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首页> 外文期刊>Cell motility and the cytoskeleton >Identification of betaIII- and betaIV-tubulin isotypes in cold-adapted microtubules from Atlantic cod (Gadus morhua): antibody mapping and cDNA sequencing.
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Identification of betaIII- and betaIV-tubulin isotypes in cold-adapted microtubules from Atlantic cod (Gadus morhua): antibody mapping and cDNA sequencing.

机译：鉴定来自大西洋鳕（Gadus morhua）的冷适应微管中的betaIII和betaIV-微管蛋白同种型：抗体作图和cDNA测序。

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Isolated microtubule proteins from the Atlantic cod (Gadus morhua) assemble at temperatures between 8 and 30 degrees C. The cold-adaptation is an intrinsic property of the tubulin molecules, but the reason for it is unknown. To increase our knowledge of tubulin diversity and its role in cold-adaptation we have further characterized cod tubulins using alpha- and beta-tubulin site-directed antibodies and antibodies towards posttranslationally modified tubulin. In addition, one cod brain beta-tubulin isotype has been sequenced. In mammals there are five beta-tubulins (betaI, betaII, betaIII, betaIVa and betaIVb) expressed in brain. A cod betaIII-tubulin was identified by its electrophoretic mobility after reduction and carboxymethylation. The betaIII-like tubulin accounted for more than 30% of total brain beta-tubulins, the highest yield yet observed in any animal. This tubulin corresponds most probably with an additional band, designated beta(x), which was found between alpha- and beta-tubulins on SDS-polyacrylamide gels. It was found to be phosphorylated and neurospecific, and constituted about 30% of total cod beta-tubulin isoforms. The sequenced cod tubulin was identified as a betaIV-tubulin, and a betaIV-isotype was stained by a C-terminal specific antibody. The amount of staining indicates that this isotype, as in mammals, only accounts for a minor part of the total brain beta-tubulin. Based on the estimated amounts of betaIII- and betaIV-tubulins in cod brain, our results indicate that cod has at least one additional beta-tubulin isotype and that beta-tubulin diversity evolved early during fish evolution. The sequenced cod betaIV-tubulin had four unique amino acid substitutions when compared to beta-tubulin sequences from other animals, while one substitution was in common with Antarctic rockcod beta-tubulin. Residues 221, Thr to Ser, and 283, Ala to Ser, correspond in the bovine tubulin dimer structure to loops that most probably interact with other tubulin molecules within the microtubule, and might contribute to cold-adaptation of microtubules.
机译：来自大西洋鳕鱼（Gadus morhua）的分离的微管蛋白在8至30摄氏度之间组装。冷适应是微管蛋白分子的固有特性，但其原因尚不清楚。为了增加我们对微管蛋白多样性及其在冷适应中的作用的认识，我们进一步使用α-和β-微管蛋白定点抗体和抗翻译后修饰微管蛋白的抗体对鳕鱼微管蛋白进行了表征。另外，已经对一种鳕鱼脑β-微管蛋白同种型进行了测序。在哺乳动物中，在大脑中表达了五种β-微管蛋白（betaI，betaII，betaIII，betaIVa和betaIVb）。通过还原和羧甲基化后的电泳迁移率鉴定了鳕鱼βIII-微管蛋白。 βIII样微管蛋白占脑β-微管蛋白总量的30％以上，是迄今为止在任何动物中观察到的最高产量。该微管蛋白最可能对应于一个附加的带，称为β（x），该带在SDS-聚丙烯酰胺凝胶上的α-微管蛋白和β-微管蛋白之间发现。它被发现是磷酸化的和神经特异性的，并构成了整个鳕鱼β-微管蛋白同工型的约30％。测序的鳕鱼微管蛋白被鉴定为betaIV-tubulin，并且betaIV同种型被C端特异性抗体染色。染色量表明，与哺乳动物一样，该同种型仅占总脑β-微管蛋白的一小部分。根据鳕鱼脑中βIII-和βIV-微管蛋白的估计量，我们的结果表明，鳕鱼还具有至少一种其他的β-微管蛋白同种型，并且β-微管蛋白的多样性在鱼类进化的早期就已经进化了。与来自其他动物的β-微管蛋白序列相比，测序的鳕鱼βIV-微管蛋白具有四个独特的氨基酸取代，而南极洛克克鳕鱼的β-微管蛋白共有一个取代。在牛微管蛋白二聚体结构中，残基221（Thr至Ser）和283（Ala至Ser）对应于最有可能与微管内其他微管蛋白分子相互作用的环，并且可能有助于微管的冷适应。

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