The yeast mitochondrial proteome, a study of fermentative and respiratory growth
The yeast mitochondrial proteome, a study of fermentative and respiratory growth
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DOI：
10.1074/jbc.m310160200
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发表时间：
2004-02-06
影响因子：
4.8
通讯作者：
Bergmann, U
中科院分区：
文献类型：
--
作者：
Ohlmeier, S;Kastaniotis, AJ;Bergmann, U
酿酒酵母能够从发酵转变为呼吸（双轴转变），代谢活动发生重大变化。先前已在转录水平上研究过这种现象。在这里，我们对酵母线粒体蛋白质组和在葡萄糖（发酵）和甘油（呼吸）上生长的细胞中相应的转录活性进行了平行分析。建立了该细胞器蛋白质组的二维参考凝胶（可在 www.biochem.oulu.fi/proteomics/ 获得），其中包含约 800 个强斑点。从 459 个点中鉴定出 253 个蛋白质，其中包括低丰度和疏水性蛋白质，以及 37 个先前被认为是假设的蛋白质，其细胞定位部分未知。双轴转变后，线粒体中只有 18 种蛋白质水平发生变化（17 种增加，1 种减少），其中涉及三羧酸循环的蛋白质（Sdh1p、Sdh2p 和 Sdh4p）和呼吸链（Cox4p、Cyb2p 和 Qcr7p），参与其他呼吸途径的蛋白质（Ach1p、Adh2p、Ald4p、Cat2p、Icl2p 和 Pdh1p），以及两种功能未知的蛋白质（Om45p 和 Ybr230p）。除了线粒体蛋白质质量总体增加外，即使在主要的代谢适应中，线粒体蛋白质组也保持显着恒定。这似乎与 DNA 微阵列分析的结果不一致，其中编码线粒体蛋白的基因的相当异质的上调或下调意味着蛋白质组的巨大变化。我们认为，蛋白质组和转录调控之间的差异，除了翻译效率不同之外，还表明蛋白质在不同生理条件下的周转率发生了变化。
Saccharomyces cerevisiae is able to switch from fermentation to respiration (diauxic shift) with major changes in metabolic activity. This phenomenon has been previously studied on the transcriptional level. Here we present a parallel analysis of the yeast mitochondrial proteome and the corresponding transcriptional activity in cells grown on glucose (fermentation) and glycerol (respiration). A two-dimensional reference gel for this organelle proteome was established (available at www.biochem.oulu.fi/proteomics/), which contains about 800 intense spots. From 459 spots 253 individual proteins were identified, among them low abundant and hydrophobic proteins, and 37 proteins previously deemed hypothetical, with partially unknown cellular localization. After the diauxic shift, mitochondrial levels of only 18 proteins were changed (17 increased, with 1 decreased), among them proteins involved in the tricarboxylic acid cycle (Sdh1p, Sdh2p, and Sdh4p) and the respiratory chain (Cox4p, Cyb2p, and Qcr7p), proteins contributing to other respiratory pathways (Ach1p, Adh2p, Ald4p, Cat2p, Icl2p, and Pdh1p), and two proteins with unknown function (Om45p and Ybr230p). Apart from an overall increase in mitochondrial protein mass, the mitochondrial proteome remains remarkably constant, even in a major metabolic adaptation. This seemingly disagrees with results of the DNA microarray analyses, where a rather heterogenous up- or down-regulation of genes encoding mitochondrial proteins implies large changes in the proteome. We propose that the discrepancy between proteome and transcriptional regulation, apart from different translation efficiency, indicates a changed turnover rate of proteins in different physiological conditions.