Chlamydomonas Flagellar Outer Row Dynein Assembly Protein Oda7 Interacts with Both Outer Row and I1 Inner Row Dyneins
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چکیده
منابع مشابه
Chlamydomonas flagellar outer row dynein assembly protein ODA7 interacts with both outer row and I1 inner row dyneins.
We previously found that a mutation at the ODA7 locus in Chlamydomonas prevents axonemal outer row dynein assembly by blocking association of heavy chains and intermediate chains in the cytoplasm. We have now cloned the ODA7 locus by walking in the Chlamydomonas genome from nearby molecular markers, confirmed the identity of the gene by rescuing the mutant phenotype with genomic clones, and ide...
متن کاملThe ODA6 locus of Chlamydomonas reinhardtii encodes a 70 kDa intermediate chain protein of the flagellar outer row dynein ATPase, and mutations at this locus prevent assembly of the entire outer row dynein arm
Dynein ATPases constitute a growing class of microtubuleassociated molecular motors. Although first characterized as force generators in cilia and flagella, dyneins are also cytoplasmic motor proteins with potential roles in axonal transport (Vallee et al., 1988), intracellular organization (Scholey et al., 1984; Lacey and Haimo, 1992) and mitosis (Pfarr et al ., 1990; Steuer et al ., 1990). Wh...
متن کاملKinetic properties of microtubule-activated 13 S and 21 S dynein ATPases. Evidence for allosteric behaviour associated with the inner row and outer row dynein arms.
The 13 S and 21 S dynein ATPases from Tetrahymena cilia rebind to extracted doublet microtubules as inner row and outer row arms. Rebinding is accompanied by four- to ninefold activation of the ATPase activity. The soluble (microtubule-free) forms of the two dyneins exhibit simple saturation kinetics (h = 1.0) with Vmax much less than mumol Pi mg-1 min-1 and Km = 20-40 microM-ATP. Mixing a fixe...
متن کاملODA16 aids axonemal outer row dynein assembly through an interaction with the intraflagellar transport machinery
Formation of flagellar outer dynein arms in Chlamydomonas reinhardtii requires the ODA16 protein at a previously uncharacterized assembly step. Here, we show that dynein extracted from wild-type axonemes can rebind to oda16 axonemes in vitro, and dynein in oda16 cytoplasmic extracts can bind to docking sites on pf28 (oda) axonemes, which is consistent with a role for ODA16 in dynein transport, ...
متن کاملRebinding of Tetrahymena 13 S and 21 S dynein ATPases to extracted doublet microtubules. The inner row and outer row dynein arms.
Ciliary axonemes from Tetrahymena contain a second salt-extractable ATPase distinguishable from outer arm 21 S dynein by sedimentation velocity (congruent to 13 S), electrophoretic mobility and substrate specificity. As characterized by turbidimetric assay, gel electrophoresis in the presence of sodium dodecyl sulphate, ATPase activity and electron microscopy, the 13 S dynein ATPase rebinds to ...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2007
ISSN: 0021-9258
DOI: 10.1074/jbc.m607509200