Dame Remus Th
Department of Physics and Astronomy and Laser Centre, VU University Amsterdam, Amsterdam, The Netherlands.
Biochem Soc Trans. 2008 Aug;36(Pt 4):732-7. doi: 10.1042/BST0360732.
Architectural proteins play a key role in the folding, organization and compaction of genomic DNA in all organisms. By bending, bridging or wrapping DNA, these proteins ensure that its effective volume is reduced sufficiently to fit inside the cell or a dedicated cellular organelle, the nucleus (in bacteria/archaea and in eukaryotes respectively). In addition, the properties of many of these proteins permit them to play specific roles as architectural cofactors in a large variety of DNA transactions. However, as architectural proteins often bind DNA with low sequence specificity and affinity, it is hard to investigate their interaction using biochemical ensemble techniques. Single-molecule micromanipulation approaches that probe the properties of DNA-binding proteins by pulling on individual protein-DNA complexes have, in this respect, proved to be a very powerful alternative. Besides revealing architectural properties, these approaches can also reveal unique parameters not accessible to biochemical approaches, such as the binding kinetics and unbinding forces of individual proteins.
结构蛋白在所有生物体基因组DNA的折叠、组织和压缩过程中发挥着关键作用。通过弯曲、桥接或缠绕DNA，这些蛋白质确保其有效体积充分减小，以分别适应细菌/古菌和真核生物的细胞或特定细胞器——细胞核内部。此外，许多这类蛋白质的特性使其能够在多种DNA交易中作为结构辅助因子发挥特定作用。然而，由于结构蛋白通常以低序列特异性和亲和力结合DNA，因此很难使用生化整体技术研究它们之间的相互作用。在这方面，通过拉动单个蛋白质-DNA复合物来探测DNA结合蛋白特性的单分子微操纵方法已被证明是一种非常有效的替代方法。除了揭示结构特性外，这些方法还能揭示生化方法无法获得的独特参数，例如单个蛋白质的结合动力学和解离力。
