Chlamydomonas alpha-tubulin is posttranslationally modified in the flagella during flagellar assembly.
Chlamydomonas alpha-tubulin is posttranslationally modified in the flagella during flagellar assembly.
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DOI：
10.1083/jcb.97.1.258
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发表时间：
1983-07
期刊：
影响因子：
--
通讯作者：
Rosenbaum JL
中科院分区：
文献类型：
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作者：
L'Hernault SW;Rosenbaum JL
莱茵衣藻鞭毛轴丝内的主要α-微管蛋白不同于细胞体中的主要α-微管蛋白。我们表明，这两个等电点的α-微管蛋白的变体是相互相关的，因为翻译后修饰的细胞体前体形式将其转化为轴丝形式。在鞭毛组装过程中，前体α-微管蛋白进入鞭毛，并在其加入到生长的轴丝微管之前或之时在鞭毛基质部分内进行后修饰。也进行了旨在鉴定这种翻译后修饰的性质的实验。当鞭毛被诱导组装在从头蛋白质合成的情况下，氚标记的乙酸可用于posteritonally标记α-微管蛋白在体内，在这些条件下，没有其他鞭毛多肽表现出可检测的标记。
The principal alpha-tubulin within Chlamydomonas reinhardtii flagellar axonemes differs from the major alpha-tubulin in the cell body. We show that these two isoelectric variants of alpha-tubulin are related to one another since posttranslational modification of the cell body precursor form converts it to the axonemal form. During flagellar assembly, precursor alpha-tubulin enters the flagella and is posttranslationally modified within the flagellar matrix fraction prior to or at the time of its addition to the growing axonemal microtubules. Experiments designed to identify the nature of this posttranslational modification have also been conducted. When flagella are induced to assemble in the absence of de novo protein synthesis, tritiated acetate can be used to posttranslationally label alpha-tubulin in vivo and, under these conditions, no other flagellar polypeptides exhibit detectable labeling.