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首页> 外文会议>International Congress of Photosynthesis >INVOLVEMENT OF A TYPE I SIGNAL PEPTIDASE IN BIOGENESIS OF CHLOROPLASTS-TOWARDS IDENTIFICATION OF THE ENZYME FOR MATURATION OF THE CHLOROPLAST PROTEIN TRANSLOCATION CHANNEL
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INVOLVEMENT OF A TYPE I SIGNAL PEPTIDASE IN BIOGENESIS OF CHLOROPLASTS-TOWARDS IDENTIFICATION OF THE ENZYME FOR MATURATION OF THE CHLOROPLAST PROTEIN TRANSLOCATION CHANNEL

机译：I型信号肽酶参与叶绿体生物发生 - 朝向叶绿体蛋白易位通道成熟的酶

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Most chloropl ast proteins are encoded in the nucleus, synthesized inthe cytoplasm, and targeted to the organelles posttranslationally. Therefore, protein import is a prerequisite for the biogenesis of chloroplasts. Toc75 forms the protein translocation channel in the chloroplast outer envelope (Keegstra & Cline 1999). It is the only protein identified so far in the outer membrane of chloroplast envelope or mitochondrion that requires a cleavable transit peptide for its biogenesis (Schleiff & Klosgen2001). The transit peptide of the Toc75 precursor, tp75, consists of two parts (Fig. 1; Tranel et al 1995). The first domain, tpn75, can target the protein into the stroma and appears to be removed by the stromal processing peptidase, SPP (Tranel & Keegstra 1996). SPP is a soluble metalloendopeptidase and postulated to be responsible for processing most, if not all, chloroplast precursor proteins (Richter & Lamppa 1998). Tpn75 by itself was shown to interact with chloroplast lipids and can inhibit targeting of other precursor proteins to chloroplasts (Inoue et al 2001). The second part of the Toc75 transit peptide, tpc75, is necessary but not sufficient for targeting the protein to the chloroplast envelope (Tranel & Keegstra 1996). It contains a unique polyglycine stretch essential to keep Toc75 from traversing the envelope membranes into the stroma (Inoue & Keegstra 2003). On the other hand, the peptidase responsible for complete maturation of Toc75 remains unidentified. In this paper, an approach towards identification of this enzyme is described.
机译：大多数斑氏AST蛋白质在核中编码，合成的肌胞质，后期靶向细胞器。因此，蛋白质进口是叶绿体生物发生的先决条件。 TOC75在叶绿体外壳中形成蛋白质易位通道（Keegstra和Cline 1999）。它是迄今为止在叶绿体包膜外膜或线粒体中鉴定的唯一蛋白质，其需要用于其生物发生的可切割的过渡肽（Schleiff＆Klosgen2001）。 TOC75前体TP75的过渡肽由两部分组成（图1; Tranel等1995）。第一结构域TPN75可以将蛋白质靶向基质中，并且似乎被基质加工肽酶，SPP（Tranel＆Keegstra 1996）除去。 SPP是一种可溶性金属丁基肽酶，假设负责加工，如果不是全部，叶绿体前体蛋白（Richter＆Lamppa 1998）。 TPN75本身被证明与叶绿体脂质相互作用，并且可以抑制其他前体蛋白质对叶绿体的靶向（Inoue等，2001）。 TOC75过渡肽，TPC75的第二部分是必需的，但不足以靶向蛋白质到叶绿体封套（Tranel＆Keegstra 1996）。它含有独特的聚葡萄酒延伸，可以使TOC75穿过包膜膜进入基质（INOUE＆KEEGSTRA 2003）。另一方面，负责TOC75完全成熟的肽酶仍未认定。在本文中，描述了一种探索该酶的方法。

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