Mutations in the "dynein regulatory complex" alter the ATP-insensitive binding sites for inner arm dyneins in Chlamydomonas axonemes.
Mutations in the "dynein regulatory complex" alter the ATP-insensitive binding sites for inner arm dyneins in Chlamydomonas axonemes.
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DOI：
10.1083/jcb.125.5.1109
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发表时间：
1994-06
期刊：
影响因子：
--
通讯作者：
Moscatelli A
中科院分区：
文献类型：
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作者：
Piperno G;Mead K;LeDizet M;Moscatelli A
为了了解力蛋白活性沿着和围绕轴丝的调节机制，我们进一步描述了“力蛋白调节复合物”（drc）。缺乏一些轴丝蛋白，这在一起被称为drc，导致抑制鞭毛麻痹的辐射辐条和中央对突变体。drc也是一种适配器，参与I2和I3内部动力蛋白臂与双联体微管的ATP不敏感结合。支持这些结论的证据是通过分析五个drc突变体：pf 2，pf 3，suppf 3，suppf 4和suppf 5获得的。来自drc突变体的轴丝缺乏部分I2和I3内部动力蛋白臂以及七种drc组分的子集（表观分子量为29，000至192，000）。在ATP-Mg的情况下，从相同的突变体动力蛋白耗尽轴丝结合I2和I3内臂在ATP敏感和不敏感的网站。在ATP不敏感位点，它们结合I2和I3内臂的程度取决于DRC缺陷。这一证据表明，drc形成一个结合位点的I2和I3的内臂上的A部分的双微管。
To understand mechanisms of regulation of dynein activity along and around the axoneme we further characterized the "dynein regulatory complex" (drc). The lack of some axonemal proteins, which together are referred to as drc, causes the suppression of flagellar paralysis of radial spoke and central pair mutants. The drc is also an adapter involved in the ATP-insensitive binding of I2 and I3 inner dynein arms to doublet microtubules. Evidence supporting these conclusions was obtained through analyses of five drc mutants: pf2, pf3, suppf3, suppf4, and suppf5. Axonemes from drc mutants lack part of I2 and I3 inner dynein arms as well as subsets of seven drc components (apparent molecular weight from 29,000 to 192,000). In the absence of ATP-Mg, dynein-depleted axonemes from the same mutants bind I2 and I3 inner arms at both ATP-sensitive and -insensitive sites. At ATP-insensitive sites, they bind I2 and I3 inner arms to an extent that depends on the drc defect. This evidence suggested to us that the drc forms one binding site for the I2 and I3 inner arms on the A part of doublet microtubules.