![Functional analyses of nucleic acid-binding proteins](images/theme08.jpg)
Some DNAs and RNAs form non-canonical structures such as quadruplexes. Recently, it has been demonstrated that these non-canonical structures can be formed even in cells. Furthermore, proteins that recognize quadruplex structures have been discovered, and are considered to act as regulators for DNA replication and transcription. We are pursuing analyses of the interaction between quadruplexes and binding proteins from a physicochemical perspective. We also aim to alter the proteins and develop novel functional molecules that specifically target cellular quadruplexes.
Reference
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S. Nagatoishi and N. Sugimoto
Interaction of water with the G-quadruplex loop contributes to the binding energy of G-quadruplex to protein Mol. Biosyst., 8, 2766-2770 (2012) -
S. Nagatoishi, N. Isono, K. Tsumoto, and N. Sugimoto
Loop residues of thrombin-binding DNA aptamer impact G-quadruplex stability and thrombin binding.
Biochemie, 93, 1231-1238 (2011) -
S. Nagatoishi, N. Isono, K. Tsumoto, and N. Sugimoto
Hydration is required in DNA G-quadruplex-protein binding.
ChemBioChem, 12, 1822-1826 (2011)
Reviews and books
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S. Nakano, D. Miyoshi, and N. Sugimoto
Effects of molecular crowding on the structures, interactions, and functions of nucleic acids
Chem. Rev., 12, 114(5), 2733-2758 (2014) -
S. Nagatoishi, D. Miyoshi, and N. Sugimoto
Effects of protein binding on DNA G-quadruplex structures
International Review of Biophysical Chemistry, 2, 129-134 (2011)