TY - JOUR
T1 - Pentatricopeptide repeat proteins involved in plant organellar RNA editing
AU - Yagi, Yusuke
AU - Tachikawa, Makoto
AU - Noguchi, Hisayo
AU - Satoh, Soichirou
AU - Obokata, Junichi
AU - Nakamura, Takahiro
N1 - Funding Information:
This work was supported by Grants-in- Aid 22681028 and 22380008 (TN) and 22370002, 23125512 and 23117006 (JO) from the Ministry of Education, Culture, Sports, Science and Technology; and the Adaptable and Seamless Technology Transfer Program through Target-driven R&D, JST (TN).
PY - 2013/9
Y1 - 2013/9
N2 - C-to-U RNA editing has been widely observed in organellar RNAs in terrestrial plants. Recent research has revealed the significance of a large, plant-specific family of pentatricopeptide repeat (PPR) proteins for RNA editing and other RNA processing events in plant mitochondria and chloroplasts. PPR protein is a sequence-specific RNA-binding protein that identifies specific C residues for editing. Discovery of the RNA recognition code for PPR motifs, including verification and prediction of the individual RNA editing site and its corresponding PPR protein, expanded our understanding of the molecular function of PPR proteins in plant organellar RNA editing. Using this knowledge and the co-expression database, we have identified two new PPR proteins that mediate chloroplast RNA editing. Further, computational target assignment using the PPR RNA recognition codes suggests a distinct, unknown mode-of-action, by which PPR proteins serve a function beyond site recognition in RNA editing.
AB - C-to-U RNA editing has been widely observed in organellar RNAs in terrestrial plants. Recent research has revealed the significance of a large, plant-specific family of pentatricopeptide repeat (PPR) proteins for RNA editing and other RNA processing events in plant mitochondria and chloroplasts. PPR protein is a sequence-specific RNA-binding protein that identifies specific C residues for editing. Discovery of the RNA recognition code for PPR motifs, including verification and prediction of the individual RNA editing site and its corresponding PPR protein, expanded our understanding of the molecular function of PPR proteins in plant organellar RNA editing. Using this knowledge and the co-expression database, we have identified two new PPR proteins that mediate chloroplast RNA editing. Further, computational target assignment using the PPR RNA recognition codes suggests a distinct, unknown mode-of-action, by which PPR proteins serve a function beyond site recognition in RNA editing.
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U2 - 10.4161/rna.24908
DO - 10.4161/rna.24908
M3 - Review article
C2 - 23669716
AN - SCOPUS:84929517201
SN - 1547-6286
VL - 10
SP - 1419
EP - 1425
JO - RNA biology
JF - RNA biology
IS - 9
ER -