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酿酒酵母的MIF2基因编码一种与哺乳动物着丝粒蛋白CENP-C具有同源性的着丝粒蛋白的证据。

Evidence that the MIF2 gene of Saccharomyces cerevisiae encodes a centromere protein with homology to the mammalian centromere protein CENP-C.

作者信息

Meluh P B, Koshland D

机构信息

Carnegie Institution of Washington, Department of Embryology, Baltimore, Maryland 21210, USA.

出版信息

Mol Biol Cell. 1995 Jul;6(7):793-807. doi: 10.1091/mbc.6.7.793.

Abstract

The MIF2 gene of Saccharomyces cerevisiae has been implicated in mitosis. Here we provide genetic evidence that MIF2 encodes a centromere protein. Specifically, we found that mutations in MIF2 stabilize dicentric minichromosomes and confer high instability (i.e., a synthetic acentric phenotype) to chromosomes that bear a cis-acting mutation in element I of the yeast centromeric DNA (CDEI). Similarly, we observed synthetic phenotypes between mutations in MIF2 and trans-acting mutations in three known yeast centromere protein genes-CEP1/CBF1/CPF1, NDC10/CBF2, and CEP3/CBF3B. In addition, the mif2 temperature-sensitive phenotype can be partially rescued by increased dosage of CEP1. Synthetic lethal interactions between a cep1 null mutation and mutations in either NDC10 or CEP3 were also detected. Taken together, these data suggest that the Mif2 protein interacts with Cep1p at the centromere and that the yeast centromere indeed exists as a higher order protein-DNA complex. The Mif2 and Cep1 proteins contain motifs of known transcription factors, suggesting that assembly of the yeast centromere is analogous to that of eukaryotic enhancers and origins of replication. We also show that the predicted Mif2 protein shares two short regions of homology with the mammalian centromere Ag CENP-C and that two temperature-sensitive mutations in MIF2 lie within these regions. These results provide evidence for structural conservation between yeast and mammalian centromeres.

摘要

酿酒酵母的MIF2基因与有丝分裂有关。在此我们提供遗传学证据,表明MIF2编码一种着丝粒蛋白。具体而言,我们发现MIF2中的突变可稳定双着丝粒微型染色体,并使在酵母着丝粒DNA(CDEI)元件I中带有顺式作用突变的染色体具有高度不稳定性(即合成无着丝粒表型)。同样,我们在MIF2中的突变与三个已知的酵母着丝粒蛋白基因CEP1/CBF1/CPF1、NDC10/CBF2和CEP3/CBF3B中的反式作用突变之间观察到了合成表型。此外,增加CEP1的剂量可部分挽救mif2温度敏感型表型。还检测到cep1缺失突变与NDC10或CEP3中的突变之间的合成致死相互作用。综上所述,这些数据表明Mif2蛋白在着丝粒处与Cep1p相互作用,并且酵母着丝粒确实以更高阶的蛋白质-DNA复合物形式存在。Mif2和Cep1蛋白包含已知转录因子的基序,这表明酵母着丝粒的组装类似于真核生物增强子和复制起点的组装。我们还表明,预测的Mif2蛋白与哺乳动物着丝粒Ag CENP-C有两个短的同源区域,并且MIF2中的两个温度敏感突变位于这些区域内。这些结果为酵母和哺乳动物着丝粒之间的结构保守性提供了证据。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c8f5/301241/9a8b093cc0bc/mbc00076-0049-a.jpg

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