Hattman S, Sun W
Department of Biology, University of Rochester, Rochester, NY 14627, USA.
Nucleic Acids Res. 1997 Nov 1;25(21):4385-8. doi: 10.1093/nar/25.21.4385.
Transcription of the bacteriophage Mu mom operon is strongly repressed by the host OxyR protein in dam - but not dam + cells. In this work we show that the extent of mom modification is sensitive to the relative levels of the Dam and OxyR proteins and OxyR appears to modulate the level of mom expression even in dam + cells. In vitro studies demonstrated that OxyR is capable of binding hemimethylated P mom , although its affinity is reduced slightly compared with unmethylated DNA. Thus, OxyR modulation of mom expression in dam + cells can be attributed to its ability to bind hemimethylated P mom DNA, the product of DNA replication.
噬菌体Mu mom操纵子的转录在dam - 细胞而非dam + 细胞中受到宿主OxyR蛋白的强烈抑制。在本研究中,我们发现mom修饰的程度对Dam和OxyR蛋白的相对水平敏感,并且即使在dam + 细胞中,OxyR似乎也能调节mom的表达水平。体外研究表明,OxyR能够结合半甲基化的P mom ,尽管与未甲基化的DNA相比,其亲和力略有降低。因此,OxyR在dam + 细胞中对mom表达的调节可归因于其结合DNA复制产物半甲基化P mom DNA的能力。