Skip to main content
Advertisement

Main menu

  • Home
  • Articles
    • Newest Articles
    • Current Issue
    • Methods & Resources
    • Archive
    • Subjects
  • Collections
  • Submit
    • Submit a Manuscript
    • Author Guidelines
    • License, Copyright, Fee
    • FAQ
    • Why Submit
  • About
    • About Us
    • Editors & Staff
    • Board Members
    • Licensing and Reuse
    • Reviewer Guidelines
    • Privacy Policy
    • Advertise
    • Contact Us
    • LSA LLC
  • Alerts
  • Other Publications
    • EMBO Press
    • The EMBO Journal
    • EMBO reports
    • EMBO Molecular Medicine
    • Molecular Systems Biology
    • Rockefeller University Press
    • Journal of Cell Biology
    • Journal of Experimental Medicine
    • Journal of General Physiology
    • Cold Spring Harbor Laboratory Press
    • Genes & Development
    • Genome Research

User menu

  • My alerts

Search

  • Advanced search
Life Science Alliance
  • Other Publications
    • EMBO Press
    • The EMBO Journal
    • EMBO reports
    • EMBO Molecular Medicine
    • Molecular Systems Biology
    • Rockefeller University Press
    • Journal of Cell Biology
    • Journal of Experimental Medicine
    • Journal of General Physiology
    • Cold Spring Harbor Laboratory Press
    • Genes & Development
    • Genome Research
  • My alerts
Life Science Alliance

Advanced Search

  • Home
  • Articles
    • Newest Articles
    • Current Issue
    • Methods & Resources
    • Archive
    • Subjects
  • Collections
  • Submit
    • Submit a Manuscript
    • Author Guidelines
    • License, Copyright, Fee
    • FAQ
    • Why Submit
  • About
    • About Us
    • Editors & Staff
    • Board Members
    • Licensing and Reuse
    • Reviewer Guidelines
    • Privacy Policy
    • Advertise
    • Contact Us
    • LSA LLC
  • Alerts
  • Follow lsa Template on Twitter
Research Article
Transparent Process
Open Access

Mitochondrial ubiquinone–mediated longevity is marked by reduced cytoplasmic mRNA translation

Marte Molenaars, Georges E Janssens, Toon Santermans, Marco Lezzerini, Rob Jelier, Alyson W MacInnes  Correspondence email, View ORCID ProfileRiekelt H Houtkooper  Correspondence email
Marte Molenaars
1Laboratory Genetic Metabolic Diseases, Amsterdam University Medical Centers, University of Amsterdam, Amsterdam Gastroenterology and Metabolism, Amsterdam, The Netherlands
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
Georges E Janssens
1Laboratory Genetic Metabolic Diseases, Amsterdam University Medical Centers, University of Amsterdam, Amsterdam Gastroenterology and Metabolism, Amsterdam, The Netherlands
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
Toon Santermans
2Centre of Microbial and Plant Genetics University of Leuven, Leuven, Belgium
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
Marco Lezzerini
1Laboratory Genetic Metabolic Diseases, Amsterdam University Medical Centers, University of Amsterdam, Amsterdam Gastroenterology and Metabolism, Amsterdam, The Netherlands
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
Rob Jelier
2Centre of Microbial and Plant Genetics University of Leuven, Leuven, Belgium
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
Alyson W MacInnes
1Laboratory Genetic Metabolic Diseases, Amsterdam University Medical Centers, University of Amsterdam, Amsterdam Gastroenterology and Metabolism, Amsterdam, The Netherlands
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
  • For correspondence: a.w.macinnes@amc.nl
Riekelt H Houtkooper
1Laboratory Genetic Metabolic Diseases, Amsterdam University Medical Centers, University of Amsterdam, Amsterdam Gastroenterology and Metabolism, Amsterdam, The Netherlands
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
  • ORCID record for Riekelt H Houtkooper
  • For correspondence: r.h.houtkooper@amc.nl
Published 31 August 2018. DOI: 10.26508/lsa.201800082
  • Article
  • Figures & Data
  • Info
  • Metrics
  • Reviewer Comments
  • PDF
Loading

Article Figures & Data

Figures

  • Tables
  • Figure 1.
    • Download figure
    • Open in new tab
    • Download powerpoint
    Figure 1. RNA-seq of the clk-1(qm30) (± nuclear or WT clk-1) mutants.

    (A) Graphical illustration of clk-1(qm30), clk-1(qm30)+nuc, and clk-1(qm30)+WT lines used for RNA-seq. mRNA was isolated from three biological replicates of each mutant, harvested at the L4 stage. (B) PCA of RNA libraries showing clear distinction between clk-1(qm30), clk-1(qm30)+nuc, and clk-1(qm30)+WT (N = 3 biological replicates for each strain). (C) Correlation matrix of RNA-seq samples shows the expected clustering of the biological triplicates of each strain. (D) Top 50 down-regulated GO terms (left graph) and up-regulated GO terms (right graph) in clk-1(qm30) versus clk-1(qm30)+WT (left column) and clk-1(qm30)+nuc versus clk-1(qm30)+WT (right column). Proportions of GO terms associated with translation and mRNA processing are depicted in yellow, development and reproduction in red, metabolism in green, and ion transport in blue.

  • Figure 2.
    • Download figure
    • Open in new tab
    • Download powerpoint
    Figure 2. Differentially expressed genes in clk-1(qm30)+nuc compared with clk-1(qm30).

    (A) Fold changes of differentially expressed genes in clk-1(qm30) versus clk-1(qm30)+WT plotted against fold changes of clk-1(qm30)+nuc versus clk-1(qm30)+WT shows a minor role for nuclear clk-1 in transcriptional changes. Colors of the individual data points correspond to the colors of the groups of genes in the Venn diagram in (B). (B) Venn diagram shows that most genes are similarly up-regulated (3720) and down-regulated (4397) in the clk-1(qm30)+nuc and clk-1(qm30) worms when comparing with clk-1+WT. There were 292 genes exclusively up-regulated in clk-1(qm30)+nuc (blue) and 704 genes exclusively in clk-1(qm30) (green) compared with clk-1+WT. Furthermore, 175 genes were down-regulated exclusively in clk-1(qm30)+nuc (red) and 805 genes down-regulated exclusively in clk-1(qm30) (orange) compared with clk-1+WT. Differential expressions in (A) and (B) are with a threshold-adjusted P value < 0.01. (C) Significant Cluster GO Enrichments (threshold Enrichment Score > 3) associated with the 704 genes specifically up-regulated (green) and 805 down-regulated (orange) in clk-1(qm30) strain. There were no significant Cluster GO Enrichments for genes exclusively up or down-regulated in clk-1(qm30)+nuc.

  • Figure 3.
    • Download figure
    • Open in new tab
    • Download powerpoint
    Figure 3. Repressed polysome profiles in the clk-1(qm30) (±nuc) mutants.

    (A) Representative traces of polysome profiles of clk-1(qm30) strains harvested at the L4 stage, when lysate is normalized to total protein levels of 500 μg. The monosomal peak and polysomal peaks (P1–P6) are indicated. (B) Quantification of polysome peak sizes (AUC). The fold change is represented compared with P1 of the clk-1(qm30)+WT. All peaks of clk-1(qm30)+WT are significantly different from both clk-1(qm30)+nuc and clk-1(qm30). No peaks were significantly different between clk-1(qm30) and clk-1(qm30)+nuc. Error bars represent mean ± SD. Significance was tested with t test and P-values were adjusted to correct for multiple testing using the Holm–Sidak method, with α = 0.05.

  • Figure S1.
    • Download figure
    • Open in new tab
    • Download powerpoint
    Figure S1. qPCR analysis of encoding initiation factors and RPs.

    Relative expression levels determined by qRT–PCR (WT versus clk-1(qm30)) normalized by expression of pmp-3 as reference gene. Significance was tested with t test and P-values were adjusted to correct for multiple testing using the Holm–Sidak method, with α = 0.05.

  • Figure 4.
    • Download figure
    • Open in new tab
    • Download powerpoint
    Figure 4. Analysis of total and polysomal RNA clk-1(qm30) and clk-1(qm30)+WT.

    (A) Schematic representation of polysomal fraction (blue) used for RNA isolation and total RNA (green) from C. elegans mutants clk-1(qm30) and clk-1(qm30)+WT that were used for RNAseq. (B) Fold changes of differentially expressed genes in the total RNA of clk-1(qm30) versus clk-1(qm30)+WT plotted against fold changes in polysomal RNA of clk-1(qm30) versus clk-1(qm30)+WT. Colors of the individual data points correspond to the colors of the groups of genes in the Venn diagram in (C). (C) Venn diagram showing 1657 genes were similarly up-regulated and 2574 genes down-regulated in both the polysomal as the total RNA in the clk-1(qm30) strain compared with clk-1(qm30)+WT. A total of 434 genes were exclusively up-regulated in the polysomal RNA (blue), whereas 2767 genes were exclusively up-regulated in the total RNA (green). Furthermore, 477 genes were exclusively down-regulated in the polysomal RNA (red) and 2628 genes were exclusively down-regulated in the total RNA. Differential expressions (B, C) are with a threshold-adjusted P value < 0.01. (D) Significant Cluster GO Enrichments (threshold Enrichment Score > 3) associated with the genes specifically up and down-regulated in groups of genes in (C) (colors of the bars correspond again to the color of the groups in (C)). (E) Fib-1 is reduced in both the total and polysomal RNA of clk-1(qm30) compared with clk-1(qm30)+WT. (F, G) FIB-1 levels are reduced in clk-1(qm30) worms compared with N2 worms. Error bars represent mean ± SD, significance was tested with t test, ***P < 0.0005.

  • Figure S2.
    • Download figure
    • Open in new tab
    • Download powerpoint
    Figure S2. Global analysis of polysomal and total RNA-seq.

    (A) Correlation matrix of RNA-seq samples shows the expected clustering of total and polysomal RNA of the biological triplicates of each strain. (B) PCA of RNA libraries showing clear distinction between polysomal and total RNA of each of the strains (N = 3 biological replicates for each strain).

  • Figure 5.
    • Download figure
    • Open in new tab
    • Download powerpoint
    Figure 5. Translation efficiency (TE) of transcripts in clk-1(qm30) worms.

    (A) Volcano plot of log2 fold change of TE (total RNA:polysomal RNA) of transcripts clk-1(qm30):clk-1(qm30)+WT. The blue data points represent transcripts with high TE in clk-1(qm30) worms being shifted from the total RNA to the highly translated polysomal RNA. The red data points represent transcripts that have low TE in clk-1(qm30) being shifted from polysomal RNA to the total RNA. Differentially translationally regulated genes in red and blue with threshold-adjusted P value < 0.01. (B) Significant Cluster GO Enrichments (threshold Enrichment Score > 3) associated with significantly different TEs (colors of the bars correspond again to the data points in (A)). (C) TE of individual transcripts involved in TOR pathway in clk-1(qm30)+WT (left bar) clk-1(qm30) (middle bar) and their ratio (right bar). Colors of the ratio bars correspond again to the data points in (A). Clk-1(qm30) worms slow reduced TE of let-363, daf-15, clk-2, and R10H10.7 and an increased TE for lgg-1. (D) Schematic overview of transcripts involved in TOR pathway that have altered TE in clk-1(qm30) versus clk-1(qm30)+WT represented in (C) and their involvement in longevity.

  • Figure 6.
    • Download figure
    • Open in new tab
    • Download powerpoint
    Figure 6. RNAi of taf-4 partially restores repressed peaks in clk-1(qm30) mutants.

    (A) Representative traces of polysome profiles of clk-1(qm30) worms fed HT115 bacteria transformed with the empty vector (EV) or expressing taf-4 RNAi when harvested at the L4 stage, when lysate is normalized to total protein levels of 500 μg. The monosomal peak and polysomal peaks (P1–P5) are indicated. (B) Representative traces of polysome profiles of clk-1(qm30)+WT worms fed HT115 bacteria transformed with the EV or expressing taf-4 RNAi, when lysate is normalized to total protein levels of 500 μg. The monosomal peak and polysomal peaks are indicated. (C) Quantification of polysome peak sizes (AUC). The fold change is represented compared with P1 of the clk-1(qm30)+WT fed with HT115 bacteria. Polysomal peaks P1 and P2 were significantly different between clk-1(qm30)+WT fed with HT115 and taf-4 RNAi bacteria. No peaks were significantly different between clk-1(qm30)+WT fed with HT115 and taf-4 RNAi bacteria. Error bars represent mean ± SD. Significance was tested with t test and P-values were adjusted to correct for multiple testing using the Holm–Sidak method, with α = 0.05. (D) Relative expression levels determined by qRT–PCR in clk-1(qm30)(+WT) fed with either the EV or taf-4 RNAi bacteria. Expression levels were normalized using the geometrical mean of reference genes Y45F10D.4, tba-1, and csq-1. Significance was tested using one-way ANOVA with Sidak's multiple comparisons test. Error bars represent mean ± SEM. **P < 0.01, significance indicated only between clk-1(qm30) EV and clk-1(qm30) taf-4 RNAi.

Tables

  • Figures
    • View popup
    Table 1.

    Identified polysomal transcripts involved in OXPHOS that, compared with clk-1(qm30)+WT, are enriched in clk-1(qm30).

    AccessionGene nameDescriptionlog2 fold change polysomal RNA
    Complex I
     C16A3.5C16A3.5Orthologue B9 subunit of the mitochondrial complex I0.42
     C18E9.4C18E9.4Orthologue B12 subunit of the mitochondrial complex I0.61
     C25H3.9C25H3.9Orthologue B5 subunit of the mitochondrial complex I0.40
     C33A12.1C33A12.1Orthologue A5/B13 subunit of the mitochondrial complex I0.43
     C34B2.8C34B2.8Orthologue A13 subunit of the mitochondrial complex I0.48
     F37C12.3F37C12.3Orthologue AB1 subunit of the mitochondrial complex I0.53
     F42G8.10F42G8.10Orthologue B11 subunit of the mitochondrial complex I0.38
     F44G4.2F44G4.2Orthologue B2 subunit of the mitochondrial complex I0.54
     F53F4.10F53F4.10Orthologue NADH-UQ oxidoreductase flavoprotein 20.45
     ZK973.10lpd-5NADH-UQ oxidoreductase fe-s protein 40.37
     W10D5.2nduf-7NADH-UQ oxidoreductase fe-s protein 70.47
     C09H10.3nuo-1NADH UQ oxidoreductase 10.35
     T10E9.7nuo-2NADH UQ oxidoreductase 20.47
     W01A8.4nuo-6NADH UQ oxidoreductase 60.47
     T20H4.5T20H4.5Orthologue NADH-UQ oxidoreductase Fe-S protein 80.39
     Y53G8AL.2Y53G8AL.2Orthologue A9 subunit of the mitochondrial complex I0.48
    Complex II
     F42A8.2sdhb-1Succinate dehydrogenase complex subunit B0.37
     F33A8.5sdhd-1Succinate dehydrogenase complex subunit D0.74
    Complex III
     C54G4.8cyc-1Cytochrome C reductase0.35
     F42G8.12isp-1Rieske iron sulphur protein subunit of the mitochondrial complex III0.27
     R07E4.3R07E4.3Orthologue subunit VII ubiquinol–cytochrome c reductase complex III0.54
     T02H6.11T02H6.11Ubiquinol–cytochrome c reductase binding protein0.40
     T27E9.2T27E9.2Ubiquinol–cytochrome c reductase hinge protein0.54
     F57B10.14ucr-11Ubiquinol–cytochrome c oxidoreductase complex0.75
    Complex IV
     F26E4.9cco-1Cytochrome C oxidase0.46
     Y37D8A.14cco-2Cytochrome C oxidase0.46
     F26E4.6F26E4.6Orthologue cytochrome c oxidase subunit 7C0.55
     F29C4.2F29C4.2Orthologue cytochrome c oxidase subunit 6C0.66
     F54D8.2tag-174Orthologue cytochrome c oxidase subunit 6A20.45
     Y71H2AM.5Y71H2AM.5Orthologue cytochrome c oxidase subunit 6B10.48
    Complex V
     C53B7.4asg-2ATP synthase G homolog0.79
     C06H2.1atp-5ATP synthase subunit0.45
     F32D1.2hpo-18Orthologue of ATP synthase, H+ transporting, mitochondrial F1 complex, ε subunit0.56
     R04F11.2R04F11.2Orthologue of ATP synthase, H+ transporting, mitochondrial Fo complex, ε subunit0.51
     R53.4R53.4Mitochondrial ATP synthase subunit f homolog0.34
     R10E11.8vha-1Vacuolar H ATPase 10.50
     R10E11.2vha-2Vacuolar H ATPase 20.63
     Y38F2AL.4vha-3 Vacuolar H ATPase 30.58
     T01H3.1vha-4Vacuolar H ATPase 40.61
     VW02B12L.1vha-6Vacuolar H ATPase 60.59
     C17H12.14vha-8Vacuolar H ATPase 80.66
     ZK970.4vha-9Vacuolar H ATPase 90.43
     F46F11.5vha-10Vacuolar H ATPase 100.64
     Y38F2AL.3vha-11Vacuolar H ATPase 110.58
     F20B6.2vha-12Vacuolar H ATPase 120.34
     Y49A3A.2vha-13Vacuolar H ATPase 130.35
     F55H2.2vha-14Vacuolar H ATPase 140.49
     T14F9.1vha-15Vacuolar H ATPase 150.51
     C30F8.2vha-16Vacuolar H ATPase 160.55
     Y69A2AR.18Y69A2AR.18Orthologue of ATP synthase, H+ transporting, mitochondrial F1 complex, γ subunit0.25
    • View popup
    Table 2.

    Identified polysomal transcripts involved in mRNA translation that, compared with clk-1(qm30)+WT, are reduced in clk-1(qm30).

    AccessionGene nameDescriptionlog2 fold change
    Translation
     ZC434.5ears-1Glutamyl(E) amino-acyl tRNA synthetase−0.51
     F31E3.5eef-1A.1Eukaryotic translation elongation factor 1-α−0.67
     F25H5.4eef-2Eukaryotic translation elongation factor 2−0.53
     C27D11.1egl-45Eukaryotic translation initiation factor 3 subunit A−0.50
     F11A3.2eif-2BdeltaEukaryotic translation initiation factor 2B subunit Δ−0.79
     Y54E2A.11eif-3.BEukaryotic translation initiation factor 3 subunit B−0.38
     T23D8.4eif-3.CEukaryotic translation initiation factor 3 subunit C−0.43
     R11A8.6iars-1Isoleucyl(I) amino-acyl tRNA synthetase−0.26
     M110.4ifg-1Initiation factor 4G (eIF4G) family−0.43
     K10C3.5K10C3.5Orthologue of Ria1p−0.92
     R74.1lars-1Leucyl(L) amino-acyl tRNA synthetase−0.36
     C47E12.1sars-1Seryl(S) amino-acyl tRNA synthetase−0.43
     F28H1.3aars-2Alanyl(A) amino-acyl tRNA synthetase−0.46
     K08F11.3cif-1COP9/signalosome and eIF3 complex shared subunit−0.37
     Y41E3.10eef-1B.2Eukaryotic translation elongation factor−0.31
     Y37E3.10eif-2AEukaryotic initiation factor−1.06
     R08D7.3eif-3.DEukaryotic initiation factor−1.61
     Y40B1B.5eif-3.JEukaryotic initiation factor−1.24
     C17G10.9eif-3.LEukaryotic initiation factor−0.61
     C47B2.5eif-6Eukaryotic initiation factor−0.53
     T05H4.6erfa-1Eukaryotic release factor homolog−0.30
     F22B5.9fars-3Phenylalanyl(F) amino-acyl tRNA synthetase−1.65
     T10F2.1gars-1Glycyl(G) amino-acyl tRNA synthetase−0.41
     F53A2.6ife-1Initiation factor 4E (eIF4E) family−0.72
     B0348.6ife-3Initiation factor 4E (eIF4E) family−0.55
     T05G5.10iff-1Initiation factor five (eIF-5A) homolog−0.31
     Y54F10BM.2iffb-1Initiation factor five B (eIF5B)−0.75
     F57B9.6inf-1Initiation factor−0.31
     T02G5.9kars-1Lysyl(K) amino-acyl tRNA synthetase−0.30
     F58B3.5mars-1Methionyl(M) amino-acyl tRNA synthetase−0.62
     F22D6.3nars-1Asparaginyl(N) amino-acyl tRNA synthetase−0.64
     Y41E3.4qars-1Glutaminyl(Q) amino-acyl tRNA synthetase−0.43
     F26F4.10rars-1Arginyl(R) amino-acyl tRNA synthetase−0.55
     C47D12.6tars-1Threonyl(T) amino-acyl tRNA synthetase−0.44
     Y87G2A.5vrs-2Valyl(V) amino-acyl tRNA synthetase−0.41
     Y80D3A.1wars-1Tryptophanyl(W) amino-acyl tRNA synthetase−0.67
     Y105E8A.19yars-1Tyrosinyl(Y) amino-acyl tRNA synthetase−0.90
    Ribosome
     Y71F9AL.13rpl-1Large ribosomal subunit L1 protein−0.53
     B0250.1rpl-2Large ribosomal subunit L2 protein−0.82
     F13B10.2rpl-3Large ribosomal subunit L3 protein−0.75
     B0041.4rpl-4Large ribosomal subunit L4 protein−0.95
     54C9.5rpl-5Large ribosomal subunit L5 protein−0.58
     R151.3rpl-6Large ribosomal subunit L6 protein−0.37
     Y24D9A.4rpl-7ALarge ribosomal subunit L7A protein−0.44
     R13A5.8rpl-9Large ribosomal subunit L9 protein−0.67
     JC8.3rpl-12Large ribosomal subunit L12 protein−0.48
     C32E8.2rpl-13Large ribosomal subunit L13 protein−0.56
     C04F12.4rpl-14Large ribosomal subunit L14 protein−0.30
     K11H12.2rpl-15Large ribosomal subunit L15 protein−0.61
     M01F1.2rpl-16Large ribosomal subunit L16 protein−0.73
     Y48G8AL.8rpl-17Large ribosomal subunit L17 protein−0.45
     Y45F10D.12rpl-18Large ribosomal subunit L18 protein−0.66
     C09D4.5rpl-19Large ribosomal subunit L18A protein−0.51
     E04A4.8rpl-20Large ribosomal subunit L20 protein−0.69
     C14B9.7rpl-21Large ribosomal subunit L18A protein−0.51
     D1007.12rpl-24.1Large ribosomal subunit L20 protein−0.51
     F28C6.7rpl-26Large ribosomal subunit L18A protein−0.29
     T24B8.1rpl-32Large ribosomal subunit L20 protein−0.26
     F37C12.4rpl-36Large ribosomal subunit L18A protein−0.39
     C26F1.9rpl-39Large ribosomal subunit L20 protein−0.98
     C09H10.2rpl-41Large ribosomal subunit L18A protein−0.41
     Y48B6A.2rpl-43Large ribosomal subunit L20 protein−0.50
     B0393.1rps-0Small ribosomal subunit S protein−0.49
     F56F3.5rps-1Small ribosomal subunit S1 protein−0.57
     C49H3.11rps-2Small ribosomal subunit S2 protein−0.50
     C23G10.3rps-3Small ribosomal subunit S3 protein−0.50
     Y43B11AR.4rps-4Small ribosomal subunit S4 protein−0.54
     T05E11.1rps-5Small ribosomal subunit S5 protein−0.45
     Y71A12B.1rps-6Small ribosomal subunit S6 protein−0.83
     ZC434.2rps-7Small ribosomal subunit S7 protein−0.39
     F40F11.1rps-11Small ribosomal subunit S11 protein−0.57
     F37C12.9rps-14Small ribosomal subunit S14 protein−0.51
     T08B2.10rps-17Small ribosomal subunit S17 protein−0.41
     Y57G11C.16rps-18Small ribosomal subunit S18 protein−0.48
     F37C12.11rps-21Small ribosomal subunit S21 protein−0.35
     F53A3.3rps-22Small ribosomal subunit S22 protein−0.44
     T07A9.11rps-24Small ribosomal subunit S24 protein−0.53
     H06I04.4ubl-1Small ribosomal subunit S27a protein−0.37
     Y62E10A.1rla-2Ribosomal protein, large subunit, acidic (P1)−0.39
     F10B5.1rpl-10Large ribosomal subunit L10 protein−0.42
     T22F3.4rpl-11.1Large ribosomal subunit L11 protein−1.26
     C27A2.2rpl-22Large ribosomal subunit L22 protein−0.47
     C03D6.8rpl-24.2Large ribosomal subunit L24 protein−0.68
     F52B5.6rpl-25.2Large ribosomal subunit L23a protein−0.82
     C53H9.1rpl-27Large ribosomal subunit L27 protein−0.52
     R11D1.8rpl-28Large ribosomal subunit L28 protein−0.65
     C42C1.14rpl-34Large ribosomal subunit L34 protein−0.53
     ZK1010.1rpl-40Large ribosomal subunit L40 protein−0.52
     C16A3.9rps-13Small ribosomal subunit S13 protein−0.57
     F36A2.6rps-15Small ribosomal subunit S15 protein−0.49
     T05F1.3rps-19Small ribosomal subunit S19 protein−0.44
     Y105E8A.16rps-20Small ribosomal subunit S20 protein−0.47
     F28D1.7rps-23Small ribosomal subunit S23 protein−0.62
     Y41D4B.5rps-28Small ribosomal subunit S28 protein−0.64
     C26F1.4rps-30Small ribosomal subunit S30 protein and ubiquitin−0.43
     F42C5.8rps-8Small ribosomal subunit S8 protein−0.70
     F40F8.10rps-9Small ribosomal subunit S9 protein−0.41
     W01D2.1W01D2.1Orthologue of human RPL37 (ribosomal protein L37)−0.41
     Y37E3.8Y37E3.8Orthologue of human RPL27A (ribosomal protein L27a)−0.40
    mRNA processing
     W03H9.4cacn-1CACtiN (Drosophila cactus interacting protein) homolog−0.65
     F32B6.3F32B6.3Pre-mRNA processing factor 18−0.85
     K07C5.6K07C5.6Homologue of splicing factor SLU7−0.95
     F33A8.1let-858Similarity to eukaryotic initiation factor eIF-4 γ−0.47
     C04H5.6mog-4DEAH helicase−0.65
     EEED8.5mog-5DEAH box helicase 8−0.52
     C50C3.6prp-8Yeast PRP (splicing factor) related−0.27
     Y46G5A.4snrp-200Small nuclear ribonucleoprotein homologue−0.38
     C07E3.1stip-1Septin- and tuftelin-interacting protein homologue−0.84
     W04D2.6W04D2.6Orthologue of human RBM25−0.57
    • Highlighted in grey are the transcripts that were up-regulated in both the polysomal RNA as the total pool of RNA.

    • View popup
    Table 3.

    Primers for qPCR.

    GeneGene IDForward primerReverse primer
    Y45F10D.4178344GTCGCTTCAAATCAGTTCAGCGTTCTTGTCAAGTGATCCGACA
    tba-1172831AGACCAACAAGCCGATGGAGTCCAGTGCGGATCTCATCAAC
    csq-1181563GTGACATCTAAATGGGCACGCCTCACGGGTTTCCTCGTCAA
    eif-1266853TCAGCGTGACAAGGTCAAGGGTGCACTCTGCAGTTGGACT
    eif-3.C172858GGAGGACAAGGACAAGACGGAGAAGGCTCGTGGCTTTTGA
    inf-1175966GGAAGGTCGACACACTCACCATGTCTCCGTGGAGGCAAGA
    rpl-11.1178778GGTTTCGGAGTTCAGGAGCATTGCGGTTCAGAACGACGTA
    rpl-14172818CAAGCTCACCGACTTCGAGAGAGCTCCACTCGGACGATTC
PreviousNext
Back to top
Download PDF
Article Alerts
Sign In to Email Alerts with your Email Address
Email Article

Thank you for your interest in spreading the word on Life Science Alliance.

NOTE: We only request your email address so that the person you are recommending the page to knows that you wanted them to see it, and that it is not junk mail. We do not capture any email address.

Enter multiple addresses on separate lines or separate them with commas.
Mitochondrial ubiquinone–mediated longevity is marked by reduced cytoplasmic mRNA translation
(Your Name) has sent you a message from Life Science Alliance
(Your Name) thought you would like to see the Life Science Alliance web site.
CAPTCHA
This question is for testing whether or not you are a human visitor and to prevent automated spam submissions.
Citation Tools
Clk-1–dependent ubiquinone biosynthesis affects translation
Marte Molenaars, Georges E Janssens, Toon Santermans, Marco Lezzerini, Rob Jelier, Alyson W MacInnes, Riekelt H Houtkooper
Life Science Alliance Aug 2018, 1 (5) e201800082; DOI: 10.26508/lsa.201800082

Citation Manager Formats

  • BibTeX
  • Bookends
  • EasyBib
  • EndNote (tagged)
  • EndNote 8 (xml)
  • Medlars
  • Mendeley
  • Papers
  • RefWorks Tagged
  • Ref Manager
  • RIS
  • Zotero
Share
Clk-1–dependent ubiquinone biosynthesis affects translation
Marte Molenaars, Georges E Janssens, Toon Santermans, Marco Lezzerini, Rob Jelier, Alyson W MacInnes, Riekelt H Houtkooper
Life Science Alliance Aug 2018, 1 (5) e201800082; DOI: 10.26508/lsa.201800082
del.icio.us logo Digg logo Reddit logo Twitter logo CiteULike logo Facebook logo Google logo Mendeley logo
  • Tweet Widget
  • Facebook Like
Issue Cover

In this Issue

Volume 1, No. 5
October 2018
  • Table of Contents
  • Cover (PDF)
  • About the Cover
  • Masthead (PDF)
Advertisement

Jump to section

  • Article
    • Abstract
    • Introduction
    • Results
    • Discussion
    • Materials and Methods
    • Acknowledgements
    • References
  • Figures & Data
  • Info
  • Metrics
  • Reviewer Comments
  • PDF

Subjects

  • Metabolism
  • Aging

Related Articles

  • No related articles found.

Cited By...

  • No citing articles found.
  • Google Scholar

More in this TOC Section

  • Pldo/ZSWIM8 and actin polymerization
  • L-NAME mouse model of preeclampsia
  • Ubiquitination action model of UPL3
Show more Research Article

Similar Articles

EMBO Press LogoRockefeller University Press LogoCold Spring Harbor Logo

Content

  • Home
  • Newest Articles
  • Current Issue
  • Archive
  • Subject Collections

For Authors

  • Submit a Manuscript
  • Author Guidelines
  • License, copyright, Fee

Other Services

  • Alerts
  • Twitter
  • RSS Feeds

More Information

  • Editors & Staff
  • Reviewer Guidelines
  • Feedback
  • Licensing and Reuse
  • Privacy Policy

ISSN: 2575-1077
© 2022 Life Science Alliance LLC

Life Science Alliance is registered as a trademark in the U.S. Patent and Trade Mark Office and in the European Union Intellectual Property Office.