A conserved DYW domain of the pentatricopeptide repeat protein possesses a novel endoribonuclease activity.
Many plant pentatricopeptide repeat (PPR) proteins are known to contain a highly conserved C-terminal DYW domain whose function is unknown. Recently, the DYW domain has been proposed to play a role in RNA editing in plant organelles. To address this possibility, we prepared recombinant DYW proteins and tested their cytidine deaminase activity. However, we could not detect any activity in the assays we used. Instead, we found that the recombinant DYW domains possessed endoribonuclease activity and cleaved before adenosine residues in the RNA molecule. Some DYW-containing PPR proteins may catalyze site-specific cleavage of target RNA species.
Nakamura
Takahiro
T
Center for Gene Research, Nagoya University, Chikusa, Aichi, Nagoya 464-8602, Japan.
Sugita
Mamoru
M
D000595:Amino Acid Sequence; D029681:Arabidopsis Proteins / Q000737:chemistry* / Q000235:genetics; D017124:Conserved Sequence; D003564:Cytidine Deaminase / Q000737:chemistry* / Q000235:genetics; D004722:Endoribonucleases / Q000737:chemistry* / Q000235:genetics; D049452:Green Fluorescent Proteins / Q000235:genetics; D008969:Molecular Sequence Data; D017434:Protein Structure, Tertiary; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000235:genetics; D020449:Repetitive Sequences, Amino Acid
D029681:Arabidopsis Proteins; D011993:Recombinant Fusion Proteins; C538752:pentatricopeptide repeat protein, Arabidopsis; D049452:Green Fluorescent Proteins; D004722:Endoribonucleases; D003564:Cytidine Deaminase