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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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A Chlamydomonas homologue of the putative murine t complex distorter Tctex-2 is an outer arm dynein light chain.

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]

References

  1. A Chlamydomonas homologue of the putative murine t complex distorter Tctex-2 is an outer arm dynein light chain. Patel-King, R.S., Benashski, S.E., Harrison, A., King, S.M. J. Cell Biol. (1997) [Pubmed]
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