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Rice MPR25 encodes a pentatricopeptide repeat protein and is essential for RNA editing of nad5 transcripts in mitochondria
Author(s) -
Toda Takushi,
Fujii Sota,
Noguchi Ko,
Kazama Tomohiko,
Toriyama Kinya
Publication year - 2012
Publication title -
the plant journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.058
H-Index - 269
eISSN - 1365-313X
pISSN - 0960-7412
DOI - 10.1111/j.1365-313x.2012.05091.x
Subject(s) - pentatricopeptide repeat , nadh dehydrogenase , biology , mutant , rna editing , mitochondrion , chloroplast , alternative oxidase , gene , mitochondrial dna , respiratory chain , biochemistry , microbiology and biotechnology , genetics , rna
Summary Pentatricopeptide repeat (PPR) proteins are involved in the modification of organelle transcripts. In this study, we investigated the molecular function in rice of the mitochondrial PPR‐encoding gene MITOCHONDRIAL PPR25 ( MPR25 ), which belongs to the E subgroup of the PPR family. A Tos17 knockout mutant of MPR25 exhibited growth retardation and pale‐green leaves with reduced chlorophyll content during the early stages of plant development. The photosynthetic rate in the mpr25 mutant was significantly decreased, especially under strong light conditions, although the respiration rate did not differ from that of wild‐type plants. MPR25 was preferentially expressed in leaves. FLAG‐tagged MPR25 accumulated in mitochondria but not in chloroplasts. Direct sequencing revealed that the mpr25 mutant fails to edit a C–U RNA editing site at nucleotide 1580 of nad5 , which encodes a subunit of complex I (NADH dehydrogenase) of the respiratory chain in mitochondria. RNA editing of this site is responsible for a change in amino acid from serine to leucine. Recombinant MPR25 directly interacted with the proximal region of the editing site of nad5 transcripts. However, the NADH dehydrogenase activity of complex I was not affected in the mutant. By contrast, genes encoding alternative NADH dehydrogenases and alternative oxidase were up‐regulated. The mpr25 mutant may therefore provide new information on the coordinated interaction between mitochondria and chloroplasts.