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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.
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