Postimport methylation of the small subunit of ribulose-1,5-bisphosphate carboxylase in chloroplasts
Postimport methylation of the small subunit of ribulose-1,5-bisphosphate carboxylase in chloroplasts
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DOI：
10.1016/s0014-5793(97)00462-6
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发表时间：
1997-05-26
期刊：
影响因子：
3.5
通讯作者：
Soll, J
中科院分区：
文献类型：
--
作者：
Grimm, R;Grimm, M;Soll, J
核酮糖-1,5-二磷酸羧化酶（Rubisco）小亚基（SSU）氨基末端氨基酸的电子轰击质谱分析表明，氨基末端甲硫氨酸残基被翻译后修饰为N-甲基甲硫氨酸。在双子叶植物豌豆和菠菜以及单子叶植物大麦和玉米的成熟 SSU 蛋白中发现氨基末端蛋氨酸残基的修饰，SSU 甲基转移酶是叶绿体基质中的可溶性蛋白，并使用 S-腺苷甲硫氨酸接受异源表达的非甲基化 SSU 作为底物 我们表明，这种修饰发生在 SSU 前体形式翻译后摄取到叶绿体中并加工至其成熟尺寸之后，该反应代表了 Rubisco 全酶导入和组装途径的新一步。 (C) 1997 年欧洲生化学会联合会。
Electron impact mass spectronomy analysis of the amino-terminal amino acid of the small subunit (SSU) of ribulose-1,5-bisphosphate carboxylase (Rubisco) showed that the amino-terminal methionine residue is post-translationally modified to N-methyl-methionine. Modification of the amino-terminal methionine residue was found in mature SSU proteins from the dicotyledonous plants pea and spinach as well as the monocotyledonous plants barley and corn, SSU methyltransferase is a soluble protein in the chloroplast stroma and accepts heterologously expressed non-methylated SSU as a substrate using S-adenosylmethionine as methyl-group donor, We show that this modification occurs after post-translational uptake of the precursor form of SSU into chloroplasts and processing to its mature size, This reaction represents a new step in the import and assembly pathway of Rubisco holoenzyme. (C) 1997 Federation of European Biochemical Societies.