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Originally published as MBC in Press, 10.1091/mbc.E02-01-0034 on December 25, 2002
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Vol. 14, Issue 3, 1017-1026, March 2003

Characterization of a New gamma TuRC Subunit with WD Repeats

Ruwanthi N. Gunawardane, Ona C. Martin, and Yixian Zheng*

Carnegie Institution of Washington/Howard Hughes Medical Institute, Baltimore, Maryland 21210

The gamma -tubulin ring complex (gamma TuRC), 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 coexpression 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. Coexpression 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.

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

Molecular Biology of the Cell
Vol. 14, 1017-1026, March 2003
Copyright © 2003 by The American Society for Cell Biology


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