Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Animals
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Bacterial Proteins / genetics*
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Base Sequence
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Blotting, Northern
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Blotting, Southern
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Chaperonins / chemistry
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Chaperonins / genetics
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Chlamydomonas reinhardtii / chemistry*
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Chlamydomonas reinhardtii / genetics
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Cloning, Molecular
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DNA Primers
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DNA, Plant / analysis
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Dyneins / chemistry
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Dyneins / genetics*
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Intracellular Signaling Peptides and Proteins*
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Male
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Mice
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Microtubule-Associated Proteins*
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Molecular Sequence Data
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Nuclear Proteins / chemistry
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Nuclear Proteins / genetics*
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RNA, Messenger / analysis
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Sequence Homology, Amino Acid
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Sperm Motility / physiology
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Sperm Tail / chemistry
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Ubiquitin-Protein Ligases
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t-Complex Genome Region
Substances
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Bacterial Proteins
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DNA Primers
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DNA, Plant
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Dynlt1b protein, mouse
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Intracellular Signaling Peptides and Proteins
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Microtubule-Associated Proteins
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Nuclear Proteins
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RNA, Messenger
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light chain protein p28, Chlamydomonas
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PPP1R11 protein, human
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Ubiquitin-Protein Ligases
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Chaperonins
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Dyneins