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从N. crassa中分离和测序一种FK506结合蛋白,该蛋白催化蛋白质折叠
M Tropschug1, E Wachter, S Mayer
1Institut für Physiologische Chemie der Universität München, FRG.
Nature
|August 16, 1990
概括
两个不同的类型的蛋白质折叠酶,环菲林和FK506结合蛋白,加速缓慢的蛋白质折叠反应. 这两类酶都被特定的免疫抑制药物抑制,揭示了蛋白质结构调节的各种机制.
科学领域:
- 生物化学 生物化学
- 分子生物学分子生物学
- 酶学 是一种酶学.
背景情况:
- 蛋白质折叠对细胞功能至关重要,缓慢的折叠步骤可能会限制速度.
- 烯基 cis/trans 异构化是蛋白质折叠的一个关键步骤.
- 赛克洛菲林是一种prolyl异构酶,与免疫抑制剂环素A相互作用.
研究的目的:
- 为了识别和描述催化缓慢蛋白质折叠步骤的新型酶.
- 调查prolyl异构酶活性与免疫抑制药物结合之间的关系.
- 探索参与蛋白质构成变化的酶的多样性.
主要方法:
- 隔离,克隆,测序和表达一种来自Neurospora crassa的新型prolyl异构酶.
- 生物化学分析测量蛋白质折叠催化.
- 使用环素A和FK506.6的抑制研究.
主要成果:
- 从N.crassa发现了一种与环菲林无关的新型prolyl异相酶.
- 这种新型酶与FK506结合蛋白具有序列相似性,并催化缓慢的蛋白质折叠步骤.
- FK506抑制了N.crassa酶的活性,而环素A没有.
- 环林的活性被环素A抑制,但不是FK506.
结论:
- 至少有两种不同的类型的酶,环素和FK506结合蛋白 (conformases),催化缓慢的蛋白质折叠步骤.
- 这些酶在不同的生物体和细胞类型中得到保存.
- 这两种酶类都是特定免疫抑制药物的点,突出显示了它们在细胞调节中的作用.
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