Bondeson K, Rönn O, Magnusson G
Department of Medical Immunology and Microbiology, Uppsala University, Biomedical Centre, Sweden.
FEBS Lett. 1998 Feb 27;423(3):307-13. doi: 10.1016/s0014-5793(98)00111-2.
Polyomavirus large T-antigen binds to GRGGC sites in double-stranded viral DNA, regulating transcription and replication. Using surface plasmon resonance to record interactions of large T-antigen with different types of binding sites, we found that the configuration of recognition motifs influenced both the association and dissociation rates. Particularly, the complex formed at the origin of DNA replication was labile. A comparison of the interactions between large T-antigen and binding sites with one, two and four GRGGC motifs in tandem showed a strong preference for dimer binding, without detectable co-operativity between dimers. Sodium chloride stabilised the complexes, whereas the dissociation increased rapidly by increasing pH above 7.0.
多瘤病毒大T抗原与双链病毒DNA中的GRGGC位点结合，调节转录和复制。利用表面等离子体共振记录大T抗原与不同类型结合位点的相互作用，我们发现识别基序的构型影响结合和解离速率。特别是，在DNA复制起点形成的复合物不稳定。对大T抗原与串联有一个、两个和四个GRGGC基序的结合位点之间相互作用的比较表明，强烈倾向于二聚体结合，二聚体之间未检测到协同作用。氯化钠使复合物稳定，而当pH值高于7.0时，解离迅速增加。
