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A conserved DYW domain of the pentatricopeptide repeat protein possesses a novel endoribonuclease activity
Author(s) -
Nakamura Takahiro,
Sugita Mamoru
Publication year - 2008
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2008.11.017
Subject(s) - pentatricopeptide repeat , endoribonuclease , rna , recombinant dna , biochemistry , organelle , biology , cytidine , rna editing , microbiology and biotechnology , chemistry , enzyme , rnase p , gene
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.