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首页> 外文期刊>Cell cycle >Reuse, replace, recycle. Specificity in subunit inheritance and assembly of higher-order septin structures during mitotic and meiotic division in budding yeast.
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Reuse, replace, recycle. Specificity in subunit inheritance and assembly of higher-order septin structures during mitotic and meiotic division in budding yeast.

机译:重复使用,更换,回收。在发芽酵母的有丝分裂和减数分裂分裂过程中,亚基遗传和更高级别的Septin结构装配的特异性。

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摘要

Septins are guanine nucleotide-binding proteins that form hetero-oligomeric complexes, which assemble into filaments and higher-order structures at sites of cell division and morphogenesis in eukaryotes. Dynamic changes in the organization of septin-containing structures occur concomitantly with progression through the mitotic cell cycle and during cell differentiation. Septins also undergo stage-specific post-translational modifications, which have been implicated in regulating their dynamics, in some cases via purported effects on septin turnover. In our recent study, the fate of two of the five septins expressed in mitotic cells of budding yeast (Saccharomyces cerevisiae) was tracked using two complementary fluorescence-based methods for pulse-chase analysis. During mitotic growth, previously-made molecules of both septins (Cdc10 and Cdc12) persisted through multiple successive divisions and were incorporated equivalently with newly synthesized molecules into hetero-oligomers and higher-order structures. Similarly, in cells undergoing meiosis and the developmental program of sporulation, pre-existing copies of Cdc10 were incorporated into new structures. In marked contrast, Cdc12 was irreversibly excluded from septin complexes and replaced by another septin, Spr3. Here, we discuss the broader implications of these results and related findings with regard to how septin dynamics is coordinated with the mitotic cell cycle and in the yeast life cycle, and how these observations may relate to control of the dynamics of other complex multi-subunit assemblies.
机译:Septins是鸟嘌呤核苷酸结合蛋白,可形成异源寡聚复合物,在真核生物的细胞分裂和形态发生位点组装成细丝和高阶结构。含Septin的结构组织的动态变化伴随着有丝分裂细胞周期和细胞分化过程的进行。隔蛋白还经历了特定于阶段的翻译后修饰,在某些情况下,据称对隔蛋白更新有影响,这涉及调节其动力学。在我们最近的研究中,使用两种基于互补荧光的脉冲追踪方法来追踪在发芽酵母(酿酒酵母)的有丝分裂细胞中表达的五个Septin中的两个的命运。在有丝分裂的生长过程中,两个分离蛋白(Cdc10和Cdc12)的先前制造的分子通过多个连续分裂而持续存在,并与新合成的分子等价地掺入杂合低聚物和高阶结构中。同样,在经历减数分裂和孢子形成的发育程序的细胞中,将预先存在的Cdc10拷贝整合到新结构中。与之形成鲜明对比的是,Cdc12不可逆地从Septin复合物中排除,并被另一个Septin Spr3取代。在这里,我们讨论了这些结果和相关发现的广泛含义,涉及septin动力学如何与有丝分裂细胞周期以及酵母生命周期协调,以及这些观察结果如何与其他复杂多亚基的动力学控制有关组件。

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