van Vuuren A J, Appeldoorn E, Odijk H, Humbert S, Moncollin V, Eker A P, Jaspers N G, Egly J M, Hoeijmakers J H
Department of Cell Biology and Genetics, Erasmus University Rotterdam, The Netherlands.
Mutat Res. 1995 Jul;337(1):25-39. doi: 10.1016/0921-8777(95)00009-9.
The nucleotide excision repair (NER) protein ERCC1 is part of a functional complex, which harbors in addition the repair correcting activities of ERCC4, ERCC11 and human XPF. ERCC1 is not associated with a defect in any of the known human NER disorders: xeroderma pigmentosum, Cockayne's syndrome or trichothiodystrophy. Here we report the partial purification and characterization of the ERCC1 complex. Immunoprecipitation studies tentatively identified a subunit in the complex with an apparent MW of approximately 120 kDa. The complex has affinity for DNA, but no clear preference for ss, ds or UV-damaged DNA substrates. The size of the entire complex determined by non-denaturing gradient gels (approximately 280 kDa) is considerably larger than previously found using size separation on glycerol gradients (approximately 120 kDa). Stable associations of the ERCC1 complex with other known repair factors (XPA, XPC, XPG and TFIIH complex) could not be detected.
核苷酸切除修复（NER）蛋白ERCC1是一个功能复合体的组成部分，该复合体还具有ERCC4、ERCC11和人类XPF的修复校正活性。ERCC1与任何已知的人类NER疾病（着色性干皮病、科凯恩综合征或毛发硫营养不良）的缺陷均无关联。在此，我们报告了ERCC1复合体的部分纯化及特性。免疫沉淀研究初步鉴定出复合体中一个表观分子量约为120 kDa的亚基。该复合体对DNA具有亲和力，但对单链、双链或紫外线损伤的DNA底物没有明显偏好。通过非变性梯度凝胶测定的整个复合体大小（约280 kDa）比之前在甘油梯度上进行大小分离所发现的（约120 kDa）要大得多。未检测到ERCC1复合体与其他已知修复因子（XPA、XPC、XPG和TFIIH复合体）的稳定关联。
