Bonk M, Tadros M, Vandekerckhove J, Al-Babili S, Beyer P
Institut für Biologie II der Universität, Zellbiologie, Belgium.
Plant Physiol. 1996 Jul;111(3):931-9. doi: 10.1104/pp.111.3.931.
In chromoplast differentiation during flower formation in Narcissus pseudonarcissus, the molecular chaperones chaperonin 60 (Cpn60; alpha and beta) and heat-shock protein 70 (Hsp70) greatly increase in abundance. Both were purified and shown to be present in a functional form in chromoplasts, indicating their requirement in the extensive structural rearrangements during the chloroplast-to-chromoplast transition. The purified proteins, sequenced N terminally and from internal peptides, showed strong homology to plastid Cpn60 and Hsp 70 representatives from other plant species. During chromoplast differentiation, the carotenoid biosynthetic pathway is strongly induced. The corresponding enzymes are all nuclear encoded and form a large, soluble, hetero-oligomeric protein complex after import but prior to their membrane attachment. By immunoprecipitations we have shown that the plastid Hsp70 is a structural constituent of a soluble entity also containing phytoene desaturase.
在水仙成花过程中的质体色素分化过程中,分子伴侣伴侣蛋白60(Cpn60;α和β)和热休克蛋白70(Hsp70)的丰度大幅增加。二者均被纯化,并显示以功能形式存在于质体色素中,这表明它们在叶绿体到质体色素转变过程中的广泛结构重排中是必需的。纯化后的蛋白质经N端测序和内部肽段测序,显示与其他植物物种的质体Cpn60和Hsp 70代表具有很强的同源性。在质体色素分化过程中,类胡萝卜素生物合成途径被强烈诱导。相应的酶均由核编码,在导入后但在它们附着于膜之前形成一个大的、可溶的、异源寡聚蛋白复合体。通过免疫沉淀,我们已表明质体Hsp70是一个也含有八氢番茄红素去饱和酶的可溶实体的结构成分。