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Partially functional outer-arm dynein in a novel Chlamydomonas mutant expressing a truncated gamma heavy chain.
- Source :
-
Eukaryotic cell [Eukaryot Cell] 2008 Jul; Vol. 7 (7), pp. 1136-45. Date of Electronic Publication: 2008 May 16. - Publication Year :
- 2008
-
Abstract
- The outer dynein arm of Chlamydomonas flagella contains three heavy chains (alpha, beta, and gamma), each of which exhibits motor activity. How they assemble and cooperate is of considerable interest. Here we report the isolation of a novel mutant, oda2-t, whose gamma heavy chain is truncated at about 30% of the sequence. While the previously isolated gamma chain mutant oda2 lacks the entire outer arm, oda2-t retains outer arms that contain alpha and beta heavy chains, suggesting that the N-terminal sequence (corresponding to the tail region) is necessary and sufficient for stable outer-arm assembly. Thin-section electron microscopy and image analysis localize the gamma heavy chain to a basal region of the outer-arm image in the axonemal cross section. The motility of oda2-t is lower than that of the wild type and oda11 (lacking the alpha heavy chain) but higher than that of oda2 and oda4-s7 (lacking the motor domain of the beta heavy chain). Thus, the outer-arm dynein lacking the gamma heavy-chain motor domain is partially functional. The availability of mutants lacking individual heavy chains should greatly facilitate studies on the structure and function of the outer-arm dynein.
- Subjects :
- Adenosine Triphosphatases chemistry
Adenosine Triphosphatases genetics
Adenosine Triphosphatases metabolism
Animals
Blotting, Western
Chlamydomonas chemistry
Chlamydomonas genetics
Chlamydomonas physiology
Dyneins chemistry
Dyneins genetics
Dyneins ultrastructure
Flagella chemistry
Flagella genetics
Flagella physiology
Protein Subunits chemistry
Protein Subunits genetics
Protein Subunits metabolism
Protozoan Proteins chemistry
Protozoan Proteins genetics
Protozoan Proteins ultrastructure
Chlamydomonas enzymology
Dyneins metabolism
Flagella enzymology
Mutation
Protozoan Proteins metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1535-9786
- Volume :
- 7
- Issue :
- 7
- Database :
- MEDLINE
- Journal :
- Eukaryotic cell
- Publication Type :
- Academic Journal
- Accession number :
- 18487347
- Full Text :
- https://doi.org/10.1128/EC.00102-08