Hubbs A. E., Roy H.
Plant Science Group, Biology Department, and Center for Biophysics, Rensselaer Polytechnic Institute, Troy, New York, 12180-3590.
Plant Physiol. 1993 Feb;101(2):523-533. doi: 10.1104/pp.101.2.523.
In higher plants, ribulose bisphosphate carboxylase/oxygenase (Rubisco) consists of eight large "L" subunits, synthesized in chloroplasts, and eight small "S" subunits, synthesized as precursors in the cytosol. Assembly of these into holoenzyme occurs in the chloroplast stroma after import and processing of the S subunits. A chloroplast chaperonin interacts with the L subunits, which dissociate from the chaperonin before they assemble into holoenzyme. Our laboratory has reported L subunit assembly into Rubisco in chloroplast extracts after protein synthesis in leaves, intact chloroplasts, and most recently in membrane-free chloroplast extracts. We report here that the incorporation of in vitro-synthesized L subunits into holoenzyme depends on the conditions of L subunit synthesis. Rubisco assembly did not occur after L subunit synthesis at 160 mM KCI. When L subunit synthesis occurred at approximately 70 mM KCI, assembly depended on the temperature at which L subunit synthesis took place. These phenomena were the result of postsynthetic events taking place during incubation for protein synthesis. We separated these events from protein synthesis by lowering the temperature during protein synthesis. Lower temperatures supported the synthesis of full-length Rubisco L subunits. The assembly of these completed L subunits into Rubisco required intervening incubation with ATP, before addition of S subunits. ATP treatment mobilized L subunits from a complex with the chloroplast chaperonin 60 oligomer. Addition of 130 mM KCI at the beginning of the intervening incubation with ATP blocked the incorporation of L subunits into Rubisco. The inhibitory effect of high KCI was due to CI- and came after association of newly synthesized L subunits with chaperonin 60, but before S subunit addition. It is interesting that L subunits synthesized at [greater than or equal to]32[deg]C failed to assemble into Rubisco under any conditions. These results agree with previous results obtained in this laboratory using newly synthesized L subunits made in intact chloroplasts. They also show that assembly of in vitro-synthesized L subunits into Rubisco requires ATP, that CI- inhibits Rubisco assembly, and that synthesis temperature affects subsequent assembly competence of L subunits.
在高等植物中,核酮糖二磷酸羧化酶/加氧酶(Rubisco)由八个在叶绿体中合成的大的“L”亚基和八个在细胞质中以前体形式合成的小的“S”亚基组成。这些亚基在导入和加工S亚基后,在叶绿体基质中组装成全酶。一种叶绿体伴侣蛋白与L亚基相互作用,L亚基在组装成全酶之前从伴侣蛋白上解离。我们实验室已经报道,在叶片、完整叶绿体以及最近在无膜叶绿体提取物中进行蛋白质合成后,L亚基在叶绿体提取物中组装成Rubisco。我们在此报告,体外合成的L亚基掺入全酶取决于L亚基的合成条件。在160 mM KCl条件下合成L亚基后,Rubisco组装未发生。当L亚基在约70 mM KCl条件下合成时,组装取决于L亚基合成时的温度。这些现象是蛋白质合成孵育期间发生的合成后事件的结果。我们通过在蛋白质合成期间降低温度将这些事件与蛋白质合成分开。较低温度支持全长Rubisco L亚基的合成。这些完整的L亚基组装成Rubisco需要在添加S亚基之前用ATP进行中间孵育。ATP处理使L亚基从与叶绿体伴侣蛋白60寡聚体的复合物中释放出来。在与ATP进行中间孵育开始时添加130 mM KCl会阻止L亚基掺入Rubisco。高KCl的抑制作用归因于Cl-,并且发生在新合成的L亚基与伴侣蛋白60结合之后,但在添加S亚基之前。有趣的是,在[大于或等于]32℃合成的L亚基在任何条件下都无法组装成Rubisco。这些结果与本实验室先前使用在完整叶绿体中合成的新合成L亚基获得的结果一致。它们还表明,体外合成的L亚基组装成Rubisco需要ATP,Cl-抑制Rubisco组装,并且合成温度影响L亚基随后的组装能力。