Global transcript and phenotypic analysis of yeast cells expressing Ssa1, Ssa2, Ssa3 or Ssa4 as sole source of cytosolic Hsp70-Ssa chaperone activity.
Global transcript and phenotypic analysis of yeast cells expressing Ssa1, Ssa2, Ssa3 or Ssa4 as sole source of cytosolic Hsp70-Ssa chaperone activity.
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表达SSA1，SSA2，SSA3或SSA4的酵母细胞的全局转录本和表型分析是胞质HSP70-SSA伴侣活性的唯一来源。
DOI：
10.1186/1471-2164-15-194
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发表时间：
2014-03-14
期刊：
影响因子：
4.4
通讯作者：
Jones GW
中科院分区：
文献类型：
--
作者：
Hasin N;Cusack SA;Ali SS;Fitzpatrick DA;Jones GW
胞浆Hsp 70是一种普遍存在的分子伴侣，参与多种细胞应激反应。热休克蛋白70的主要功能是通过与暴露的疏水区结合并防止无定形聚集体的积累来防止变性蛋白的聚集。为了进一步了解高度同源的酵母Hsp 70-Ssa家族的功能冗余和专业化，我们表达了每个单独的Ssa蛋白作为细胞中Hsp 70的唯一来源，并评估了朊病毒繁殖和抗应激性的表型差异。此外，我们还使用微阵列和RT-qPCR分析分析了表达单个Ssa蛋白的酵母菌株中的全局基因表达模式。我们证实和扩展以前的研究表明，细胞表达不同的Hsp 70-Ssa亚型不同的酵母[PSI+]朊病毒的繁殖能力，Ssa 3是最精通。四个Ssa家族成员的热诱导亚型更精通获得耐热性，我们表现出更大的要求比以前认为的，除了传统的Hsp 104蛋白解聚酶机制的细胞过程，在获得这种耐热性。表达不同Hsp 70-Ssa同种型的细胞也显示出对暴露于细胞壁损伤和氧化应激剂的表型应答的差异，同样，热诱导同种型比组成型同种型提供更好的保护。我们评估了表达单个Hsp 70-Ssa同种型作为胞质Hsp 70唯一来源的细胞的全局转录组谱，并确定了这些菌株之间细胞基因表达的显著差异。基因表达谱的差异为我们在本研究中观察到的一些表型差异提供了依据。我们还证明了微阵列数据和选择基因的RT-qPCR分析之间的高度相关性。Hsp 70-Ssa家族在酵母细胞内提供冗余和变体特异性功能。表达Hsp 70-Ssa家族的单个成员作为Ssa蛋白的唯一来源的酵母细胞显示全局基因表达谱的差异。这些全球基因表达的变化可能有助于显着的Hsp 70-Ssa家族成员之间观察到的表型差异。本文的在线版本（doi：10.1186/1471-2164-15-194）包含补充材料，可供授权用户使用。
Cytosolic Hsp70 is a ubiquitous molecular chaperone that is involved in responding to a variety of cellular stresses. A major function of Hsp70 is to prevent the aggregation of denatured proteins by binding to exposed hydrophobic regions and preventing the accumulation of amorphous aggregates. To gain further insight into the functional redundancy and specialisation of the highly homologous yeast Hsp70-Ssa family we expressed each of the individual Ssa proteins as the sole source of Hsp70 in the cell and assessed phenotypic differences in prion propagation and stress resistance. Additionally we also analysed the global gene expression patterns in yeast strains expressing individual Ssa proteins, using microarray and RT-qPCR analysis. We confirm and extend previous studies demonstrating that cells expressing different Hsp70-Ssa isoforms vary in their ability to propagate the yeast [PSI+] prion, with Ssa3 being the most proficient. Of the four Ssa family members the heat inducible isoforms are more proficient in acquiring thermotolerance and we show a greater requirement than was previously thought, for cellular processes in addition to the traditional Hsp104 protein disaggregase machinery, in acquiring such thermotolerance. Cells expressing different Hsp70-Ssa isoforms also display differences in phenotypic response to exposure to cell wall damaging and oxidative stress agents, again with the heat inducible isoforms providing better protection than constitutive isoforms. We assessed global transcriptome profiles for cells expressing individual Hsp70-Ssa isoforms as the sole source of cytosolic Hsp70, and identified a significant difference in cellular gene expression between these strains. Differences in gene expression profiles provide a rationale for some phenotypic differences we observed in this study. We also demonstrate a high degree of correlation between microarray data and RT-qPCR analysis for a selection of genes. The Hsp70-Ssa family provide both redundant and variant-specific functions within the yeast cell. Yeast cells expressing individual members of the Hsp70-Ssa family as the sole source of Ssa protein display differences in global gene expression profiles. These changes in global gene expression may contribute significantly to the phenotypic differences observed between the Hsp70-Ssa family members. The online version of this article (doi:10.1186/1471-2164-15-194) contains supplementary material, which is available to authorized users.
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影响因子：
46.9
作者：
Bach, S;Talarek, N;Blondel, M
通讯作者：
Blondel, M
DOI：
10.1006/bbrc.1998.9864
发表时间：
1998-12-30
影响因子：
3.1
作者：
Grant, CM;Perrone, G;Dawes, IW
通讯作者：
Dawes, IW
影响因子：
64.5
作者：
Glover, JR;Lindquist, S
通讯作者：
Lindquist, S
DOI：
10.1073/pnas.82.19.6455
发表时间：
1985-01-01
影响因子：
11.1
作者：
HUNT, C;MORIMOTO, RI
通讯作者：
MORIMOTO, RI
影响因子：
11.4
作者：
Dragovic, Zdravko;Broadley, Sarah A.;Hartl, F. Ulrich
通讯作者：
Hartl, F. Ulrich