The substructure of isolated and in situ outer dynein arms of sea urchin sperm flagella.
The substructure of isolated and in situ outer dynein arms of sea urchin sperm flagella.
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DOI：
10.1083/jcb.101.4.1400
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发表时间：
1985-10
期刊：
影响因子：
--
通讯作者：
Heuser JE
中科院分区：
文献类型：
--
作者：
Sale WS;Goodenough UW;Heuser JE
紫海胆精子的外臂动力蛋白被吸附在云母薄片上，并通过快速冷冻、深蚀刻技术进行可视化。复制品揭示了由两个球形头部组成的粒子，两个不规则形状的茎连接在一起，沿着它们的长度接触。一个头是梨形的(18.5×12.5 nm)，另一个是球形的(14.5 nm直径)。茎由珠状亚单位组成的复合体装饰。在蔗糖梯度的21S dynein-1部分中也发现了同样的双头蛋白。β-重链/中间链1(β/IC-1)dynein亚组分是通过低盐透析和高盐提取的dynein-1区带离心法产生的，只含有单茎的单头分子。这些头部主要是梨形的(18.5X12.5 nm)。由于21S dynein-1含有两条重链(α和β)，而β/IC-1亚组分只由β重链组成(Tang等人，1982，J.Biol)。化学。257：508-515)，我们得出结论，每个头部由一个重链组成，梨形头部包含β-重链，球形头部包含α-重链。用快速冷冻、深蚀刻的方法对去膜精子的外动力蛋白臂进行了原位研究。当冷冻在没有ATP的激活缓冲液中时，每条臂由一个大的球状头部组成，它通过远端扭曲的亚基附着到A微管，并通过细长的柄附着到B微管。在ATP中，这个头部会改变方向，这样就可以看到它是由两个球状结构域构成的。我们提供了原位图像和体外图像之间的可能联系，并将海胆动力蛋白的结构与先前从衣藻和四膜虫中描述的动力蛋白进行了比较。
Outer-arm dynein from the sperm of the sea urchin S. purpuratus was adsorbed to mica flakes and visualized by the quick-freeze, deep-etch technique. Replicas reveal particles comprised of two globular heads joined by two irregularly shaped stems which make contact along their length. One head is pear-shaped (18.5 X 12.5 nm) and the other is spherical (14.5-nm diam). The stems are decorated by a complex of bead- like subunits. The same two-headed protein is found in the 21S dynein-1 fraction of sucrose gradients. The beta-heavy chain/intermediate chain 1 (beta/IC-1) dynein subfraction, produced by low-salt dialysis and zonal centrifugation of the high-salt-extracted dynein-1, contains only single-headed molecules with single stems. These heads are predominantly pear-shaped (18.5 X 12.5 nm). Since 21S dynein-1 contains two heavy chains (alpha and beta), and the beta/IC-1 subfraction is comprised of only the beta-heavy chain (Tang et al., 1982, J. Biol. Chem. 257: 508-515), we conclude that each head is formed by a heavy chain, that the pear-shaped head contains the beta-heavy chain, and that the spherical head contains the alpha-heavy chain. The in situ outer dynein arms of demembranated sperm were also studied by the quick- freeze, deep-etch method. When frozen in reactivation buffer devoid of ATP, each arm consists of a large globular head that attaches to the A- microtubule by distally skewed subunits and attaches to the B- microtubule by a slender stalk. In ATP, this head shifts its orientation such that it can be seen to be constructed from two globular domains. We offer possible correlates between the in situ and the in vitro images, and we compare the structure of sea-urchin dynein with dynein previously described from Chlamydomonas and Tetrahymena.
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影响因子：
5.6
作者：
HEUSER, JE
通讯作者：
HEUSER, JE
DOI：
10.1073/pnas.76.11.5759
发表时间：
1979-01-01
影响因子：
11.1
作者：
HAIMO, LT;TELZER, BR;ROSENBAUM, JL
通讯作者：
ROSENBAUM, JL
影响因子：
2.7
作者：
HISANAGA, SI;SAKAI, H
通讯作者：
SAKAI, H
对纤毛的横截面的重新研究。
影响因子：
7.8
作者：
Allen, R D
通讯作者：
Allen, R D
影响因子：
7.8
作者：
JOHNSON, KA;WALL, JS
通讯作者：
WALL, JS