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A novel subunit of axonemal dynein conserved among lower and higher eukaryotes
Author(s) -
Yamamoto Ryosuke,
Yanagisawa Haru-aki,
Yagi Toshiki,
Kamiya Ritsu
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2006.10.047
Subject(s) - dynein , flagellum , cilium , intraflagellar transport , biology , protein subunit , chlamydomonas , dynactin , microbiology and biotechnology , microtubule , immunoprecipitation , axoneme , immunoglobulin light chain , mutant , genetics , gene , antibody
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.