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首页> 外文期刊>Molecular and Cellular Biology >Domains of beta-tubulin essential for conserved functions in vivo.
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Domains of beta-tubulin essential for conserved functions in vivo.

机译：β-微管蛋白的域对于体内的保守功能必不可少。

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The relationship between the primary sequence of tubulins and their properties in cells was studied by gene transfection experiments. Previously, we studied a chimeric beta-tubulin formed from chicken beta-tubulin-2 sequences in the amino-terminal portion and the highly divergent Saccharomyces cerevisiae TUB2 sequences in the carboxy-terminal 25% of the molecule. In the cytoplasm of cultured animal cells, this protein incorporates into all microtubule structures and assembles with the same efficiency as endogenous tubulin. We show that the protein products of chimeric genes with an increasing proportion of yeast sequence, extending 5' of the carboxy-terminal 25%, are abnormal in two ways. First, they assemble with a significantly lower efficiency than the original chimeric protein or the endogenous tubulins. Second, they are less stable in the cytoplasm. The results suggest that the position of the yeast sequences is crucial in determining the properties of the molecule. Results of analyses of 1 deletion mutation and 10 linker insertions in the original chimeric tubulin suggest that those changes made outside the carboxyl terminus completely disrupt assembly activity, while those made in the carboxyl terminus do not.
机译：通过基因转染实验研究了微管蛋白的主要序列与其细胞特性之间的关系。以前，我们研究了由鸡的β-微管蛋白2序列在氨基末端部分中形成的嵌合β-微管蛋白和在分子的25％羧基端具有高度趋异性的酿酒酵母TUB2序列。在培养的动物细胞的细胞质中，该蛋白质整合到所有微管结构中，并以与内源微管蛋白相同的效率组装。我们表明，嵌合基因的蛋白质产物具有增加比例的酵母序列，在羧基末端的5'端延伸25％，在两种方面都是异常的。首先，它们的组装效率大大低于原始的嵌合蛋白或内源性微管蛋白。第二，它们在细胞质中不稳定。结果表明，酵母序列的位置对于确定分子的性质至关重要。原始嵌合微管蛋白中1个缺失突变和10个接头插入的分析结果表明，在羧基末端之外进行的那些改变完全破坏了组装活性，而在羧基末端进行的则没有。

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