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首页> 外文期刊>Protoplasma: An International Journal of Cell Biology >Accumulation of extracellular proteins bearing unique proline-rich motifs in intercellular spaces of the legume nodule parenchyma
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Accumulation of extracellular proteins bearing unique proline-rich motifs in intercellular spaces of the legume nodule parenchyma

机译：豆科结节实质细胞间空间中携带独特的富含脯氨酸基序的细胞外蛋白的积累

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Nodulins encoding repetitive proline-rich cell wall proteins (PRPs) are induced during early interactions with rhizobia, suggesting a massive restructuring of the plant extracellular matrix during infection and nodulation. However, the proteins corresponding to these gene products have not been isolated or characterized, nor have cell wall localizations been confirmed. Posttranslational modifications, conformation, and interactions with other wall polymers are difficult to predict on the basis of only the deduced amino acid sequence of PRPs. PsENOD2 is expressed in nodule parenchyma tissue during nodule organogenesis and encodes a protein with distinctive PRP motifs that are rich in glutamate and basic amino acids. A database search for the ENOD2 signature motifs indicates that similar proteins may have a limited phylogenetic distribution, as they are presently only known from legumes. To determine the ultrastructural location of the proteins, antibodies were raised against unique motifs from the predicted ENOD2 sequence. The antibodies recognized nodule-specific proteins in pea (Pisum sativum), with a major band detected at 110 kDa, representing a subset of PRPs from nodules. The protein was detected specifically in organelles of the secretory pathway and intercellular spaces in the nodule parenchyma, but it was not abundant in primary walls. Similar proteins with an analogous distribution were detected in soybean (Glycine max). The use of polyclonal antibodies raised against signature motifs of extracellular matrix proteins thus appears to be an effective strategy to identify and isolate specific structural proteins for functional analysis.
机译：在与根瘤菌的早期相互作用期间，诱导编码重复的富含脯氨酸的细胞壁蛋白（PRPs）的结节蛋白，表明在感染和结瘤过程中植物细胞外基质的大规模重组。但是，尚未分离或表征与这些基因产物相对应的蛋白质，也未确认细胞壁的定位。仅根据推导的PRP的氨基酸序列很难预测翻译后修饰，构象以及与其他壁聚合物的相互作用。 PsENOD2在结节器官发生期间在结节实质组织中表达，并编码具有独特的PRP基序的蛋白，该蛋白富含谷氨酸和碱性氨基酸。对ENOD2签名基序的数据库搜索表明，相似的蛋白质可能具有有限的系统发育分布，因为目前仅从豆类中才知道它们。为了确定蛋白质的超微结构位置，产生了针对来自预测的ENOD2序列的独特基序的抗体。抗体识别豌豆（Pisum sativum）中的根瘤特异性蛋白，在110 kDa处检测到一条主要谱带，代表了根瘤中PRP的一个子集。该蛋白是在结节实质中的分泌途径的细胞器和细胞间空间中特异性检测到的，但在原壁中并不丰富。在大豆中检测到具有相似分布的相似蛋白质（Glycine max）。因此，针对细胞外基质蛋白特征性基序的多克隆抗体的使用看来是鉴定和分离用于功能分析的特定结构蛋白的有效策略。

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