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首页> 外文期刊>Journal of Experimental Botany >Cysteine proteinases regulate chloroplast protein content and composition in tobacco leaves: a model for dynamic interactions with ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) vesicular bodies
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Cysteine proteinases regulate chloroplast protein content and composition in tobacco leaves: a model for dynamic interactions with ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) vesicular bodies

机译：半胱氨酸蛋白酶调节烟叶中叶绿体蛋白的含量和组成：与核糖-1,5-双磷酸羧化酶/加氧酶（Rubisco）囊泡体动态相互作用的模型

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The roles of cysteine proteinases (CP) in leaf protein accumulation and composition were investigated in transgenic tobacco (Nicotiana tabacum L.) plants expressing the rice cystatin, OC-1. The OC-1 protein was present in the cytosol, chloroplasts, and vacuole of the leaves of OC-1 expressing (OCE) plants. Changes in leaf protein composition and turnover caused by OC-1-dependent inhibition of CP activity were assessed in 8-week-old plants using proteomic analysis. Seven hundred and sixty-five soluble proteins were detected in the controls compared to 860 proteins in the OCE leaves. A cyclophilin, a histone, a peptidyl-prolyl cis-trans isomerase, and two ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) activase isoforms were markedly altered in abundance in the OCE leaves. The senescence-related decline in photosynthesis and Rubisco activity was delayed in the OCE leaves. Similarly, OCE leaves maintained higher leaf Rubisco activities and protein than controls following dark chilling. Immunogold labelling studies with specific antibodies showed that Rubisco was present in Rubisco vesicular bodies (RVB) as well as in the chloroplasts of leaves from 8-week-old control and OCE plants. Western blot analysis of plants at 14 weeks after both genotypes had flowered revealed large increases in the amount of Rubisco protein in the OCE leaves compared to controls. These results demonstrate that CPs are involved in Rubisco turnover in leaves under optimal and stress conditions and that extra-plastidic RVB bodies are present even in young source leaves. Furthermore, these data form the basis for a new model of Rubisco protein turnover involving CPs and RVBs.
机译：在表达水稻半胱氨酸蛋白酶抑制剂OC-1的转基因烟草（Nicotiana tabacum L.）植物中，研究了半胱氨酸蛋白酶（CP）在叶片蛋白质积累和组成中的作用。 OC-1蛋白存在于表达OC-1的（OCE）植物的细胞质，叶绿体和液泡中。使用蛋白质组学分析评估了8周龄植物中由OC-1依赖性抑制CP活性引起的叶片蛋白质组成和周转率的变化。与OCE叶片中的860种蛋白质相比，对照中检测到765种可溶性蛋白质。 OCE叶片的丰度显着改变了亲环蛋白，组蛋白，肽基-脯氨酰顺反异构酶和两个1,5-双磷酸核糖羧化酶/加氧酶（Rubisco）活化酶同工型。 OCE叶片延迟了衰老相关的光合作用和Rubisco活性下降。类似地，暗冷后，OCE叶片保持比对照更高的叶片Rubisco活性和蛋白质。用特异性抗体进行的免疫金标记研究表明，Rubisco存在于Rubisco囊泡体（RVB）以及8周龄对照和OCE植物叶片的叶绿体中。两种基因型都开花后第14周对植物进行的蛋白质印迹分析表明，与对照相比，OCE叶片中Rubisco蛋白的含量大大增加。这些结果表明，在最佳和胁迫条件下，CPs参与了Rubisco叶片的周转，即使幼源叶片中也存在质外RVB体。此外，这些数据构成了涉及CP和RVB的Rubisco蛋白更新新模型的基础。

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    《Journal of Experimental Botany》 |2008年第7期|p.1935-1950|共16页
  • 作者

    Anneke Prins12 Philippus D.R. van Heerden3 Enrique Olmos4 Karl J. Kunert2 and Christine H. Foyer1*;

  • 作者单位

    1School of Agriculture, Food and Rural Development, Agriculture Building, Newcastle University, Newcastle upon Tyne NE1 7RU, UK 2Forestry and Agricultural Biotechnology Institute, Botany Department, University of Pretoria, Pretoria 0002, South Africa 3School of Environmental Sciences and Development, Section Botany, North-West University, Potchefstroom 2520, South Africa 4CEBAS-CSIC, Department of Plant Physiology, PO Box 164, E-30080 Murcia, Spain;

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