James H E, Bartling D, Musgrove J E, Kirwin P M, Herrmann R G, Robinson C
Department of Biological Sciences, University of Warwick, Coventry, United Kingdom.
J Biol Chem. 1989 Nov 25;264(33):19573-6.
The 33-, 23-, and 16-kDa proteins of the photosynthetic oxygen-evolving complex are synthesized as precursors in the cytoplasm and transported into the thylakoid lumen of higher plant chloroplasts. In this report we have analyzed the import and maturation of these precursors, using reconstituted protein import assays and partially purified preparations of the processing peptidases involved. Precursors of the 33- and 23-kDa proteins from Spinacia and Triticum aestivum are processed by a stromal peptidase to intermediate forms; polypeptides of similar size are observed during the transport of these precursors and possibly that of the 16-kDa protein, into isolated chloroplasts. Complete maturation of the 33- and 23-kDa proteins is carried out by a thylakoidal peptidase shown previously to be involved in plastocyanin biogenesis. The data support an import mechanism involving successive cleavages by the stromal and thylakoidal processing peptidases.
光合放氧复合体的33 kDa、23 kDa和16 kDa蛋白质在细胞质中以前体形式合成,并被转运到高等植物叶绿体的类囊体腔中。在本报告中,我们使用重组蛋白导入分析方法以及所涉及的加工肽酶的部分纯化制剂,分析了这些前体的导入和成熟过程。菠菜和普通小麦的33 kDa和23 kDa蛋白质前体由一种基质肽酶加工成中间形式;在这些前体以及可能的16 kDa蛋白质向分离的叶绿体转运过程中,观察到了大小相似的多肽。33 kDa和23 kDa蛋白质的完全成熟是由一种先前已证明参与质体蓝素生物合成的类囊体肽酶完成的。数据支持一种涉及基质和类囊体加工肽酶连续切割的导入机制。