Swanson P C, Desiderio S
Department of Molecular Biology and Genetics, Howard Hughes Medical Institute, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA.
Immunity. 1998 Jul;9(1):115-25. doi: 10.1016/s1074-7613(00)80593-2.
Protein interactions with V(D)J recombination signal sequences (RSSs) were mapped in complexes containing RAG1 with (M1/2) or without (M1) RAG2. In both complexes, RAG interactions with the DNA backbone are biased toward one side of the helix; nonamer contacts resemble those of Hin with hixL. In the M1 complex, DNA contacts are centered on the nonamer. In the M1/2 complex, protein-RSS interactions extend through the spacer and into the nonamer-proximal portion of the heptamer. Chemical modifications near the heptamer-coding junction are overrepresented in the M1/2 complex, providing evidence for perturbation of DNA structure in this region. Thus, while RAG1 alone can bind the nonamer, RAG2 is required for heptamer occupancy.
在含有RAG1且有（M1/2）或没有（M1）RAG2的复合物中，绘制了蛋白质与V（D）J重组信号序列（RSSs）的相互作用。在这两种复合物中，RAG与DNA主链的相互作用偏向于螺旋的一侧；九聚体接触类似于Hin与hixL的接触。在M1复合物中，DNA接触集中在九聚体上。在M1/2复合物中，蛋白质-RSS相互作用延伸穿过间隔区并进入七聚体的九聚体近端部分。七聚体编码连接处附近的化学修饰在M1/2复合物中过度存在，为该区域DNA结构的扰动提供了证据。因此，虽然单独的RAG1可以结合九聚体，但七聚体占据需要RAG2。
