A RAG1 and RAG2 tetramer complex is active in cleavage in V(D)J recombination.
A RAG1 and RAG2 tetramer complex is active in cleavage in V(D)J recombination.
复制标题
RAG1 和 RAG2 四聚体复合物在 V(D)J 重组中的裂解中具有活性。
DOI：
10.1128/mcb.19.7.4664
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发表时间：
1999
影响因子：
5.3
通讯作者：
Sadofsky,MJ
中科院分区：
文献类型：
--
作者：
Bailin,T;Mo,X;Sadofsky,MJ
在V(D)J重组过程中，RAG1和RAG2蛋白与含有重组信号序列（RSSs）的合适DNA靶点组装成蛋白质-DNA复合物。这种复合物的性质需要一套相当复杂的蛋白质-蛋白质和蛋白质- dna接触。在这里，我们证明了RAG1的纯化衍生物，没有DNA，主要以同二聚体的形式存在。RAG2衍生物有单体、二聚体和更大的形式。共表达的RAG1和RAG2蛋白在溶液中形成混合四聚体，每种蛋白含有两个分子。RAG1和RAG2的相同四聚体加上一个DNA分子是在裂解中活跃的形式。此外，我们表明，切割后的两个DNA产物仍然可以在一个稳定的蛋白质-DNA复合体中结合在一起。
During V(D)J recombination two proteins, RAG1 and RAG2, assemble as a protein-DNA complex with the appropriate DNA targets containing recombination signal sequences (RSSs). The properties of this complex require a fairly elaborate set of protein-protein and protein-DNA contacts. Here we show that a purified derivative of RAG1, without DNA, exists predominantly as a homodimer. A RAG2 derivative alone has monomer, dimer, and larger forms. The coexpressed RAG1 and RAG2 proteins form a mixed tetramer in solution which contains two molecules of each protein. The same tetramer of RAG1 and RAG2 plus one DNA molecule is the form active in cleavage. Additionally, we show that both DNA products following cleavage can still be held together in a stable protein-DNA complex.