Kim S K, Kaiser D
Department of Biochemistry, Stanford University School of Medicine, California 94305.
Proc Natl Acad Sci U S A. 1990 May;87(10):3635-9. doi: 10.1073/pnas.87.10.3635.
C-factor, a Myxococcus xanthus protein that restores the developmental defects of a class of nonautonomous mutants resulting from mutation of the csgA gene, has been purified approximately 1000-fold from starved wild-type cells. The monomeric form of C-factor is a single polypeptide with a molecular mass of 17 kDa that can be solubilized by detergent from membrane components. Characterization by gel filtration and denaturing gel electrophoresis suggests that biologically active C-factor is a dimer composed of two 17-kDa monomers. Antibodies against a form of the M. xanthus csgA gene product overexpressed in Escherichia coli react with purified C-factor.
C因子是一种来自黄色粘球菌的蛋白质，它能够修复因csgA基因突变导致的一类非自主突变体的发育缺陷，已从饥饿的野生型细胞中纯化了约1000倍。C因子的单体形式是一种分子量为17 kDa的单一多肽，可通过去污剂从膜成分中溶解出来。凝胶过滤和变性凝胶电泳分析表明，具有生物活性的C因子是由两个17 kDa单体组成的二聚体。针对在大肠杆菌中过表达的黄色粘球菌csgA基因产物的一种形式所产生的抗体与纯化的C因子发生反应。
