Kuroda I, Inagaki J, Yamamoto Y
Department of Biology, Faculty of Science, Okayama University, Japan.
Plant Mol Biol. 1993 Jan;21(1):171-6. doi: 10.1007/BF00039627.
Polyprotein-type precursors have been reported for the nuclear-encoded proteins such as the small subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) and the apoproteins of light-harvesting chlorophyll-protein (LHC) in Euglena. We report here that the precursor of the extrinsic 30 kDa protein of photosystem II (PS II) encoded by nuclear DNA is not a polyprotein. The precursor was identified as a 45 kDa protein by immunoprecipitation of in vitro translation products of mRNA and by a pulse-chase experiment. It is probable that the structure of the precursor of the nuclear-encoded protein in Euglena chloroplast is closely related to the feature of assembly, as well as of transport, of the protein in chloroplast.
据报道,在眼虫中,核编码蛋白如1,5-二磷酸核酮糖羧化酶/加氧酶(Rubisco)的小亚基和捕光叶绿素蛋白(LHC)的脱辅基蛋白存在多蛋白类型的前体。我们在此报告,由核DNA编码的光系统II(PS II)的30 kDa外在蛋白的前体不是多蛋白。通过对mRNA体外翻译产物进行免疫沉淀以及脉冲追踪实验,该前体被鉴定为一种45 kDa的蛋白。眼虫叶绿体中核编码蛋白前体的结构可能与该蛋白在叶绿体中的组装以及转运特性密切相关。