HEAT-SHOCK FACTOR IS REQUIRED FOR GROWTH AT NORMAL TEMPERATURES IN THE FISSION YEAST SCHIZOSACCHAROMYCES-POMBE
HEAT-SHOCK FACTOR IS REQUIRED FOR GROWTH AT NORMAL TEMPERATURES IN THE FISSION YEAST SCHIZOSACCHAROMYCES-POMBE
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DOI：
10.1128/mcb.13.2.749
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发表时间：
1993-02-01
影响因子：
5.3
通讯作者：
KINGSTON, RE
中科院分区：
文献类型：
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作者：
GALLO, GJ;PRENTICE, H;KINGSTON, RE
粟酒裂殖酵母在细胞过程的研究中越来越有用，因为在某些方面，如细胞周期和剪接，它与后生动物相似。以往的生物化学研究表明，S.粟酒裂殖酵母热休克因子（HSF）仅在应激条件下被完全诱导，其方式类似于黑腹果蝇和人类，但不同于出芽酵母中HSF的组成型结合。本文报道了从S.粟球。S.粟酒裂殖酵母HSF的结构域与人和D.与芽殖酵母HSFs的结构相比，黑腹酵母HSFs中的HSFs的调节作用更强。粟酒孢可能反映了后生动物的调节。令人惊讶的是，S。粟酒裂殖酵母HSF基因是在常温下生长所必需的。我们证明了S.粟酒裂殖酵母HSF基因可以被D.黑腹果蝇HSF基因，并且含有这些基因中的任一个的菌株在活力和来自热激启动子的热诱导转录物的水平方面与瞬时热激菌株表现相似。将含有D.然而，黑腹果蝇HSF基因在正常生长温度下具有较低的生长速率并显示改变的形态。这些数据表明，热休克反应所需的HSF域的功能保守。他们进一步表明，在正常（非应激）生长条件下，HSF在真核细胞生长中的一般作用。
Schizosaccharomyces pombe is becoming an increasingly useful organism for the study of cellular processes, since in certain respects, such as the cell cycle and splicing, it is similar to metazoans. Previous biochemical studies have shown that the DNA binding ability of S. pombe heat shock factor (HSF) is fully induced only under stressed conditions, in a manner similar to that of Drosophila melanogaster and humans but differing from the constitutive binding by HSF in the budding yeasts. We report the isolation of the cDNA and gene for the HSF from S. pombe. S. pombe HSF has a domain structure that is more closely related to the structure of human and D. melanogaster HSFs than to the structure of the budding yeast HSFs, further arguing that regulation of HSF in S. pombe is likely to reflect regulation in metazoans. Surprisingly, the S. pombe HSF gene is required for growth at normal temperatures. We show that the S. pombe HSF gene can be replaced by the D. melanogaster HSF gene and that strains containing either of these genes behave similarly to transiently heat-shocked strains with respect to viability and the level of heat-induced transcripts from heat shock promoters. Strains containing the D. melanogaster HSF gene, however, have lower growth rates and show altered morphology at normal growth temperatures. These data demonstrate the functional conservation of domains of HSF that are required for response to heat shock. They further suggest a general role for HSF in growth of eukaryotic cells under normal (nonstressed) growth conditions.