Purification and characterization of the 16-kDa heat-shock-responsive protein from the thermophilic cyanobacterium Synechococcus vulcanus, which is an alpha-crystallin-related, small heat shock protein.
Purification and characterization of the 16-kDa heat-shock-responsive protein from the thermophilic cyanobacterium Synechococcus vulcanus, which is an alpha-crystallin-related, small heat shock protein.
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来自嗜热蓝藻聚球藻的 16 kDa 热休克响应蛋白的纯化和表征，该蛋白是一种与 α-晶状体蛋白相关的小热休克蛋白。
DOI：
10.1046/j.1432-1327.1999.00380.x
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发表时间：
1999
期刊：
影响因子：
--
通讯作者：
Hitoshi Nakamoto
中科院分区：
文献类型：
--
作者：
S. Roy;T. Hiyama;Hitoshi Nakamoto
一个16-kDa的蛋白质，热休克处理后在嗜热蓝细菌聚球藻中积累的主要蛋白质之一，被纯化到明显的同质性。该蛋白的N-末端和内部氨基酸序列与来自其他生物体的α-晶状体蛋白相关的小热休克蛋白具有同源性。该蛋白被命名为HspA。分子排阻层析和非变性凝胶电泳结果表明，HspA形成了一个由24个亚基组成的大的同源寡聚体。它阻止了猪苹果酸脱氢酶在45 ℃和50 ℃下的聚集，以及柠檬酸合酶在50 ℃下的聚集。然而，苹果酸脱氢酶的活性在这些热激条件下没有得到保护，或者在温度从45或50摄氏度转变到21摄氏度后重新活化。热休克蛋白A能够增强化学变性的兔肌肉乳酸脱氢酶的重折叠在一个ATP非依赖性的方式。同源的16-kDa的蛋白质也被发现诱导后，热休克处理中温蓝藻集胞藻属PCC 6803。
A 16-kDa protein, one of the major proteins that accumulates upon heat-shock treatment in the thermophilic cyanobacterium Synechococcus vulcanus, was purified to apparent homogeneity. The N-terminal and internal amino acid sequences of the protein exhibited a homology to the alpha-crystallin-related, small heat shock proteins from other organisms. The protein was designated HspA. Size-exclusion chromatography and nondenaturing gel electrophoresis demonstrated that HspA formed a large homo-oligomer consisting of 24 subunits. It prevented the aggregation of porcine malic dehydrogenase at 45 degrees C and 50 degrees C and citrate synthase at 50 degrees C. The activity of the malic dehydrogenase, however, was not protected under these heat-shock conditions or reactivated after a shift in temperature from 45 or 50 degrees C to 21 degrees C. HspA was able to enhance the refolding of chemically denatured rabbit muscle lactate dehydrogenase in an ATP-independent manner. A homologue to the 16-kDa protein was also found to be induced upon heat-shock treatment in the mesophilic cyanobacterium Synechocystis sp. PCC 6803.
DOI：
10.1016/s0021-9258(17)36821-7
发表时间：
1994-05
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Q. Chen;K. Osteryoung;E. Vierling
通讯作者：
Q. Chen;K. Osteryoung;E. Vierling
叶绿体小热激蛋白寡聚体在体内热应激期间不被磷酸化并且不解离。
影响因子：
7.4
作者：
Suzuki,TC;Krawitz,DC;Vierling,E
通讯作者：
Vierling,E