A novel subunit of axonemal dynein conserved among lower and higher eukaryotes.
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.
Yamamoto
Ryosuke
R
Department of Biological Sciences, Graduate School of Science, University of Tokyo, 7-3-1 Hongo, Tokyo 113-0033, Japan.
Yanagisawa
Haru-aki
HA
Yagi
Toshiki
T
Kamiya
Ritsu
R
D020418:Algal Proteins / Q000235:genetics* / Q000378:metabolism; D000818:Animals; D002696:Chlamydomonas / Q000235:genetics* / Q000378:metabolism; D002923:Cilia / Q000235:genetics / Q000378:metabolism; D004398:Dyneins / Q000235:genetics* / Q000378:metabolism; D005407:Flagella / Q000235:genetics / Q000378:metabolism; D015800:Protozoan Proteins / Q000235:genetics* / Q000378:metabolism
D020418:Algal Proteins; D015800:Protozoan Proteins; D004398:Dyneins