TY - JOUR
T1 - A conserved DYW domain of the pentatricopeptide repeat protein possesses a novel endoribonuclease activity
AU - Nakamura, Takahiro
AU - Sugita, Mamoru
N1 - Funding Information:
We thank Dr. Yasuo Niwa for providing us plasmid CaMV35S-sGFP(S65T)-nos3′ and the construct for mitochondrial γATPase-GFP fusion protein. We thank the Arabidopsis Biological Resource Center for providing seed stocks in this study. MS was supported by a Grant-in-Aid for Scientific Research (C) from the Japan Society for the Promotion of Science (JSPS) KAKENHI (19570157) and TN by the JSPS Research Fellowship for Young Scientists (16-5643) and by Precursory Research for Embryonic Science and Technology program grant from the Japan Science and Technology Agency (PRESTO).
PY - 2008/12/24
Y1 - 2008/12/24
N2 - 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.
AB - 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.
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U2 - 10.1016/j.febslet.2008.11.017
DO - 10.1016/j.febslet.2008.11.017
M3 - Article
C2 - 19041647
AN - SCOPUS:57149118430
VL - 582
SP - 4163
EP - 4168
JO - FEBS Letters
JF - FEBS Letters
SN - 0014-5793
IS - 30
ER -