Characterization of a Chlamydomonas insertional mutant that disrupts flagellar central pair microtubule-associated structures.
Characterization of a Chlamydomonas insertional mutant that disrupts flagellar central pair microtubule-associated structures.
复制标题
衣原体插入突变体的表征，该突变体破坏了鞭毛中心对微管相关结构。
DOI：
10.1083/jcb.144.2.293
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发表时间：
1999-01-25
影响因子：
7.8
通讯作者：
Sale, W S
中科院分区：
文献类型：
--
作者：
Mitchell, D R;Sale, W S
两个等位基因在一个新的位点，中央配对相关复合物1（CPC 1），选择在筛选衣原体鞭毛运动突变。这些突变破坏了与中心对微管相关的结构，并降低了鞭毛的跳动频率，但不能阻止与活细胞的疏水反应或趋光积累相关的鞭毛活性的变化。cpc 1和pf 6轴丝的比较表明，cpc 1影响的一排突起沿着C1微管与pf 6中缺失的那些不同，以及一排细纤维，在两个中心对微管之间形成弧形。电子显微镜图像的中央对轴丝从径向发言缺陷株揭示以前未描述的中央对结构，包括向径向辐条头横向延伸的突起，和C2微管和cpc 1投影之间的对角链接。通过SDS-PAGE，cpc 1轴丝显示350-，265-和79-kD蛋白质的减少。当从野生型轴丝中提取时，这三种蛋白质在蔗糖梯度上与其他三种中心对蛋白（135，125和56 kD）在16 S复合物中共沉积。cpc 1的特性提供了新的见解的结构和生物化学的中央对装置，并进入其功能作为一个调节动力蛋白为基础的运动。
Two alleles at a new locus, central pair–associated complex 1 (CPC1), were selected in a screen for Chlamydomonas flagellar motility mutations. These mutations disrupt structures associated with central pair microtubules and reduce flagellar beat frequency, but do not prevent changes in flagellar activity associated with either photophobic responses or phototactic accumulation of live cells. Comparison of cpc1 and pf6 axonemes shows that cpc1 affects a row of projections along C1 microtubules distinct from those missing in pf6, and a row of thin fibers that form an arc between the two central pair microtubules. Electron microscopic images of the central pair in axonemes from radial spoke–defective strains reveal previously undescribed central pair structures, including projections extending laterally toward radial spoke heads, and a diagonal link between the C2 microtubule and the cpc1 projection. By SDS-PAGE, cpc1 axonemes show reductions of 350-, 265-, and 79-kD proteins. When extracted from wild-type axonemes, these three proteins cosediment on sucrose gradients with three other central pair proteins (135, 125, and 56 kD) in a 16S complex. Characterization of cpc1 provides new insights into the structure and biochemistry of the central pair apparatus, and into its function as a regulator of dynein-based motility.