PURIFICATION AND CHARACTERIZATION OF A PROTEIN THAT BINDS TO THE RECOMBINATION SIGNAL SEQUENCE OF THE IMMUNOGLOBULIN-J-ALEPH SEGMENT
PURIFICATION AND CHARACTERIZATION OF A PROTEIN THAT BINDS TO THE RECOMBINATION SIGNAL SEQUENCE OF THE IMMUNOGLOBULIN-J-ALEPH SEGMENT
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DOI：
10.1093/nar/17.22.9015
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发表时间：
1989-11-25
影响因子：
14.9
通讯作者：
HONJO, T
中科院分区：
文献类型：
--
作者：
HAMAGUCHI, Y;MATSUNAMI, N;HONJO, T
一种与免疫球蛋白J κ的重组信号序列（RS）结合的蛋白质。从鼠前B细胞系38 B 9的核提取物中纯化片段几乎至均一。在淋巴样细胞系中发现了类似的结合蛋白，但在非淋巴样细胞系中未发现。结合活性与分子量为60，000的多肽相关。DNA酶I足迹分析表明，该结合蛋白与七聚体和靠近七聚体的几个3“碱基相互作用。J. vkappa. RS结合蛋白的J. vkappa。RS为1 nM。在J. vkappa的七聚体中的一个碱基替换。RS大大降低了J. vkappa的亲和力。RS结合蛋白高特异性的结合位点的J. vkappa。RS结合蛋白表明该蛋白可能参与V-J重组。
A protein that binds to the recombination signal sequence (RS) of the immunoglobulin J.vkappa. segment was purified almost to homogeneity from the nuclear extract of a murine pre-B cell line 38B9. A similar binding protein was found in lymphoid cell lines but not in non-lymphoid cell lines. The binding activity was associated with a polypeptide with a molecular weight of 60,000. DNase I footprinting analysis demonstrated that this binding protein interacted with the heptamer and several 3'' base close to the heptamer. The Kd value of the J.vkappa. RS binding protein to the J.vkappa. RS was 1nM. One base substitution in the heptamer of the J.vkappa. RS greatly reduced the affinity of the J.vkappa. RS binding protein. The high specificity of the binding site of the J.vkappa. RS binding protein suggests that this protein may be involved in V-J recombination.