scholarly journals Haste makes waste: The significance of translation fidelity for development and longevity

2021 ◽  
Vol 81 (18) ◽  
pp. 3675-3676
Author(s):  
Kenneth A. Wilson ◽  
Sudipta Bar ◽  
Pankaj Kapahi
Keyword(s):  
Translation Fidelity

scholarly journals Identification of the Genes Encoding the Cytosolic Translation Release Factors from Podospora anserina and Analysis of Their Role During the Life Cycle

Genetics ◽  
1998 ◽  
Vol 149 (4) ◽  
pp. 1763-1775 ◽  
Author(s):  
Bénédicte Gagny ◽  
Philippe Silar
Keyword(s):  
Life Span ◽  
Translation Termination ◽  
Podospora Anserina ◽  
Terminal Region ◽  
Terminal Portion ◽  
Nonsense Mutations ◽  
Translation Fidelity ◽  
Reproductive Impairment ◽  
Genes Encoding ◽  
Nonsense Suppressor

Abstract In an attempt to decipher their role in the life history and senescence process of the filamentous fungus Podospora anserina, we have cloned the su1 and su2 genes, previously identified as implicated in cytosolic translation fidelity. We show that these genes are the equivalents of the SUP35 and SUP45 genes of Saccharomyces cerevisiae, which encode the cytosolic translation termination factors eRF3 and eRF1, respectively. Mutations in these genes that suppress nonsense mutations may lead to drastic mycelium morphology changes and sexual impairment but have little effect on life span. Deletion of su1, coding for the P. anserina eRF3, is lethal. Diminution of its expression leads to a nonsense suppressor phenotype whereas its overexpression leads to an antisuppressor phenotype. P. anserina eRF3 presents an N-terminal region structurally related to the yeast eRF3 one. Deletion of the N-terminal region of P. anserina eRF3 does not cause any vegetative alteration; especially life span is not changed. However, it promotes a reproductive impairment. Contrary to what happens in S. cerevisiae, deletion of the N terminus of the protein promotes a nonsense suppressor phenotype. Genetic analysis suggests that this domain of eRF3 acts in P. anserina as a cis-activator of the C-terminal portion and is required for proper reproduction.

scholarly journals Structural insights into mRNA reading frame regulation by tRNA modification and slippery codon-anticodon pairing

2020 ◽  
Author(s):  
Eric D. Hoffer ◽  
Samuel Hong ◽  
S. Sunita ◽  
Tatsuya Maehigashi ◽  
Ruben L. Gonzalez ◽  
...  
Keyword(s):  
Conformational Changes ◽  
Data Bank ◽  
Reading Frame ◽  
Translation Fidelity ◽  
Bacterial Ribosome ◽  
Structure Factors ◽  
Sequential Addition ◽  
Polypeptide Chains ◽  
Structural Insights ◽  
Atomic Coordinates

ABSTRACTModifications in the tRNA anticodon, adjacent to the three-nucleotide anticodon, influence translation fidelity by stabilizing the tRNA to allow for accurate reading of the mRNA genetic code. One example is the N1-methylguaonosine modification at guanine nucleotide 37 (m1G37) located in the anticodon loop, immediately adjacent to the anticodon nucleotides 34-36. The absence of m1G37 in tRNAPro causes +1 frameshifting on polynucleotide, slippery codons. Here, we report structures of the bacterial ribosome containing tRNAPro bound to either cognate or slippery codons to determine how the m1G37 modification prevents mRNA frameshifting. The structures reveal that certain codon-anticodon contexts and m1G37 destabilize interactions of tRNAPro with the peptidyl site, causing large conformational changes typically only seen during EF-G mediated translocation of the mRNA-tRNA pairs. These studies provide molecular insights into how m1G37 stabilizes the interactions of tRNAPro with the ribosome and the influence of slippery codons on the mRNA reading frame.IMPACT STATEMENTChemical modifications near the tRNA anticodon and specific mRNA-tRNA pairs combine to control the ribosomal three-nucleotide mRNA reading frame, essential for the sequential addition of amino acids into polypeptide chains.Data depositionCrystallography, atomic coordinates, and structure factors have been deposited in the Protein Data Bank, www.pdb.org (PDB codes 6NTA, 6NSH, 6NUO, 6NWY, 6O3M, 6OSI)

scholarly journals Production and Application of Stable Isotope-Labeled Internal Standards for RNA Modification Analysis

Genes ◽  
2019 ◽  
Vol 10 (1) ◽  
pp. 26 ◽  
Author(s):  
Kayla Borland ◽  
Jan Diesend ◽  
Taku Ito-Kureha ◽  
Vigo Heissmeyer ◽  
Christian Hammann ◽  
...  
Keyword(s):  
Messenger Rna ◽  
Isotope Labeling ◽  
Rna Stability ◽  
Internal Standard ◽  
Modified Nucleosides ◽  
Rna Modification ◽  
Mouse Tissue ◽  
Rna Modifications ◽  
Internal Standards ◽  
Translation Fidelity

Post-transcriptional RNA modifications have been found to be present in a wide variety of organisms and in different types of RNA. Nucleoside modifications are interesting due to their already known roles in translation fidelity, enzyme recognition, disease progression, and RNA stability. In addition, the abundance of modified nucleosides fluctuates based on growth phase, external stress, or possibly other factors not yet explored. With modifications ever changing, a method to determine absolute quantities for multiple nucleoside modifications is required. Here, we report metabolic isotope labeling to produce isotopically labeled internal standards in bacteria and yeast. These can be used for the quantification of 26 different modified nucleosides. We explain in detail how these internal standards are produced and show their mass spectrometric characterization. We apply our internal standards and quantify the modification content of transfer RNA (tRNA) from bacteria and various eukaryotes. We can show that the origin of the internal standard has no impact on the quantification result. Furthermore, we use our internal standard for the quantification of modified nucleosides in mouse tissue messenger RNA (mRNA), where we find different modification profiles in liver and brain tissue.

scholarly journals The nature of the purine at position 34 in tRNAs of 4-codon boxes is correlated with nucleotides at positions 32 and 38 to maintain decoding fidelity

2020 ◽  
Vol 48 (11) ◽  
pp. 6170-6183 ◽  
Author(s):  
Ketty Pernod ◽  
Laure Schaeffer ◽  
Johana Chicher ◽  
Eveline Hok ◽  
Christian Rick ◽  
...  
Keyword(s):  
Intergenic Region ◽  
Bacterial Genomes ◽  
Eukaryotic Translation ◽  
Eukaryotic Ribosome ◽  
Translation Fidelity ◽  
Translation Systems ◽  
Eukaryotic Genomes ◽  
Paralysis Virus ◽  
Decoding Fidelity

Abstract Translation fidelity relies essentially on the ability of ribosomes to accurately recognize triplet interactions between codons on mRNAs and anticodons of tRNAs. To determine the codon-anticodon pairs that are efficiently accepted by the eukaryotic ribosome, we took advantage of the IRES from the intergenic region (IGR) of the Cricket Paralysis Virus. It contains an essential pseudoknot PKI that structurally and functionally mimics a codon-anticodon helix. We screened the entire set of 4096 possible combinations using ultrahigh-throughput screenings combining coupled transcription/translation and droplet-based microfluidics. Only 97 combinations are efficiently accepted and accommodated for translocation and further elongation: 38 combinations involve cognate recognition with Watson-Crick pairs and 59 involve near-cognate recognition pairs with at least one mismatch. More than half of the near-cognate combinations (36/59) contain a G at the first position of the anticodon (numbered 34 of tRNA). G34-containing tRNAs decoding 4-codon boxes are almost absent from eukaryotic genomes in contrast to bacterial genomes. We reconstructed these missing tRNAs and could demonstrate that these tRNAs are toxic to cells due to their miscoding capacity in eukaryotic translation systems. We also show that the nature of the purine at position 34 is correlated with the nucleotides present at 32 and 38.

scholarly journals In Xenopus laevis, the product of a developmentally regulated mRNA is structurally and functionally homologous to a Saccharomyces cerevisiae protein involved in translation fidelity.

1993 ◽  
Vol 13 (5) ◽  
pp. 2815-2821 ◽  
Author(s):  
J P Tassan ◽  
K Le Guellec ◽  
M Kress ◽  
M Faure ◽  
J Camonis ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Sequence Analysis ◽  
Structural Homology ◽  
Developmentally Regulated ◽  
Functional Homology ◽  
Translation Fidelity ◽  
Functional Homolog ◽  
Xenopus Egg ◽  
Higher Eukaryotes ◽  
Nonsense Codons

We have performed a differential screen of a Xenopus egg cDNA library and selected two clones (Cl1 and Cl2) corresponding to mRNA which are specifically adenylated and recruited into polysomes after fertilization. Sequence analysis of Cl1 reveals that the corresponding protein is 67.5% identical (83% similar) to the product of the Saccharomyces cerevisiae SUP45 (also called SUP1 or SAL4) gene. This gene, when mutated, is an omnipotent suppressor of nonsense codons. When expressed in a sup45 mutant, the Xenopus Cl1 cDNA was able to suppress sup45-related phenotypes, showing that the structural homology reflects a functional homology. Our discovery of a structural and functional homolog in Xenopus cells implies that the function of SUP45 is not restricted to lower eukaryotes and that the SUP45 protein may perform a crucial cellular function in higher eukaryotes.

scholarly journals THE CONCEPT OF FIDELITY IN COMICS TRANSLATION

2016 ◽  
Vol 8 (2) ◽  
pp. 8
Author(s):  
Erico Assis
Keyword(s):  
Literary Translation ◽  
Literary Texts ◽  
Reading Process ◽  
Fair Share ◽  
Source Text ◽  
Topological Relations ◽  
Page Layout ◽  
Translation Fidelity ◽  
Linguistic Sign

The long-discussed – and frequently dismissed – concept of translation faithfulness or translation fidelity, though usually applied to literary texts, has its fair share of applications when considered for comics translation. In literary translation, non-linguistic portions such as illustrations are often considered addenda or “paratexts” relative to the main, linguistic text. Comics, by its turn, present a certain set of features which single them out as a form that demands a new concept of “text” and, therefore, of translation fidelity. The comic-reading process, as pertaining to cognitive apprehension, implies interpretative accords that differ from the ones in purely linguistic texts: each and every element of the comics page – non-linguistic (mainly imagetic) signs, linguistic signs, panel borders, typography and such – are intertwined and should be perceived in regards to its spatial and topological relations. This approach to understanding comics is based on Groensteen (1999) and his concepts of arthrology, spatio-topia, page layout, breakdown and braiding. As for translation fidelity, we rely on authors such as Berman (1984), Guidere (2010) and Aubert (1993). On comics translation, Zanettin (2008), Rota (2008) and Yuste Frías (2010, 2011) are of particular interest. Based on various concepts of fidelity – supported by samples of translated comics with varied degrees of fidelity to the source text – we discuss the different grounds of source-text fidelity, target-reader fidelity and source-author fidelity in the following instances: linguistic sign fidelity, imagetic sign fidelity, spatio-topia fidelity, typographic fidelity and format fidelity.

scholarly journals The dominant PNM2- mutation which eliminates the psi factor of Saccharomyces cerevisiae is the result of a missense mutation in the SUP35 gene.

Genetics ◽  
1994 ◽  
Vol 137 (3) ◽  
pp. 659-670 ◽  
Author(s):  
S M Doel ◽  
S J McCready ◽  
C R Nierras ◽  
B S Cox
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Suppressor Gene ◽  
Chain Termination ◽  
Major Band ◽  
Minor Band ◽  
Terminal Domain ◽  
Translation Fidelity ◽  
Extrachromosomal Element ◽  
A Minor ◽  
Sup35 Gene

Abstract The PNM2- mutation of Saccharomyces cerevisiae eliminates the extrachromosomal element psi. PNM2 is closely linked to the omnipotent suppressor gene SUP35 (also previously identified as SUP2, SUF12, SAL3 and GST1). We cloned PNM2- and showed that PNM2 and SUP35 are the same gene. We sequenced the PNM2- mutant allele and found a single G-->A transition within the N-terminal domain of the protein. We tested the effects of various constructs of SUP35 and PNM2- on psi inheritance and on allosuppressor and antisuppressor functions of the gene. We found that the C-terminal domain of SUP35 protein (SUP35p) could be independently expressed; expression produced dominant antisuppression. Disruption of the N-terminal domain of PNM2- destroyed the ability to eliminate psi. These results imply that the domains of SUP35p act in an antagonistic manner: the N-terminal domain decreases chain-termination fidelity, while the C-terminal domain imposes fidelity. Two transcripts were observed for SUP35, a major band at 2.4 kb and a minor band at 1.3 kb; the minor band corresponds to 3' sequences only. We propose a model for the function of SUP35, in which comparative levels of N- and C-terminal domains of SUP35p at the ribosome modulate translation fidelity.

scholarly journals Translation fidelity coevolves with longevity

Aging Cell ◽  
2017 ◽  
Vol 16 (5) ◽  
pp. 988-993 ◽  
Author(s):  
Zhonghe Ke ◽  
Pramit Mallik ◽  
Adam B. Johnson ◽  
Facundo Luna ◽  
Eviatar Nevo ◽  
...  
Keyword(s):  
Translation Fidelity
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