gunawardane1, Ona C. Martin1, and Yixian Zheng1*

1 Carnegie Institution of Washington/HHMI, Baltimore, Maryland 21210

* Corresponding author. E-mail address: zheng{at}ciwemb.edu.

The {gamma}-Tubulin Ring Complex T({gamma}uRC), consisting of multiple protein subunits, can nucleate microtubule assembly. Although many subunits of the {gamma}TuRC have been identified, a complete set remains to be defined in any organism. In addition, how the subunits interact with each other to assemble into {gamma}TuRC remains largely unknown. Here, we report the characterization of a novel {gamma}TuRC subunit, Drosophila gamma ring protein with WD repeats (Dgp71WD). With the exception of {gamma}-tubulin, Dgp71WD is the only {gamma}TuRC component identified to date that does not contain the grip motifs, which are signature sequences conserved in {gamma}TuRC components. By performing immunoprecipitations after pair-wise co-expression in Sf9 cells, we show that Dgp71WD directly interacts with the grip motif-containing {gamma}TuRC subunits, Dgrips84, 91, 128, and 163, suggesting that Dgp71WD may play a scaffolding role in {gamma}TuRC organization. We also show that Dgrips128 and 163, like Dgrips84 and 91, can interact directly with {gamma}-tubulin. Co-expression of any of these grip motif-containing proteins with {gamma}-tubulin promotes {gamma}-tubulin binding to guanine nucleotide. In contrast, in the same assay Dgp71WD interacts with {gamma}-tubulin but does not facilitate nucleotide binding.




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