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© The Rockefeller University Press, 0021-9525/1997//1081 $5.00
The Journal of Cell Biology, Volume 137, Number 5, , 1997 1081-1090

Article

A Chlamydomonas Homologue of the Putative Murine t Complex Distorter Tctex-2 Is an Outer Arm Dynein Light Chain



Ramila S. Patel-King, Sharon E. Benashski, Alistair Harrison, and Stephen M. King

Department of Biochemistry, University of Connecticut Health Center, Farmington, Connecticut 06032-3305

Molecular analysis of a 19,000-Mr protein from the Chlamydomonas flagellum reveals that it is homologous to the t complex–encoded protein Tctex-2, which is a candidate for one of the distorter products that cause the extreme transmission ratio distortion (meiotic drive) of the murine t complex. The 19,000-Mr protein is extracted from the axoneme with 0.6 M NaCl and comigrates with the outer dynein arm in sucrose density gradients. This protein also is specifically missing in axonemes prepared from a mutant that does not assemble the outer arm. These data raise the possibility that Tctex-2 is a sperm flagellar dynein component. Combined with the recent identification of Tctex-1 (another distorter candidate) as a light chain of cytoplasmic dynein, these results lead to a biochemical model for how differential defects in spermiogenesis that result in the phenomenon of meiotic drive might be generated in wild-type vs t-bearing sperm.

1. Abbreviations used in this paper: DHC, dynein heavy chain; IC, intermediate chain; LC, light chain; MBP, maltose binding protein.

Please address all correspondence to Stephen M. King, Department of Biochemistry, University of Connecticut Health Center, 263 Farmington Avenue, Farmington, CT 06032-3305. Tel.: (860) 679-3347. Fax: (860) 6793408. e-mail: king{at}panda.uchc.edu


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