Chlamydomonas flagellar outer row dynein assembly protein Oda7 interacts with both outer row and I1 inner row dyneins
Chlamydomonas flagellar outer row dynein assembly protein Oda7 interacts with both outer row and I1 inner row dyneins
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DOI：
10.1074/jbc.m607509200
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发表时间：
2007-02-23
影响因子：
4.8
通讯作者：
Mitchell, David R.
中科院分区：
文献类型：
--
作者：
Freshour, Judy;Yokoyama, Ruth;Mitchell, David R.
我们之前发现衣藻ODA7位点的突变通过阻断细胞质中重链和中间链的结合来阻止轴丝外排动力蛋白的组装。我们现在通过从附近的分子标记在衣藻基因组中行走来克隆 ODA 7 基因座，通过用基因组克隆拯救突变表型来确认该基因的身份，并将 ODA7 基因产物鉴定为与外排动力蛋白 LC1 无关的 58 kDa 富含亮氨酸的重复蛋白。 Oda7p 在 oda7 突变体鞭毛中缺失，但存在于其他外行或内行动力蛋白组装突变体的鞭毛中。然而，在缺乏外排动力蛋白和内排 11 动力蛋白的鞭毛中，Oda7 水平大大降低。生化分馏和重新结合研究支持了一种模型，其中 Oda7 参与了内排动力蛋白和外排动力蛋白之间先前未表征的结构连接。
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 ODA 7 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 identified the ODA7 gene product as a 58-kDa leucine-rich repeat protein unrelated to outer row dynein LC1. Oda7p is missing from oda7 mutant flagella but is present in flagella of other outer row or inner row dynein assembly mutants. However, Oda7 levels are greatly reduced in flagella that lack both outer row dynein and inner row 11 dynein. Biochemical fractionation and rebinding studies support a model in which Oda7 participates in a previously uncharacterized structural link between inner and outer row dyneins.