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DNA binding of polyomavirus large T-antigen: kinetics of interactions with different types of binding sites.
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Biochemistry and Microbiology.ORCID iD: 0000-0001-9684-7887
1998 (English)In: FEBS Letters, ISSN 0014-5793, E-ISSN 1873-3468, Vol. 423, no 3, 307-13 p.Article in journal (Refereed) Published
Abstract [en]

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.

Place, publisher, year, edition, pages
1998. Vol. 423, no 3, 307-13 p.
National Category
Microbiology in the medical area
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URN: urn:nbn:se:uu:diva-319219PubMedID: 9515729OAI: oai:DiVA.org:uu-319219DiVA: diva2:1086322
Available from: 2017-03-31 Created: 2017-03-31 Last updated: 2017-03-31

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