Real-time Investigation of SV40 Large T-antigen Helicase Activity Using Surface Plasmon Resonance |
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| Authors: | Jason Plyler Karl Jasheway Bodin Tuesuwan Jessica Karr Jarryd S. Brennan Sean M. Kerwin Wendi M. David |
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| Affiliation: | (1) Department of Chemistry and Biochemistry, Texas State University-San Marcos, San Marcos, TX 78666, USA;(2) Division of Medicinal Chemistry, College of Pharmacy, Department of Chemistry and Biochemistry, The University of Texas at Austin, Austin, TX, 78712, USA;(3) Present address: Department of Pharmaceutical Chemistry, Faculty of Pharmaceutical Sciences, Chulalongkorn University, Bangkok, 10330, Thailand |
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| Abstract: | ![]()
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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| Keywords: | SV40 T-antigen Helicase G-quadruplex DNA SPR |
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