Journal
CELL BIOCHEMISTRY AND BIOPHYSICS
Volume 53, Issue 1, Pages 43-52Publisher
HUMANA PRESS INC
DOI: 10.1007/s12013-008-9038-z
Keywords
SV40 T-antigen; Helicase; G-quadruplex DNA; SPR
Funding
- Welch Foundation [AI 0045, F1298]
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The simian virus 40 (SV40) genome is a model system frequently employed for investigating eukaryotic replication. Large T-antigen (T-ag) is a viral protein responsible for unwinding the SV40 genome and recruiting necessary host factors prior to replication. In addition to duplex unwinding T-ag possesses G-quadruplex DNA helicase activity, the physiological consequence of which is unclear. However, formation of G-quadruplex DNA structures may be involved in genome maintenance and function, and helicase activity to resolve these structures may be necessary for efficient replication. We report the first real-time investigation of SV40 T-ag helicase activity using surface plasmon resonance (SPR). In the presence of ATP, T-ag was observed to bind to immobilized single-stranded DNA, forked duplex DNA, and the human telomeric foldover quadruplex DNA sequence. Inhibition of T-ag duplex helicase activity was observable in real-time and the intramolecular quadruplex was unwound.
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