| Budget Amount *help |
¥4,810,000 (Direct Cost: ¥3,700,000、Indirect Cost: ¥1,110,000)
Fiscal Year 2019: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2018: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2017: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
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| Outline of Final Research Achievements |
G-quadruplex (G4) binding protein, TLS/FUS, led to trimethylation of histone H4 at lysine 20 at the heterochromatin of telomeres and downregulation of transcription of telomeric repeat-containing RNA. To investigate the effect of structure of the arginine－glycine－glycine repeat (RGG) domain in TLS/FUS for G4 binding, we analyzed the G4 binding activities of proteins purified in a buffer with high concentrations of urea and KCl to disrupt the β-spiral structure of RGG domain. It reveals that the G4-specific binding abilities of TLS/FUS require β-spiral structure formation of RGG domain. Furthermore, we investigated the effect of the RNA recognition motif (RRM) and RGG domain of nucleolin on G4 binding and formation. Our findings indicate that Phe in RGG domain is responsible for G4 binding and folding. Moreover, RRM potentially binds to a guanine-rich single strand and folds the G4 with a 5′-terminal and 3′-terminal single strand containing guanine.
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