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MBC in Press, published online ahead of print October 17, 2003
Mol. Biol. Cell 10.1091/mbc.E03-06-0418

A more recent version of this article appeared on January 1, 2004
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Submitted on June 18, 2003
Revised on August 25, 2003
Accepted on September 8, 2003

The C. elegans Microtubule Severing Complex MEI-1/MEI-2 Katanin Interacts Differently with Two Superficially Redundant {beta}-tubulin Isotypes

Chenggang Lu1, Martin Srayko2, and Paul E. Mains1*

1 Genes and Development Research Group and Department of Biochemistry and Molecular Biology, University of Calgary, Calgary, Alberta, T2N 4N1 Canada
2 Genes and Development Research Group and Department of Biochemistry and Molecular Biology, University of Calgary, Calgary, Alberta, T2N 4N1 Canada; Max-Planck-Institute of Molecular Cell Biology and Genetics, Pfotenhauerstrasse 108, D-01307 Dresden, Germany

* Corresponding author. E-mail address: mains{at}ucalgary.ca.

The microtubule severing protein complex katanin is required for a variety of important microtubule-base morphological changes in both animals and plants. C. elegans katanin is encoded by the mei-1 and mei-2 genes and is required for oocyte meiotic spindle formation and must be inactivated before the first mitotic cleavage. We identified a mutation, sb26, in the tbb-2 {beta}-tubulin gene that partially inhibits MEI-1/MEI-2 activity: sb26 rescues lethality caused by ectopic MEI-1/MEI-2 expression during mitosis, and sb26 increases meiotic defects in a genetic background where MEI-1/MEI-2 activity is lower than normal. sb26 does not interfere with MEI-1/MEI-2 microtubule localization, suggesting that this mutation likely interferes with severing. Tubulin deletion alleles and RNA mediated interference revealed that TBB-2 and the other germline enriched {beta}-tubulin isotype, TBB-1, are redundant for embryonic viability. However, limiting MEI-1/MEI-2 activity in these experiments revealed that MEI-1/MEI-2 preferentially interacts with TBB-2-containing microtubules. Our results demonstrate that these two superficially redundant {beta}-tubulin isotypes have functionally distinct roles in vivo.




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C. Lu and P. E. Mains
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