• 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Molecular and Cellular Biology >Phospholipase C Is Involved in Kinetochore Function in Saccharomyces cerevisiae
【24h】

Phospholipase C Is Involved in Kinetochore Function in Saccharomyces cerevisiae

机译：磷脂酶C参与酿酒酵母的线粒体功能。

获取原文
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

The budding yeast PLC1 gene encodes a homolog of the δ isoform of mammalian phosphoinositide-specific phospholipase C. Here, we present evidence that Plc1p associates with the kinetochore complex CBF3. This association is mediated through interactions with two established kinetochore proteins, Ndc10p and Cep3p. We show by chromatin immunoprecipitation experiments that Plc1p resides at centromeric loci in vivo. Deletion of PLC1, as well asplc1 mutations which abrogate the interaction of Plc1p with the CBF3 complex, results in a higher frequency of minichromosome loss, nocodazole sensitivity, and mitotic delay. Overexpression of Ndc10p suppresses the nocodazole sensitivity of plc1 mutants, implying that the association of Plc1p with CBF3 is important for optimal kinetochore function. Chromatin extracts fromplc1Δ cells exhibit reduced microtubule binding to minichromosomes. These results suggest that Plc1p associates with kinetochores and regulates some aspect of kinetochore function and demonstrate an intranuclear function of phospholipase C in eukaryotic cells.
机译：萌芽的酵母 PLC1 基因编码哺乳动物磷酸肌醇特异性磷脂酶C的δ亚型的同源物。在这里，我们提供了Plc1p与动粒复合物CBF3相关的证据。这种关联是通过与两个建立的动粒蛋白Ndc10p和Cep3p相互作用来介导的。我们通过染色质免疫沉淀实验表明，Plc1p在体内位于着丝粒基因座。删除 PLC1 以及 plc1 突变（这些突变会消除Plc1p与CBF3复合物的相互作用），导致更高的微型染色体丢失频率，诺考达唑敏感性和有丝分裂延迟。 Ndc10p的过表达抑制了 plc1 突变株的诺考达唑敏感性，这表明Plc1p与CBF3的缔合对于最佳的动粒功能很重要。来自 plc1 Δ细胞的染色质提取物显示出与微染色体的结合减少。这些结果表明Plc1p与动植物相关联，并调节动粒功能的某些方面，并证明真核细胞中磷脂酶C的核内功能。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号