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Ribosomal protein S19 is encoded by the mitochondrial genome in Petunia hybrida.

ABSTRACT: The rps19 ribosomal protein gene, which has not been previously reported in any mitochondrial genome, was identified by sequence analysis in the mitochondrial DNA of the higher plant Petunia hybrida. According to the sequence of eight rps19 cDNAs, seven C to U conversions with respect to the genomic sequence are present in rps19 transcripts. Not all transcripts are fully edited at these seven sites. Six of the seven C to U conversions change the encoded amino acid sequence by altering four codons. The rps19 gene is located entirely within a repeat sequence which is present in three copies on the 443 kb genome. Due to intragenomic recombination across these repeats, Petunia rps19 is present in nine different genomic environments.

SUBMITTER: Conklin PL

PROVIDER: S-EPMC328189 | biostudies-other | 1991 May

REPOSITORIES: biostudies-other

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Ribosomal protein S19 is encoded by the mitochondrial genome in Petunia hybrida.

Conklin P L PL Hanson M R MR

Nucleic acids research 19910501 10

The rps19 ribosomal protein gene, which has not been previously reported in any mitochondrial genome, was identified by sequence analysis in the mitochondrial DNA of the higher plant Petunia hybrida. According to the sequence of eight rps19 cDNAs, seven C to U conversions with respect to the genomic sequence are present in rps19 transcripts. Not all transcripts are fully edited at these seven sites. Six of the seven C to U conversions change the encoded amino acid sequence by altering four codon ...[more]

PMID: 2041746

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Project description:BackgroundEukaryotic organisms contain mitochondria, organelles capable of producing large amounts of ATP by oxidative phosphorylation. Each cell contains many mitochondria with many copies of mitochondrial DNA in each organelle. The mitochondrial DNA encodes a small but functionally critical portion of the oxidative phosphorylation machinery, a few other species-specific proteins, and the rRNA and tRNA used for the translation of these transcripts. Because the microenvironment of the mitochondrion is unique, mitochondrial genes may be subject to different selectional pressures than those affecting nuclear genes.ResultsFrom an analysis of the mitochondrial genomes of a wide range of eukaryotic species we show that there are three simple rules for the pyrimidine and purine abundances in mitochondrial DNA transcripts. Mitochondrial membrane protein transcripts are pyrimidine rich, rRNA transcripts are purine-rich and the soluble protein transcripts are purine-rich. The transitions between pyrimidine and purine-rich regions of the genomes are rapid and are easily visible on a pyrimidine-purine walk graph. These rules are followed, with few exceptions, independent of which strand encodes the gene. Despite the robustness of these rules across a diverse set of species, the magnitude of the differences between the pyrimidine and purine content is fairly small. Typically, the mitochondrial membrane protein transcripts have a pyrimidine richness of 56%, the rRNA transcripts are 55% purine, and the soluble protein transcripts are only 53% purine.ConclusionThe pyrimidine richness of mitochondrial-encoded membrane protein transcripts is partly driven by U nucleotides in the second codon position in all species, which yields hydrophobic amino acids. The purine-richness of soluble protein transcripts is mainly driven by A nucleotides in the first codon position. The purine-richness of rRNA is also due to an abundance of A nucleotides. Possible mechanisms as to how these trends are maintained in mtDNA genomes of such diverse ancestry, size and variability of A-T richness are discussed.

Project description:The interplay between ribosomal protein composition and mitochondrial function is essential for sustaining energy homeostasis. Precise stoichiometric production of ribosomal proteins is crucial to maximize protein synthesis efficiency while reducing the energy costs to the cell. However, the impact of this balance on mitochondrial ATP generation, morphology and function remains unclear. Particularly, the loss of a single copy ribosomal protein gene is observed in Mendelian disorders like Diamond Blackfan Anemia and is common in somatic tumors, yet the implications of this imbalance on mitochondrial function and energy dynamics are still unclear. In this study, we investigated the impact of haploinsufficiency for four ribosomal protein genes implicated in ribosomopathy disorders (rps-10, rpl-5, rpl-33, rps-23) in Caenorhabditis elegans and corresponding reductions in human lymphoblast cells. Our findings uncover significant, albeit variably penetrant, mitochondrial morphological differences across these mutants, alongside an upregulation of glutathione transferases, and SKN-1 dependent increase in oxidative stress resistance, indicative of increased ROS production. Specifically, loss of a single copy of rps-10 in C. elegans led to decreased mitochondrial activity, characterized by lower energy levels and reduced oxygen consumption. A similar reduction in mitochondrial activity and energy levels was observed in human leukemia cells with a 50% reduction in RPS10 transcript levels. Importantly, we also observed alterations in the translation efficiency of nuclear and mitochondrial electron transport chain components in response to reductions in ribosomal protein genes’ expression in both C. elegans and human cells. This suggests a conserved mechanism whereby the synthesis of components vital for mitochondrial function are adjusted in the face of compromised ribosomal machinery. Finally, mitochondrial membrane and cytosolic ribosomal components exhibited significant covariation at the RNA and translation efficiency level in lymphoblastoid cells across a diverse group of individuals, emphasizing the interplay between the protein synthesis machinery and mitochondrial energy production. By uncovering the impact of ribosomal protein haploinsufficiency on the translation efficiency of electron transport chain components, mitochondrial physiology, and the adaptive stress responses, we provide evidence for an evolutionarily conserved strategy to safeguard cellular functionality under genetic stress.

Dataset Information

Ribosomal protein S19 is encoded by the mitochondrial genome in Petunia hybrida.

Publications

Ribosomal protein S19 is encoded by the mitochondrial genome in Petunia hybrida.

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