oenothera fruticosa/oxidase

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5 matokeo

Cytochrome oxidase subunit II mRNAs in Oenothera mitochondria are edited at 24 sites.

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Ingia / Ingia

Analysis of cDNA clones covering the entire coding region of cytochrome oxidase subunit II in Oenothera mitochondria reveals 24 potential editing sites: 23 C to U transitions and one U to C conversion. One editing event is observed outside the open reading frame in the 3' non-coding region. Thirteen

The cytochrome oxidase subunit I and subunit III genes in Oenothera mitochondria are transcribed from identical promoter sequences.

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Ingia / Ingia

Two loci encoding subunit III of the cytochrome oxidase (COX) in Oenothera mitochondria have been identified from a cDNA library of mitochondrial transcripts. A 657-bp sequence block upstream from the open reading frame is also present in the two copies of the COX subunit I gene and is presumably

Cytochrome oxidase subunit II gene in mitochondria of Oenothera has no intron.

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Ingia / Ingia

The cytochrome oxidase subunit II gene has been localized in the mitochondrial genome of Oenothera berteriana and the nucleotide sequence has been determined. The coding sequence contains 777 bp and, unlike the corresponding gene in Zea mays, is not interrupted by an intron. No TGA codon is found

Distribution of RNA editing sites in Oenothera mitochondrial mRNAs and rRNAs.

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Ingia / Ingia

To investigate whether RNA editing in plant mitochondria modifies structural RNAs as well as protein-coding RNAs we compared the genomic-encoded information with the respective transcripts of several genes in Oenothera. The genes analysed are the 5S, 18S and 26 S rRNAs, the alpha-subunit of ATPase

The gene for ribosomal protein S10 is present in mitochondria of pea and potato but absent from those of Arabidopsis and Oenothera.

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Ingia / Ingia

A novel group II intron has been identified in the pea (Pisum sativum) mitochondrial genome. The gene harbouring this intron is identified as rps10 (encoding protein S10 of the small ribosomal subunit) by similarity to its known homologues in bacteria and in the mitochondrion of the liverwort

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