Overexpression of Pa_1_10620 encoding a mitochondrial Podospora anserina protein with homology to superoxide dismutases and ribosomal proteins leads to lifespan extension

2014 ◽  
Vol 61 (1) ◽  
pp. 73-86 ◽  
Author(s):  
Carolin Grimm ◽  
Lena Böhl ◽  
Heinz D. Osiewacz
Keyword(s):  
Ribosomal Proteins ◽  
Podospora Anserina ◽  
Superoxide Dismutases ◽  
Lifespan Extension

scholarly journals Cytosolic Ribosomal Mutations That Abolish Accumulation of Circular Intron in the Mitochondria Without Preventing Senescence of Podospora anserina

Genetics ◽  
1997 ◽  
Vol 145 (3) ◽  
pp. 697-705 ◽  
Author(s):  
Philippe Silar ◽  
France Koll ◽  
Michèle Rossignol
Keyword(s):  
Mitochondrial Dna ◽  
Ribosomal Proteins ◽  
Podospora Anserina ◽  
Cox1 Gene ◽  
Accuracy Control ◽  
Additional Function ◽  
Mutant Proteins ◽  
Double Stranded Dna ◽  
Dna Modifications

The filamentous fungus Podospora anserina presents a degeneration syndrome called Senescence associated with mitochondrial DNA modifications. We show that mutations affecting the two different and interacting cytosolic ribosomal proteins (S7 and S19) systematically and specifically prevent the accumulation of senDNAα (a circular double-stranded DNA plasmid derived from the first intron of the mitochondrial cox1 gene or intron α) without abolishing Senescence nor affecting the accumulation of other usually observed mitochondrial DNA rearrangements. One of the mutant proteins is homologous to the Escherichia coli S4 and Saccharomyces cerevisiae S13 ribosomal proteins, known to be involved in accuracy control of cytosolic translation. The lack of accumulation of senDNAα seems to result from a nontrivial ribosomal alteration unrelated to accuracy control, indicating that S7 and S19 proteins have an additional function. The results strongly suggest that modified expression of nucleus-encoded proteins contributes to Senescence in P. anserina. These data do not fit well with some current models, which propose that intron α plays the role of the cytoplasmic and infectious Determinant of Senescence that was defined in early studies.

scholarly journals Does autophagy mediate age-dependent effect of dietary restriction responses in the filamentous fungus Podospora anserina ?

2014 ◽  
Vol 369 (1646) ◽  
pp. 20130447 ◽  
Author(s):  
Anne D. van Diepeningen ◽  
Daniël J. P. Engelmoer ◽  
Carole H. Sellem ◽  
Daphne H. E. W. Huberts ◽  
S. Marijke Slakhorst ◽  
...  
Keyword(s):  
Dietary Restriction ◽  
Filamentous Fungus ◽  
Time Window ◽  
Nutrient Recycling ◽  
Genetic Regulation ◽  
Model Organism ◽  
Podospora Anserina ◽  
Lifespan Extension ◽  
Similar Response ◽  
Wild Type

Autophagy is a well-conserved catabolic process, involving the degradation of a cell's own components through the lysosomal/vacuolar machinery. Autophagy is typically induced by nutrient starvation and has a role in nutrient recycling, cellular differentiation, degradation and programmed cell death. Another common response in eukaryotes is the extension of lifespan through dietary restriction (DR). We studied a link between DR and autophagy in the filamentous fungus Podospora anserina , a multicellular model organism for ageing studies and mitochondrial deterioration. While both carbon and nitrogen restriction extends lifespan in P. anserina, the size of the effect varied with the amount and type of restricted nutrient. Natural genetic variation for the DR response exists. Whereas a switch to carbon restriction up to halfway through the lifetime resulted in extreme lifespan extension for wild-type P. anserina , all autophagy-deficient strains had a shorter time window in which ageing could be delayed by DR. Under nitrogen limitation, only Pa Atg1 and Pa Atg8 mediate the effect of lifespan extension; the other autophagy-deficient mutants Pa PspA and Pa Uth1 had a similar response as wild-type. Our results thus show that the ageing process impinges on the DR response and that this at least in part involves the genetic regulation of autophagy.

scholarly journals The eukaryotic ribosomal protein S15/uS19 is involved in fungal development and its C-terminal tail contributes to stop codon recognition

2020 ◽  
Author(s):  
Tan-Trung Nguyen ◽  
Guillaume Stahl ◽  
Michelle Déquard-Chablat ◽  
Véronique Contamine ◽  
Sylvie Hermann-Le Denmat
Keyword(s):  
Ribosomal Protein ◽  
Ribosomal Proteins ◽  
Stop Codon ◽  
Ribosomal Subunit ◽  
Podospora Anserina ◽  
80S Ribosome ◽  
Fungal Development ◽  
Codon Recognition ◽  
Stop Codon Recognition ◽  
A Site

SummaryS15/uS19 is one of the fifteen universally conserved ribosomal proteins of the small ribosomal subunit. While prokaryotic uS19 is located away from the mRNA decoding site, cross-linking studies identified eukaryotic uS19 C-terminal tail as contacting the A site on the 80S ribosome. Here, we study the effects of uS19 mutations isolated as translation accuracy mutations in the filamentous fungus Podospora anserina. All mutations alter residues of uS19 C-terminal tail, and cluster to the eukaryote-specific decapeptide 138-PGIGATHSSR-147. All mutations modify fungal development and cytosolic translation, albeit differently. Two mutations (P138S and S145F) increase fungus longevity and display mild effects on translation, while others (G139D and G139C) decrease longevity, have stronger effects on translation and confer hypersensitivity to paromomycin. By mimicking P. anserina mutations in the yeast Saccharomyces cerevisiae RPS15 gene, we further show that P138S and S145F induce hyperaccurate recognition of the three stop codons, whereas G139D and G139C impair UAG and UAA codon recognition. Noteworthy, in P. anserina, uS19 genetically interacts with the eRF1 and eRF3 release factors. All together, our data indicate that uS19 C-terminal tail contributes in vivo to eukaryotic translation termination, and identify key amino acids of uS19 that potentially modulate eRF1-eRF3 interaction in the pre-termination complex.Graphical abstractAbbreviated SummaryS15/uS19 is a conserved small ribosomal protein that in eukaryotes harbors a flexible C-terminal extension proposed to interact with the A site mRNA codon during translation. Here, we describe how C-terminal variants variously affect Podospora anserina development and longevity and impact fungal ribosome and polysome formation. We reveal that stop codon recognition is significantly altered by the presence of those C-terminal variants, which either expand or on the contrary restrict termination ambiguity.

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