Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2052335 | FEBS Letters | 2006 | 4 Pages |
Abstract
To elucidate the subunit composition of axonemal inner-arm dynein, we examined a 38 kDa protein (p38) co-purified with a Chlamydomonas inner arm subspecies, dynein d. We found it is a novel protein conserved among a variety of organisms with motile cilia and flagella. Immunoprecipitation using specific antibody verified its association with a heavy chain, actin and a previously identified light chain (p28). Unexpectedly, mutant axonemes lacking dynein d and other dyneins retained reduced amounts of p38. This finding suggests that p38 is involved in the docking of dynein d to specific loci.
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Authors
Ryosuke Yamamoto, Haru-aki Yanagisawa, Toshiki Yagi, Ritsu Kamiya,