Chloroplast Protein Turnover: The Influence of Extraplastidic Processes, Including Autophagy.
Chloroplast Protein Turnover: The Influence of Extraplastidic Processes, Including Autophagy.
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DOI：
10.3390/ijms19030828
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发表时间：
2018-03-12
影响因子：
5.6
通讯作者：
Nakamura S
中科院分区：
文献类型：
--
作者：
Izumi M;Nakamura S
陆地植物叶片中的大多数同化营养素作为光合蛋白储存在叶绿体中，在生长期间介导CO2同化。在衰老期间或在次优条件下，叶绿体蛋白质被降解，并且在此过程中释放的氨基酸用于产生年轻的组织、种子或呼吸能量。蛋白质降解机制有助于叶绿体的质量控制，通过去除由来自阳光的过量能量引起的受损蛋白质。而以前的研究表明，叶绿体含有几种类型的可能来自叶绿体的内共生原核祖先的质内蛋白酶，最近的报告表明，多extrapastidic途径也有助于叶绿体蛋白质周转响应特定的线索。一种这样的途径是自噬，这是一种进化上保守的过程，导致真核细胞中细胞质组分的空泡或溶酶体降解。在这里，我们描述和对比降解叶绿体的质体外途径。本文综述了在糖饥饿、衰老和氧化胁迫过程中，叶绿体的更新过程中有多种途径参与。阐明调节这些途径的机制将有助于破译介导叶绿体蛋白质周转的不同途径之间的关系。
Most assimilated nutrients in the leaves of land plants are stored in chloroplasts as photosynthetic proteins, where they mediate CO2 assimilation during growth. During senescence or under suboptimal conditions, chloroplast proteins are degraded, and the amino acids released during this process are used to produce young tissues, seeds, or respiratory energy. Protein degradation machineries contribute to the quality control of chloroplasts by removing damaged proteins caused by excess energy from sunlight. Whereas previous studies revealed that chloroplasts contain several types of intraplastidic proteases that likely derived from an endosymbiosed prokaryotic ancestor of chloroplasts, recent reports have demonstrated that multiple extraplastidic pathways also contribute to chloroplast protein turnover in response to specific cues. One such pathway is autophagy, an evolutionarily conserved process that leads to the vacuolar or lysosomal degradation of cytoplasmic components in eukaryotic cells. Here, we describe and contrast the extraplastidic pathways that degrade chloroplasts. This review shows that diverse pathways participate in chloroplast turnover during sugar starvation, senescence, and oxidative stress. Elucidating the mechanisms that regulate these pathways will help decipher the relationship among the diverse pathways mediating chloroplast protein turnover.
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