Christiano Romain, Nagaraj Nagarjuna, Fröhlich Florian, Walther Tobias C
Department of Cell Biology, Yale School of Medicine, New Haven, CT 06510, USA; Department of Genetics and Complex Diseases, Harvard School of Public Health, Boston, MA 02115, USA.
Mass spectrometry core facility, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany.
Cell Rep. 2014 Dec 11;9(5):1959-1965. doi: 10.1016/j.celrep.2014.10.065. Epub 2014 Nov 26.
How cells maintain specific levels of each protein and whether that control is evolutionarily conserved are key questions. Here, we report proteome-wide steady-state protein turnover rate measurements for the evolutionarily distant but ecologically similar yeasts, Saccharomyces cerevisiae and Schizosaccharomyces pombe. We find that the half-life of most proteins is much longer than currently thought and determined to a large degree by protein synthesis and dilution due to cell division. However, we detect a significant subset of proteins (∼15%) in both yeasts that are turned over rapidly. In addition, the relative abundances of orthologous proteins between the two yeasts are highly conserved across the 400 million years of evolution. In contrast, their respective turnover rates differ considerably. Our data provide a high-confidence resource for studying protein degradation in common yeast model systems.
细胞如何维持每种蛋白质的特定水平,以及这种调控在进化上是否保守,是关键问题。在这里,我们报告了在进化上距离遥远但生态上相似的酵母酿酒酵母和裂殖酵母的全蛋白质组稳态蛋白质周转率测量结果。我们发现,大多数蛋白质的半衰期比目前认为的要长得多,并且在很大程度上由细胞分裂导致的蛋白质合成和稀释所决定。然而,我们在两种酵母中都检测到了一个显著的快速周转蛋白质子集(约15%)。此外,在4亿年的进化过程中,两种酵母直系同源蛋白质的相对丰度高度保守。相比之下,它们各自的周转率差异很大。我们的数据为研究常见酵母模型系统中的蛋白质降解提供了一个高可信度的资源。