Jacq A, Kern R, Tsugita A, Kohiyama M
Institut Jacques Monod, Universite Paris, France.
J Bacteriol. 1989 Mar;171(3):1409-16. doi: 10.1128/jb.171.3.1409-1416.1989.
A purification procedure was devised for a low-molecular-mass (about 10-kilodalton) membrane protein from Escherichia coli that was shown to bind specifically to the chromosomal replication origin region (oriC). Nitrocellulose membrane retention assays showed the binding site to be adjacent to the right boundary of the oriC minimal sequence. We determined the amino acid sequence of the N-terminal and C-terminal regions as well as the global amino acid composition of this membrane protein. Specific antibodies against the protein were produced and used to confirm the cell membrane location of the protein. These results demonstrate that this is a new membrane protein, different from the previously described B' protein, with specific binding activity for the oriC region. We propose that this protein be called membrane oriC-binding protein 2 (MOB2 protein).
设计了一种从大肠杆菌中纯化低分子量（约10千道尔顿）膜蛋白的方法，该蛋白被证明能特异性结合染色体复制起始区域（oriC）。硝酸纤维素膜保留试验表明结合位点与oriC最小序列的右边界相邻。我们确定了该膜蛋白N端和C端区域的氨基酸序列以及整体氨基酸组成。制备了针对该蛋白的特异性抗体，并用于确认该蛋白在细胞膜上的定位。这些结果表明这是一种新的膜蛋白，不同于先前描述的B'蛋白，对oriC区域具有特异性结合活性。我们建议将该蛋白称为膜oriC结合蛋白2（MOB2蛋白）。
