Journal
FEBS LETTERS
Volume 580, Issue 27, Pages 6357-6360Publisher
WILEY
DOI: 10.1016/j.febslet.2006.10.047
Keywords
inner arm dynein; light chain; p28; actin; Chlamydomonas
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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. (c) 2006 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.
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