Shigemori Y, Inagaki J, Mori H, Nishimura M, Takahashi S, Yamamoto Y
Department of Biology, Faculty of Science, Okayama University, Japan.
Plant Mol Biol. 1994 Jan;24(1):209-15. doi: 10.1007/BF00040587.
A cDNA clone for the extrinsic 30 kDa protein (OEC30) of photosystem II in Euglena gracilis Z was isolated and characterized. The open reading frame of the cDNA encoded a polypeptide of 338 amino acids, which consisted of a long presequence of 93 amino acids and a mature polypeptide of 245 amino acids. Two hydrophobic domains were identified in the presequence, in contrast to the presence of a single hydrophobic domain in the presequence of the corresponding proteins from higher plants. At the N- and C-terminal regions, respectively, of the presequence, a signal-peptide-like sequence and a thylakoid-transfer domain were identified. The presence of a long and unique presequence in the precursor to OEC30 is probably related to the complexity of the intracellular processes required for the synthesis and/or transport of the protein in Euglena.
分离并鉴定了纤细裸藻（Euglena gracilis Z）光系统II外在30 kDa蛋白（OEC30）的cDNA克隆。该cDNA的开放阅读框编码一个由338个氨基酸组成的多肽，其中包括一个由93个氨基酸组成的长前导序列和一个由245个氨基酸组成的成熟多肽。在前导序列中鉴定出两个疏水结构域，这与高等植物相应蛋白前导序列中存在单个疏水结构域形成对比。在前导序列的N端和C端区域分别鉴定出一个信号肽样序列和一个类囊体转运结构域。OEC30前体中存在长且独特的前导序列可能与裸藻中该蛋白合成和/或运输所需的细胞内过程的复杂性有关。
