Okochi Mina, Yoshida Takao, Maruyama Tadashi, Kawarabayasi Yutaka, Kikuchi Hisashi, Yohda Masafumi
Department of Biotechnology and Life Science, Tokyo University of Agriculture and Technology, 2-24-16, Naka-cho, Koganei, Tokyo 184-8588, Japan.
Biochem Biophys Res Commun. 2002 Mar 8;291(4):769-74. doi: 10.1006/bbrc.2002.6523.
A molecular chaperone prefoldin/GimC from the hyperthermophilic archaeum Pyrococcus horikoshii OT3 was characterized. Pyrococcus prefoldin protected porcine heart citrate synthase from thermal aggregation whereas each subunit alone afforded little protection. It also arrested the spontaneous refolding of acid-denatured green fluorescent protein and then transferred it not only to a group II chaperonin from the hyperthermophilic archaeum Thermococcus sp. strain KS-1, but also to a group I chaperonin from the thermophilic bacterium Thermus thermophilus HB8 for subsequent ATP dependent refolding.
对嗜热古菌火球菌OT3来源的分子伴侣预折叠蛋白/ GimC进行了表征。火球菌预折叠蛋白可保护猪心柠檬酸合酶免受热聚集影响，而其每个亚基单独作用时几乎没有保护作用。它还能阻止酸变性绿色荧光蛋白的自发重折叠，然后不仅将其转移至嗜热古菌嗜热栖热放线菌KS-1菌株的II型伴侣蛋白，还转移至嗜热细菌嗜热栖热菌HB8的I型伴侣蛋白，以便随后进行ATP依赖的重折叠。
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