Fine-tuning of the PPR protein directs the RNA editing activity toward C-to-U or U-to-C conversion DOI Creative Commons
Mizuho Ichinose, Takamasa Teramoto,

Izumi Nakamura

et al.

Scientific Reports, Journal Year: 2025, Volume and Issue: 15(1)

Published: Feb. 21, 2025

A subfamily of pentatricopeptide repeat (PPR) proteins, known as PPR-DYW:PG, catalyzes the cytidine to uridine (C-to-U) RNA editing in plant organelles. related PPR subfamily, PPR-DYW:KP, (U-to-C) reaction, via a crosslinking mechanism involving lysine residue. We demonstrate that Lys88 DYW:KP domain is essential for U-to-C activity PPR-DYW:KP proteins. Substituting with other amino acids designer proteins switches protein C-to-U and prevents edited RNA. However, this mutation leads off-target downstream targeted site. Finally, modifications can modulate catalytic alter type reaction catalyzed by DYW domain. Altogether, our results suggest subtle influence position nucleotide reaction.

Language: Английский

Fine-tuning of the PPR protein directs the RNA editing activity toward C-to-U or U-to-C conversion DOI Creative Commons
Mizuho Ichinose, Takamasa Teramoto,

Izumi Nakamura

et al.

Scientific Reports, Journal Year: 2025, Volume and Issue: 15(1)

Published: Feb. 21, 2025

A subfamily of pentatricopeptide repeat (PPR) proteins, known as PPR-DYW:PG, catalyzes the cytidine to uridine (C-to-U) RNA editing in plant organelles. related PPR subfamily, PPR-DYW:KP, (U-to-C) reaction, via a crosslinking mechanism involving lysine residue. We demonstrate that Lys88 DYW:KP domain is essential for U-to-C activity PPR-DYW:KP proteins. Substituting with other amino acids designer proteins switches protein C-to-U and prevents edited RNA. However, this mutation leads off-target downstream targeted site. Finally, modifications can modulate catalytic alter type reaction catalyzed by DYW domain. Altogether, our results suggest subtle influence position nucleotide reaction.

Language: Английский

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