A SMALL INFLUENCE OF HSP90 LEVELS ON THE TREHALOSE AND HEAT-SHOCK ELEMENT INDUCTIONS OF THE YEAST HEAT-SHOCK RESPONSE
A SMALL INFLUENCE OF HSP90 LEVELS ON THE TREHALOSE AND HEAT-SHOCK ELEMENT INDUCTIONS OF THE YEAST HEAT-SHOCK RESPONSE
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DOI：
10.1006/bbrc.1993.2030
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发表时间：
1993-08-31
影响因子：
3.1
通讯作者：
PIPER, PW
中科院分区：
文献类型：
--
作者：
CHENG, LI;KIRK, N;PIPER, PW
热休克蛋白（HSP）诱导只是热休克在酵母中引起的一种变化。海藻糖也会积累，而细胞内pH值的下降刺激了质膜atp酶的活性。最近，海藻糖诱导被证明受HSP70水平的调控，在较小程度上受HSP104水平的调控。另一种可能参与调控的热休克蛋白是HSP90，特别是当HSP90与真核细胞的热休克转录因子和几种调节蛋白形成复合物时。用HSP90正常、降低或升高的等基因酵母菌株研究了这种可能性。结果表明，HSP90水平对海藻糖和热休克元件的热诱导有较小的负影响，与HSP70的主要调节作用相比，影响较小。
Heat shock protein (HSP) induction is only one change elicited in yeast by heat shock. Trehalose is also accumulated, while declining intracellular pH stimulates plasma membrane ATPase activity. Recently the trehalose induction was shown to be regulated by levels of HSP70 and, to a lesser extent, HSP104. Another HSP which might contribute to regulation is HSP90, especially as HSP90 forms complexes with heat shock transcription factor and several of the regulatory proteins of eukaryotic cells. This possibility was investigated using isogenic yeast strains with normal, decreased or elevated HSP90. The results show HSP90 levels having a small negative influence over the heat inductions of trehalose and the heat shock element, a minor effect compared with the major regulation exerted by HSP70.