PURIFICATION, PRIMARY STRUCTURE, AND HOMOLOGY RELATIONSHIPS OF A CHLOROPLAST RIBOSOMAL-PROTEIN
PURIFICATION, PRIMARY STRUCTURE, AND HOMOLOGY RELATIONSHIPS OF A CHLOROPLAST RIBOSOMAL-PROTEIN
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DOI：
10.1073/pnas.79.22.6871
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发表时间：
1982-01-01
期刊：
影响因子：
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通讯作者：
SUBRAMANIAN, AR
中科院分区：
文献类型：
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作者：
BARTSCH, M;KIMURA, M;SUBRAMANIAN, AR
从菠菜 (Spinacia oleracea) 叶子中纯化出与大肠杆菌核糖体蛋白 L12 表现出免疫同源性的叶绿体核糖体蛋白，并通过手动微 Edman 降解测定了其一级结构。该蛋白质由 130 个氨基酸残基组成，分子量为 13,576。它显示了真细菌 70S 核糖体的 L12 蛋白的结构特征（例如，大约 50% 的序列中具有相同的氨基酸残基），但与真核细胞质 80S 核糖体的 L12 型蛋白没有明显的同源性。与真细菌蛋白的同源性在 COOH 末端区域最高 (70%)，在 NH2 末端区域较低 (< 20%)。
A chloroplast ribosomal protein that showed immunological homology to Escherichia coli ribosomal protein L12 was purified from spinach (Spinacia oleracea) leaves and its primary structure was determined by manual micro Edman degradation. The protein is composed of 130 amino acid residues and has MW 13,576. It shows structural features characteristic of the L12 proteins of eubacterial 70S ribosomes (e.g., identical amino acid residues in about 50% of the sequence) but no apparent homology to the L12-type proteins of eukaryotic cytoplasmic 80S ribosomes. The homology to eubacterial proteins is highest in the COOH-terminal region (70%) and low in the NH2-terminal region (< 20%).