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rag-1 and rag-2 are components of a high-molecular-weight complex, and association of rag-2 with this complex is rag-1 dependent.

机译:rag-1和rag-2是高分子量复合物的组成部分,而rag-2与该复合物的结合取决于rag-1。

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Despite the essential and synergistic functions of the rag-1 and rag-2 proteins in V(D)J recombination and lymphocyte development, little is known about the biochemical properties of the two proteins. We have developed cell lines expressing high levels of the rag proteins and specific, sensitive immunological reagents for their detection, and we have examined the physical properties of the rag proteins in vitro and their subcellular localizations in vivo. rag-1 is tightly associated with nuclear structures, requires a high salt concentration to maintain its solubility, and is a component of large, heterogeneously sized complexes. Furthermore, the presence of rag-1 alters the behavior of rag-2, conferring on it properties similar to those of rag-1 and changing its distribution in the nucleus. We demonstrate that rag-1 and rag-2 are present in the same complex by coimmunoprecipitation, and we provide evidence that these complexes contain more molecules of rag-2 than of rag-1. The demonstration of intracellular complexes containing rag-1 and rag-2 raises the possibility that interaction between these proteins is necessary for their biological function.
机译:尽管rag-1和rag-2蛋白在V(D)J重组和淋巴细胞发育中起着必不可少的协同作用,但对这两种蛋白的生化特性知之甚少。我们已经开发了表达高水平的rag蛋白和特异性,灵敏的免疫试剂进行检测的细胞系,并且已经研究了rag蛋白的体外物理特性及其在体内的亚细胞定位。 rag-1与核结构紧密相关,需要高盐浓度才能保持其溶解度,并且是大型,异质复合物的组成部分。此外,rag-1的存在改变了rag-2的行为,赋予了其与rag-1相似的特性,并改变了其在细胞核中的分布。我们证明了rag-1和rag-2通过共免疫沉淀法存在于同一复合物中,并且我们提供的证据表明这些复合物比rag-1包含更多的rag-2分子。包含rag-1和rag-2的细胞内复合物的演示增加了这些蛋白质之间的相互作用对其生物学功能所必需的可能性。

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