Zurla Chiara, Samuely Tomas, Bertoni Giovanni, Valle Francesco, Dietler Giovanni, Finzi Laura, Dunlap David D
Department of Physics, Emory University, Atlanta, GA 30322, USA.
Biophys Chem. 2007 Jul;128(2-3):245-52. doi: 10.1016/j.bpc.2007.04.012. Epub 2007 May 3.
The integration host factor protein of Escherichia coli, which sharply bends DNA at specific sites and non-specifically compacts the bacterial genome, can also alter looping of DNA in an artificial system based on the lactose repressor protein of E. coli. In single molecule experiments, we show that both specific bending and non-specific compaction alter LacI-mediated looping of DNA. Our results highlight the subtle regulatory roles that proteins, which confer structure upon DNA, might have in controlling DNA transcription and other processes in which the conformation of DNA determines the binding and activity of processive enzymes.
大肠杆菌的整合宿主因子蛋白可在特定位点使DNA急剧弯曲并使细菌基因组非特异性压缩,在基于大肠杆菌乳糖阻遏蛋白的人工系统中,它还能改变DNA的环化。在单分子实验中,我们发现特异性弯曲和非特异性压缩均会改变LacI介导的DNA环化。我们的结果突出了赋予DNA结构的蛋白质在控制DNA转录以及DNA构象决定进行性酶的结合与活性的其他过程中可能具有的微妙调控作用。