Halligan B D, Teng M, Guilliams T G, Nauert J B, Halligan N L
Department of Microbiology, Medical College of Wisconsin, Milwaukee 53226, USA.
Gene. 1995 Aug 19;161(2):217-22. doi: 10.1016/0378-1119(95)00299-l.
A putative full-length 1.7-kb cDNA, encoding a murine protein that specifically binds to the nonamer portion of the V(D)J recombinational signal sequence (RSS) element, has been cloned. By its sequence analysis, this cDNA is identical to a portion of the 4.5-kb murine replication factor C large-subunit-encoding cDNA. By Northern blot analysis, the 1.7-kb mRNA species is observed in murine immature B cells but not in non-lymphoid cells and tissues, while the 4.5-kb replication factor C-encoding cDNA is expressed in all cell types. The deduced VDJP amino-acid sequence includes a region of homology with bacterial DNA ligases at the C terminus of each of the proteins. VDJP has been synthesized as a fusion protein in bacteria, and the purified protein has been previously shown to mediate the joining of DNA fragments in a V(D)J RSS-dependent fashion (Guilliams et al., Biochem. Biophys. Res. Commun. 202 (1994) 1134-1141).
已克隆出一个推测的全长1.7kb cDNA,其编码一种小鼠蛋白,该蛋白能特异性结合V(D)J重组信号序列(RSS)元件的九聚体部分。通过序列分析,该cDNA与4.5kb小鼠复制因子C大亚基编码cDNA的一部分相同。通过Northern印迹分析,在小鼠未成熟B细胞中观察到1.7kb的mRNA种类,而非淋巴细胞和组织中未观察到,而4.5kb复制因子C编码cDNA在所有细胞类型中均有表达。推导的VDJP氨基酸序列在每个蛋白质的C末端包含一个与细菌DNA连接酶同源的区域。VDJP已在细菌中作为融合蛋白合成,并且先前已证明纯化的蛋白能以V(D)J RSS依赖的方式介导DNA片段的连接(Guilliams等人,《生物化学与生物物理研究通讯》202 (1994) 1134 - 1141)。