Scharfenberger Maren, Ortiz Jennifer, Grau Nicole, Janke Carsten, Schiebel Elmar, Lechner Johannes
Biochemie-Zentrum Heidelberg Ruprecht-Karls Universität, Im Neuenheimer Feld 328, D-69120 Heidelberg, Germany.
EMBO J. 2003 Dec 15;22(24):6584-97. doi: 10.1093/emboj/cdg636.
We identified a physical complex consisting of Mtw1p, an established kinetochore protein, with Nnf1p, Nsl1p and Dsn1p and have demonstrated that Nnf1p, Nsl1p and Dsn1p localize to the Saccharomyces cerevisiae kinetochore. When challenged prior to metaphase, the temperature-sensitive mutants nsl1-16 and nsl1-42 as well as Nsl1p-depleted cells failed to establish a bipolar spindle-kinetochore interaction and executed monopolar segregation of sister chromatids. In contrast, an nsl1-16 defect could not be evoked after the establishment of bipolarity. The observed phenotype is characteristic of that of mutants with defects in the protein kinase Ipl1p or components of the Dam-Duo kinetochore complex. However nsl1 mutants did not exhibit a defect in microtubule-kinetochore untethering as the ipl1-321 mutant does. Instead, they exhibited a severe defect in the kinetochore localization of the Dam-Duo complex suggesting this to be the cause for the failure of nsl1 cells to establish bipolarity. Moreover the analysis of Nsl1p-depleted cells indicated that Nsl1p is required for the spindle checkpoint and kinetochore integrity.
我们鉴定出一个由已确定的动粒蛋白Mtw1p与Nnf1p、Nsl1p和Dsn1p组成的物理复合体,并证明Nnf1p、Nsl1p和Dsn1p定位于酿酒酵母的动粒。在中期之前受到挑战时,温度敏感突变体nsl1-16和nsl1-42以及Nsl1p缺失的细胞未能建立双极纺锤体-动粒相互作用,并执行了姐妹染色单体的单极分离。相比之下,在建立双极性之后无法诱发nsl1-16缺陷。观察到的表型是蛋白激酶Ipl1p或Dam-Duo动粒复合体成分有缺陷的突变体的特征。然而,nsl1突变体并不像ipl1-321突变体那样在微管-动粒解聚方面表现出缺陷。相反,它们在Dam-Duo复合体的动粒定位方面表现出严重缺陷,这表明这是nsl1细胞无法建立双极性的原因。此外,对Nsl1p缺失细胞的分析表明,Nsl1p是纺锤体检查点和动粒完整性所必需的。