Payne W E, Fitzgerald-Hayes M
Department of Biochemistry and Molecular Biology, University of Massachusetts, Amherst 01003.
Mol Cell Biol. 1993 Jul;13(7):4351-64. doi: 10.1128/mcb.13.7.4351-4364.1993.
We identified a putative Saccharomyces cerevisiae homolog of a phosphoinositide-specific phospholipase C (PI-PLC) gene, PLC1, which encodes a protein most similar to the delta class of PI-PLC enzymes. The PLC1 gene was isolated during a study of yeast strains that exhibit defects in chromosome segregation. plc1-1 cells showed a 10-fold increase in aberrant chromosome segregation compared with the wild type. Molecular analysis revealed that PLC1 encodes a predicted protein of 101 kDa with approximately 50 and 26% identity to the highly conserved X and Y domains of PI-PLC isozymes from humans, bovines, rats, and Drosophila melanogaster. The putative yeast protein also contains a consensus EF-hand domain that is predicted to bind calcium. Interestingly, the temperature-sensitive and chromosome missegregation phenotypes exhibited by plc1-1 cells were partially suppressed by exogenous calcium.
我们鉴定出了一种假定的酿酒酵母磷酸肌醇特异性磷脂酶C(PI-PLC)基因的同源物PLC1,它编码一种与PI-PLC酶的δ类最为相似的蛋白质。PLC1基因是在对表现出染色体分离缺陷的酵母菌株进行研究的过程中分离得到的。与野生型相比,plc1-1细胞中异常染色体分离增加了10倍。分子分析表明,PLC1编码一种预测分子量为101 kDa的蛋白质,与来自人类、牛、大鼠和黑腹果蝇的PI-PLC同工酶的高度保守的X和Y结构域具有约50%和26%的同一性。这种假定的酵母蛋白还含有一个预测可结合钙的共有EF手型结构域。有趣的是,plc1-1细胞所表现出的温度敏感性和染色体错分离表型被外源钙部分抑制。