Deficiency of mitoribosomal S10 protein affects translation and splicing in Arabidopsis mitochondria
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ABSTRACT:
PROVIDER: PRJNA548091 | ENA |
REPOSITORIES: ENA
Dataset's files
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| SRR9257373.fastq.gz | Fastqsanger.gz | |||
| SRR9257374.fastq.gz | Fastqsanger.gz | |||
| SRR9257375.fastq.gz | Fastqsanger.gz | |||
| SRR9257376.fastq.gz | Fastqsanger.gz | |||
| SRR9257377.fastq.gz | Fastqsanger.gz |
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Project description:The ribosome is not only a protein-making machine, but also a regulatory element in protein synthesis. This view is supported by our earlier data showing that Arabidopsis mitoribosomes altered due to the silencing of the nuclear RPS10 gene encoding mitochondrial ribosomal protein S10 differentially translate mitochondrial transcripts compared with the wild-type. Here, we used ribosome profiling to determine the contribution of transcriptional and translational control in the regulation of protein synthesis in rps10 mitochondria compared with the wild-type ones. Oxidative phosphorylation system proteins are preferentially synthesized in wild-type mitochondria but this feature is lost in the mutant. The rps10 mitoribosomes show slightly reduced translation efficiency of most respiration-related proteins and at the same time markedly more efficiently synthesize ribosomal proteins and MatR and TatC proteins. The mitoribosomes deficient in S10 protein protect shorter transcript fragments which exhibit a weaker 3-nucleotide periodicity compared with the wild-type. The decrease in the triplet periodicity is particularly drastic for genes containing introns. Notably, splicing is considerably less effective in the mutant, indicating an unexpected link between the deficiency of S10 and mitochondrial splicing. Thus, a shortage of the mitoribosomal S10 protein has wide-ranging consequences on mitochondrial gene expression.
2019-10-29 | GSE132441 | GEO
Project description:The ribosome is not only a protein-making machine, but also a regulatory element in protein synthesis. This view is supported by our earlier data showing that Arabidopsis mitoribosomes altered due to the silencing of the nuclear RPS10 gene encoding mitochondrial ribosomal protein S10 differentially translate mitochondrial transcripts compared with the wild-type. Here, we used ribosome profiling to determine the contribution of transcriptional and translational control in the regulation of protein synthesis in rps10 mitochondria compared with the wild-type ones. Oxidative phosphorylation system proteins are preferentially synthesized in wild-type mitochondria but this feature is lost in the mutant. The rps10 mitoribosomes show slightly reduced translation efficiency of most respiration-related proteins and at the same time markedly more efficiently synthesize ribosomal proteins and MatR and TatC proteins. The mitoribosomes deficient in S10 protein protect shorter transcript fragments which exhibit a weaker 3-nt periodicity compared with the wild-type. The decrease in the triplet periodicity is particularly drastic for genes containing introns. Notably, splicing is considerably less effective in the mutant, indicating an unexpected link between the deficiency of S10 and mitochondrial splicing. Thus, a shortage of the mitoribosomal S10 protein has wide-ranging consequences on mitochondrial gene expression.
| S-EPMC7145619 | biostudies-literature
Project description:Using mitoribosomal profiling to investigate human mitochondrial translation
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Project description:GTPBP8 is required for mitoribosomal biogenesis and mitochondrial translation
2021-02-15 | MSV000086865 | MassIVE
Project description:Mitochondrial mRNAs encode key subunits of the oxidative phosphorylation complexes that produce energy for the cell. In Saccharomyces cerevisiae, mitochondrial translation is under the control of translational activators, specific to each mRNA. In Schizosaccharomyces pombe, which more closely resembles the human system by its mitochondrial DNA structure and physiology, most translational activators appear to be either lacking, or recruited for post-translational functions. By combining bioinformatics, genetic and biochemical approaches we identified two interacting factors, Cbp7 and Cbp8, controlling Cytb production in S. pombe. We show that their absence affects cytb mRNA stability and decreases the accumulation of the Cytb protein. We further identified two classes of Cbp7/Cbp8 partners and showed that they modulated Cytb or Cox1 synthesis. First, two isoforms of bS1m small mitoribosomal subunits, that appear mutually exclusive and confer translational specificity. Second, a complex of four proteins dedicated to Cox1 synthesis, which includes an RNA helicase that interacts with the mitochondrial ribosome. Our results suggest that S. pombecontains, in addition to complexes of translational activators, a heterogeneous population of mitochondrial ribosomes that could specifically modulate translation depending on the mRNA translated, in order to optimally balance the production of different respiratory complex subunits.
2021-10-11 | PXD025400 | Pride
Project description:Human 143B.206 Rho+ cells (depleted mitochondrial DNA) and cytoplasts (derived from mitochondrial patient fibroblast containing C1624T mutation in mitochondrial tRNAVal ) were previously used to generated transmitochondrial cybrid lines. Hek293T cells,143B cells and cybrid cells were cultured in DMEM supplemented with 10% FCS in 5% CO2 at 37 °C. Cells were treated with Chloramphenicol (100 μg/ ml) for 15 min before harvest. Cells were then lysed and RNase I digested. Lysates were then loaded on a sucrose gradient (7%-47%). Fractions containing mito-monosomes were used to isolated RNA which were used to generate the library for deep sequencing. Mitoribosomal profiling were generated for both control (143B and Hek293T) and cybrid cells to reveal aspects of mitoribosome behaviour.
2017-12-01 | E-MTAB-6284 | biostudies-arrayexpress
Project description:The synthesis of mitochondrial OXPHOS complexes is central to cellular metabolism, yet many molecular details of mitochondrial translation remain elusive. It is commonly held view that translation initiation in human mitochondria proceeded in a manner similar to bacterial systems, with the mitoribosomal small subunit bound to the initiation factors, mtIF2 and mtIF3, along with initiator tRNA and an mRNA. However, unlike in bacteria, most human mitochondrial mRNAs lack 5′ leader sequences that can mediate small subunit binding, raising the question of how leaderless mRNAs are recognized by mitoribosomes. By using novel in vitro mitochondrial translation initiation assays, alongside biochemical and genetic characterization of cellular knockouts of mitochondrial translation factors, we describe unique features of translation initiation in human mitochondria. We show that in vitro, leaderless mRNA transcripts can be loaded directly onto assembled 55S mitoribosomes, but not onto the mitoribosomal small subunit (28S). In addition, we demonstrate that while mtIF2 is indispensable for mitochondrial translation, mtIF3 activity is not required for translation of leaderless mitochondrial transcripts but is essential for translation of ATP6 in the case of the bicistronic ATP8/ATP6 transcript. Our results confirm important evolutionary divergences of the mitochondrial translation system, and further our understanding of a process central to eukaryotic metabolism.
2022-12-01 | GSE156937 | GEO
Project description:Mitochondria has its own mRNA translation system, which is mediated by mitochondria-specific protein synthesis machinery – ‘mitoribosomes’. Dysregulation of mitochondrial translation disrupts the metabolic homeostasis and has been implicated in pathologies including metabolic syndromes, neurological disorders and cardiac diseases. Here, we identify that EOLA1 (Endothelium and lymphocyte associated ASCH domain 1) as a novel mitochondrial protein and exclusively localizes to mitochondria matrix. We further show that knockout of EOLA1 dramatically affects mitochondrial translation and subsequently the oxidative phosphorylation in mammalian cells. Mechanistically, EOLA1 interacts with mt-rRNA (mitochondrial ribosomal RNA) and EFTU, which maintains the translation elongation of mitochondrial mRNAs. Importantly, we generated a Eola1 knocked-out mice model and found that heart functions are obviously abnormal upon depletion of EOLA1 homolog in mouse, implying that EOLA1 are important for proper functions of heart via regulating mitochondrial translation. Taken together, our work demonstrates that EOLA1 is a novel regulator for mt-RNA and mitochondrial translation.
2026-02-20 | GSE300159 | GEO
Project description:LONP-1 deficiency causes dysregulated protein synthesis within mitochondria that is restored by mitoribosomal mutations
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Project description:MicroRNAs (miRNAs) are crucial post-transcriptional regulators that extensively affect protein synthesis. Emerging evidence suggests the presence of miRNAs in mitochondria and important regulatory roles of miRNAs in mitochondrial translation. To investigate whether miRNAs are involved in the CR-induced mitochondrial translational changes, we used small RNA sequencing to profile miRNA expression in whole liver tissue as well as in liver mitochondria. The sequencing results revealed that the number of miRNAs identified in mitochondria was comparable to that found in the whole tissue.
2017-09-06 | GSE103478 | GEO