ROLE OF THE PROTEIN CHAPERONE YDJ1 IN ESTABLISHING HSP90-MEDIATED SIGNAL-TRANSDUCTION PATHWAYS
ROLE OF THE PROTEIN CHAPERONE YDJ1 IN ESTABLISHING HSP90-MEDIATED SIGNAL-TRANSDUCTION PATHWAYS
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DOI：
10.1126/science.7761857
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发表时间：
1995-06-02
期刊：
影响因子：
56.9
通讯作者：
LINDQUIST, S
中科院分区：
文献类型：
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作者：
KIMURA, Y;YAHARA, I;LINDQUIST, S
酿酒酵母底物特异性蛋白伴侣Hsp90(热休克蛋白90)在多种信号转导途径中发挥作用。在Hsp90突变体的合成致死筛选中，发现了DNAJ伴侣家族成员YDJ1的突变。在另一种野生型背景下，ydj1突变对三种Hsp90底物产生强烈而特异的影响，其中两种(雌激素和糖皮质激素受体)去抑制，第三种(酪氨酸激酶p60(v-src))的功能减弱。对其中一种底物糖皮质激素受体的分析表明，Ydj1通过与Hsp90底物的物理相互作用发挥作用。
The substrate-specific protein chaperone Hsp90 (heat shock protein 90) from Saccharomyces cerevisiae functions in diverse signal transduction pathways. A mutation in YDJ1, a member of the DnaJ chaperone family, was recovered in a synthetic-lethal screen with Hsp90 mutants. in an otherwise wild-type background, the ydj1 mutation exerted strong and specific effects an three Hsp90 substrates, derepressing two (the estrogen and glucocorticoid receptors) and reducing the function of the third (the tyrosine kinase p60(v-src)). Analysis of one of these substrates, the glucocorticoid receptor, indicated that Ydj1 exerts its effects through physical interaction with Hsp90 substrates.