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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Yamamoto R,Yanagisawa HA,Yagi T,Kamiya Rdoi
10.1016/j.febslet.2006.10.047subject
Has Abstractpub_date
2006-11-27 00:00:00pages
6357-60issue
27eissn
0014-5793issn
1873-3468pii
S0014-5793(06)01274-9journal_volume
580pub_type
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