K. Bondeson et al., DNA-BINDING OF POLYOMAVIRUS LARGE T-ANTIGEN - KINETICS OF INTERACTIONS WITH DIFFERENT TYPES OF BINDING-SITES, FEBS letters, 423(3), 1998, pp. 307-313
Polyomavirus large T-antigen binds to GRGGC sites in double-stranded v
iral DNA, regulating transcription and replication, Using surface plas
mon resonance to record interactions of large T-antigen with different
types of binding sites, we found that the configuration of recognitio
n motifs influenced both the association and dissociation rates, Parti
cularly, the complex formed at the origin of DNA replication was labil
e, A comparison of the interactions between targe T-antigen and bindin
g sites with one, two and four GRGGC motifs in tandem showed a strong
preference for dimer binding, without detectable co-operativity betwee
n dimers, Sodium chloride stabilised the complexes, whereas the dissoc
iation increased rapidly by increasing pH above 7.0. (C) 1998 Federati
on of European Biochemical Societies.