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Axoneme specialization embedded in a 'Generalist' beta-tubulin.

机译:Axoneme专业化嵌入“通才”β-微管蛋白中。

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The relationship between the primary structure of the beta-tubulin C-terminal tail (CTT) and axoneme structure and function is explored using the spermatogenesis-specific beta2-tubulin of Drosophila. We previously showed that all beta-tubulins used for motile 9 + 2 axonemes contain a conserved sequence motif in the proximal part of the CTT, the beta-tubulin axoneme motif. The differential ability of tubulin isoforms and abilities of beta2-tubulin C-terminal truncations to form axonemes led us to hypothesize that the axoneme motif is essential for axoneme formation and the distal half of the CTT was less important. The studies we report here indicate that it is not that simple. Unexpectedly, some changes in the core sequence of the axoneme motif did not disrupt formation of motile axonemes. And, while deletion of the distal CTT did not disrupt the ability to produce functional sperm [Popodi et al., Cell Motil Cytoskeleton 2005;62:48-64], changing the amino acid sequence in this region can. Thus both regions are important. The deep conservation of the axoneme motif in all eukaryotic groups implies that the presence of the sequence motif confers a functional advantage. The central pair is the axoneme structure most sensitive to perturbations in tubulin molecules; we hypothesize central pair assembly is facilitated by the presence of this motif. Our data reveal that beta2-tubulin has robust properties for axoneme assembly, and that axonemal specializations are embedded in both the CTT and the body of the beta2 molecule.
机译:使用果蝇的生精特异性β2-微管蛋白探索β-微管蛋白C末端尾巴(CTT)的一级结构与轴突结构与功能之间的关系。我们先前显示,用于运动型9 + 2轴索蛋白的所有β-微管蛋白在CTT的近端部分均包含一个保守的序列基序,即β-微管蛋白的轴突基序。微管蛋白同种型和β2-微管蛋白C末端截短形成轴突的能力的差异使我们假设轴突基序对于轴突形成至关重要,而CTT的远端则不那么重要。我们在这里报告的研究表明,它并不是那么简单。出乎意料的是,轴突基序的核心序列中的某些变化不会破坏能动的轴突的形成。并且,尽管远端CTT的缺失并未破坏产生功能性精子的能力[Popodi等人,Cell Motil Cytoskeleton 2005; 62:48-64],但是可以改变该区域中的氨基酸序列。因此,这两个区域都很重要。轴突基序在所有真核生物基团中的深层保守性表明,序列基序的存在赋予了功能优势。中枢对是对微管蛋白分子扰动最敏感的轴突结构。我们假设该基序的存在促进了中央对的组装。我们的数据表明,β2-微管蛋白具有强大的轴突组装特性,并且轴突的特化性同时嵌入了CTT和β2分子的体内。

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