首页> 外文期刊>Nucleic Acids Research >The fission yeast chromo domain encoding gene chp1(+) is required for chromosome segregation and shows a genetic interaction with alpha-tubulin.
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The fission yeast chromo domain encoding gene chp1(+) is required for chromosome segregation and shows a genetic interaction with alpha-tubulin.

机译:裂变酵母染色体域编码基因chp1(+)是染色体分离所必需的,并显示与α-微管蛋白的遗传相互作用。

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In eukaryotes, the segregation of chromosomes is co-ordinated by the centromere and must proceed accurately if aneuploidy and cell death are to be avoided. The fission yeast centromere is complex, containing highly repetitive regions of DNA showing the characteristics of heterochromatin. Two proteins, Swi6p and Clr4p, that are associated with the fission yeast centromere also contain a chromo (chromatin organisation modifier) domain and are required for centromere function. We have analysed a novel fission yeast gene encoding a putative chromo domain called chp 1(+) (chromo domain protein in Schizosaccharomyces p ombe ). In the absence of Chp1p protein, cells are viable but show chromosome segregation defects such as lagging chromosomes on the spindle during anaphase and high rates of minichromosome loss, phenotypes which are also displayed by swi 6 and clr 4. A fusion protein between green fluorescent protein (GFP) and Chp1p, like Swi6p, is localized to discrete sites within the nucleus. In contrast to Swi6p and Clr4p, Chp1p is not required to repress silent mating-type genes. We demonstrate a genetic interaction between chp 1(+) and alpha-tubulin ( nda 2(+)) and between swi 6(+) and beta-tubulin ( nda 3(+)). Chp1p and Swi6p proteins may be components of the kinetochore which captures and stabilizes the microtubules of the spindle.
机译:在真核生物中,染色体的分离由着丝粒协调,如果要避免非整倍性和细胞死亡,必须准确地进行染色体分离。裂变酵母着丝粒很复杂,包含高度重复的DNA区域,显示出异染色质的特征。与裂变酵母着丝粒相关的两种蛋白质Swi6p和Clr4p也包含染色体(染色质组织修饰物)结构域,是着丝粒功能所必需的。我们已经分析了一种新的裂变酵母基因,该基因编码一个称为chp 1(+)的染色体结构域(Schizosaccharomyces p ombe中的染色体结构域蛋白)。在缺乏Chp1p蛋白的情况下,细胞是有活力的,但会表现出染色体分离缺陷,例如后期时纺锤体上的染色体滞后以及微型染色体丢失率高,swi 6和clr 4也表现出表型。绿色荧光蛋白之间的融合蛋白(GFP)和Chp1p与Swi6p类似,位于细胞核内的离散位点。与Swi6p和Clr4p相反,Chp1p不需要抑制沉默的交配型基因。我们证明了chp 1(+)和α-微管蛋白(nda 2(+))之间以及swi 6(+)和β-微管蛋白(nda 3(+))之间的遗传相互作用。 Chp1p和Swi6p蛋白可能是线粒体的组成部分,可以捕获并稳定纺锤体的微管。

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