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PubMed1986

A DNA polymerase activity with characteristics of a reverse transcriptase in Podospora anserina.

In the filamentous ascomycete fungus Podospora anserina, senescence is associated with dramatic changes of the juvenile mitochondrial genome. During senescence specific regions of the non-senescent genome are excised, ligated and amplified as a plasmid. In this paper, we report our studies on nuclear-mitochondrial extracts for the presence of RNA-dependent DNA polymerase activity (reverse transcriptase). In so-called middle aged mycelia of race A, we detected a DNA polymerase possessing properties of a reverse transcriptase. It prefers the ribopolymer templates poly(rA)-oligo(dT)12-18 and poly(rCm)-oligo(dG)12-18 over the deoxypolymer template poly(dA)-oligo(dT)12-18. It also uses natural rabbit globin mRNA as a template. The enzymatic activity can clearly be distinguished from a second DNA polymerase activity found in the same extracts of both young and middle aged mycelia.

Aging↗
PubMed1985

Analysis of class I introns in a mitochondrial plasmid associated with senescence of Podospora anserina reveals extraordinary resemblance to the Tetrahymena ribosomal intron.

Recently, the nucleotide sequences for three "mitochondrial plasmids" associated with senescence of Podospora anserina were determined (Cummings et al. 1985). One of these sequences, corresponding to the plasmid termed epsilon senDNA, contains three class I introns, all within a protein coding sequence equivalent to the mammalian "URF1" gene. Here, we present primary and secondary structure analyses for two of these introns as well as a partial analysis for the third, which extends beyond the DNA sequence determined. With regard to both primary and secondary structure, the closest known relative of intron 1 is the self-splicing intron in the large ribosomal RNA gene of Tetrahymena. One secondary structure domain at the periphery of intron 1 and Tetrahymena models is also present in intron 2. The latter intron is the longest known class I member and contains remnants of two protein-coding sequences, one of which is split by the other. Evolutionary processes that might be responsible for the unusual structure of introns 1 and 2 are discussed.

Animals↗
PubMed1986

Positive screening and transformation of ura5 mutants in the fungus Podospora anserina: characterization of the transformants.

To develop a transformation system in the filamentous fungus Podospora anserina we have selected ura5 mutants deficient in orotidylic acid pyrophosphorylase using a positive screening. These mutants could be transformed to prototrophy by an hybrid vector carrying the ura5 gene of this organism. The properties of the transformants have been analysed. In most cases integration of the transforming vector occurred outside the ura5 locus and frequently repeated tandem copies of the vector were found. Reversion of the transformants could also be selected and we found that it can occur by exact or only partial excision of the integrated vector.

Ascomycota↗
PubMed1985

The onset of senescence is affected by DNA rearrangements of a discontinuous mitochondrial gene in Podospora anserina.

Mapping and transcription studies have revealed that in Podospora anserina the causative agent of senescence, a mitochondrial plasmid (plDNA), is identical with intron 1 of the discontinuous gene for cytochrome-c-oxidase subunit 1 (COI), which is 2 kpb from the discontinuous gene for cytochrome b (Cytb). A mitochondrial mutant (ex1) devoid of the COI, but not of the Cytb gene provides longevity. A molecular model for the onset of senescence is presented.

Amino Acid Sequence↗
PubMed1977

The phenol oxidases of the ascomycete Podospora anserina. XII. Affinity of laccases II and III to substrates with different substitution patterns.

For the low molecular weight laccases II and III of Podospora anserina the kinetic parameters Michaelis constant (KM) and maximum reaction velocity (V) were determined polarographically under pH optimum conditions for representative substrates of different substitution patterns. Laccase II showed two peaks in its pH optimum curve, each with a different substrate specificity, indicating structural differences to laccase III which exhibits only one broad peak. Under optimum conditions the affinities of various substrates are determined by their substitution patterns: high affinity for simple o- and p-diphenols, low affinity for m-henols. The maximal velocity remains largely uninfluenced. This study of the effect of substitution on substrate utilization leads to the assumption that there is no specific reactive site for m-phenols in either laccase. Oxidation of m-phenols, however, takes only place at high pH values.

Ascomycota↗
PubMed1986

Genetics of translational fidelity in Podospora anserina: are all the genes involved in this ribosomal function identified?

Su12-1 and su12-2 are two ribosomal suppressor mutations previously described in the fungus Podospora anserina. Revertants were isolated on the criteria of either improved growth at 27 degrees C (for su12-1) or suppression of the paromomycin hypersensitivity (for su12-2). Among 45 mutations lying outside the su12 locus, only one was found which defines a new antisuppressor locus, AS9. About 3/4 of these mutations are antisuppressor mutations localized in the previously identified AS6 and AS7 genes. While the AS6 mutations harbour diverse phenotypes, all the mutations lying in the AS7 gene lead to the same phenotypic alterations. In addition, two new su3 mutations were obtained and shown to display an antisuppressor effect on su12-1.

Ascomycota↗
PubMed1981

Ribosomal suppressors and antisuppressors in Podospora anserina: altered susceptibility to paromomycin and relationships between genetic and phenotypic suppression.

Informational suppressors and antisuppressors have been previously isolated in Podospora anserina, and their properties suggest that they could be ribosomal mutants involved in the control of translational fidelity. In this paper we present results concerning relationships between these mutants and paromomycin, an aminoglycoside antibiotic known to stimulate translational errors. The mutants were found to manifest an altered growth sensitivity to this drug as compared with the wild-type strain: Most of the suppressors were more sensitive and, in contrast, most of the antisuppressors were more resistant to paromomycin. Moreover, phenotypic suppression of an auxotrophic mutation by paromomycin was observed only if a suppressor and an antisuppressor had been introduced in the strain. These results suggest that ambiguity levels could be altered in the suppressor and antisuppressor strains. In addition, paromomycin was shown to abolish sporulation, which suggests relationships between mistranslation and a step of cellular differentiation.

Ascomycota↗
PubMed1978

Genetic and biochemical analysis of cycloheximide resistance in the fungus Podospora anserina.

Genetic analysis of cycloheximide-resistant mutants has shown that at least three genes control the resistance to cycloheximide in Podospora anserina and that the antibiotic resistance is recessive to sensitivity. In vitro and in vivo studies of protein synthesis indicated that for two mutants cycloheximide resistance is associated with the ribosomes. For one of these mutants, the elongation step in protein biosynthesis is insensitive to cycloheximide over a wide range of concentration. In this mutant the resistance to cycloheximide is a property of the 60S subunit.

Ascomycota↗
PubMed1980

Search for ribosomal mutants in Podospora anserina: genetic analysis of mutants resistant to paromomycin.

It has recently been shown that paromomycin, an antibiotic of the aminoglycoside family, is also active on eukaryotic cytoplasmic ribosomes. In the fungus Podospora anserina, genetic analysis of ten mutants resistant to high doses of paromomycin shows that this resistance is caused by mutations in two different nuclear genes. These mutants display pleiotropic phenotypes (cold sensitivity, mycelium and spore appearance and coloration, cross-resistance to other antibiotics). Double mutants are either lethal or very altered and unstable. Moreover, the cytochrome spectra of these mutants seem to indicate that cytoplasmic protein synthesis is affected. The mutants also display a slight suppressor effect. We can therefore assume that these mutations affect cytoplasmic ribosomes.

Ascomycota↗
PubMed1992

Self-splicing of a mitochondrial group I intron from the cytochrome b gene of the ascomycete Podospora anserina.

We have shown that the second intron of the Podospora mitochondrial gene coding for cytochrome b (Cytb 12) splices autocatalytically, using in vitro transcripts generated from the T7 promoter. The reaction takes place at 37 degrees C in the presence of 50 mM TRIS-HCl pH 7.5, 60 mM MgCl2 and 1 mM GTP but shows a low efficiency even at high KCl concentrations of up to 1.2 M. Under these conditions, intron bI2 follows the conventional pathway of group I splicing, and all characteristic products, with regard to both transesterification and hydrolysis, could be identified. Moreover, the intron is capable of undergoing cyclization, thereby releasing the noncoded G and one additional nucleotide (U) from the 5' end. The 5' cleavage site is preceded by the same two nucleotides, indicating a base-pairing at the same site of the internal guide sequence (IGS) for both splicing and cyclization ("one-binding-site model"). In addition, products resulting from site-specific hydrolysis 138 nucleotides downstream of the 5' splice site were detected. Unusually, the shortened intron is also able to form a circular RNA and an alternative sequence that aligns the cyclization site to the catalytic core of the intron must be assumed.

Ascomycota↗
PubMed1992

The mating types of Podospora anserina: functional analysis and sequence of the fertilization domains.

The two idiomorphic alleles called mat+ and mat-, which control the mating types in Podospora anserina, have been cloned. Mat+ and mat- encompass 3.8 kb and 4.7 kb respectively, of unrelated DNA sequences flanked by common sequences. Subcloning allowed the identification and localization in each locus of the gene that controls fertilization, probably by determining the mating type. The mat+ gene, called FPR1, encodes a protein with a potential DNA-binding HMG domain. The presence of this motif suggests that the FPR1 polypeptide may act as a transcriptional factor. The mat- gene called FMR1 encodes a protein containing a motif that is also found in proteins controlling mating functions in Saccharomyces cerevisiae and Neurospora crassa. The role of this motif has not yet been established. Unlike the mat+ locus, where the FPR1 gene seems to represent the major information, the mat- locus contains information necessary for the post-fertilization steps of the sexual cycle besides the FMR1 gene.

Amino Acid Sequence↗
PubMed1977

Mitochondrial genes in Podospora anserina: recombination and linkage.

A fifth cytoplasmic mutation (capr 1) obtained in Podospora anserina is described. In addition to chloramphenicol resistance it confers a strong deficiency in cytochrome aa3 and impairs the germination of ascospores. Genetic analysis shows: 1) strict maternal inheritance of (capr 1) allele; 2) selection against the (capr 1) allele as well in sexual crosses as during vegetative growth; 3) complete reversion of this selection by even low concentration of CAP. On the basis of their cytoplasmic inheritance and altered cytochrome spectra the five cytoplasmic mutations are assumed to be mitochondrial. Analysis of crosses between them allows to class them in 3 loci, 2 of which being closely linked.

Alleles↗
PubMed1989

DNA sequence, structure, and phylogenetic relationship of the small subunit rRNA coding region of mitochondrial DNA from Podospora anserina.

DNA sequence analysis and the localization of the 5' and 3' termini by S1 mapping have shown that the mitochondrial (mt) small subunit rRNA coding region from Podospora anserina is 1980 bp in length. The analogous coding region for mt rRNA is 1962 bp in maize, 1686 bp in Saccharomyces cerevisiae, and 956 bp in mammals, whereas its counterpart in Escherichia coli is 1542 bp. The P. anserina mt 16S-like rRNA is 400 bases longer than that from E. coli, but can be folded into a similar secondary structure. The additional bases appear to be clustered at specific locations, including extensions at the 5' and 3' termini. Comparison with secondary structure diagrams of 16S-like RNAs from several organisms allowed us to specify highly conserved and variable regions of this gene. Phylogenetic tree construction indicated that this gene is grouped with other mitochondrial genes, but most closely, as expected, with the fungal mitochondrial genes.

Ascomycota↗
PubMed1989

DNA sequence and secondary structures of the large subunit rRNA coding regions and its two class I introns of mitochondrial DNA from Podospora anserina.

DNA sequence analysis has shown that the gene coding for the mitochondrial (mt) large subunit ribosomal RNA (rRNA) from Podospora anserina is interrupted by two class I introns. The coding region for the large subunit rRNA itself is 3715 bp and the two introns are 1544 (r1) and 2404 (r2) bp in length. Secondary structure models for the large subunit rRNA were constructed and compared with the equivalent structure from Escherichia coli 23S rRNA. The two structures were remarkably similar despite an 800-base difference in length. The additional bases in the P. anserina rRNA appear to be mostly in unstructured regions in the 3' part of the RNA. Secondary structure models for the two introns show striking similarities with each other as well as with the intron models from the equivalent introns in Saccharomyces cerevisiae, Neurospora crassa, and Aspergillus nidulans. The long open reading frames in each intron are different from each other, however, and the nucleotide sequence similarity diverges as it proceeds away from the core structure. Each intron is located within regions of the large subunit rRNA gene that are highly conserved in both sequence and structure. Computer analysis showed that the open reading frame for intron r1 contained a common maturase-like polypeptide. The open reading frames of intron r2 appeared to be chimeric, displaying high sequence similarity with the open reading frames in the r1 and ATPase 6 introns of N. crassa.

Ascomycota↗
PubMed1996

Isolation and characterization of a laccase gene from Podospora anserina.

The genome of the filamentous ascomycete Podospora anserina contains at least four non-adjacent regions that are homologous to the laccase gene of Neurospora crassa. One of these regions contains a gene (lac2) encoding a protein that displays 62% identity with the N. crassa laccase. In shaken cultures, lac2 mRNA is present at low basal levels throughout the growth phase but increases at least 20-fold at the beginning of the autolytic phase and decreases again thereafter. Addition of aromatic xenobiotics (guaiacol, hydroquinone, benzoquinone) to the medium during the growth phase results in a rapid, drastic and temporary increase in the abundance of lac2 mRNA. The promoter region of lac2 contains two sequences which display complete homology with the eukaryotic Xenobiotic Responsive Element and two sequences homologous to the eukaryotic Antioxidant Responsive Element. The identity and function of the laccase encoded by lac2 are discussed.

Amino Acid Sequence↗
PubMed1996

GRISEA, a putative copper-activated transcription factor from Podospora anserina involved in differentiation and senescence.

Podospora anserina is a filamentous fungus with a limited lifespan. Lifespan is controlled by both environmental and genetic factors. Using a combination of genetic and molecular approaches we have cloned one of these factors, gerontogene grisea. The cloned wild-type copy of grisea complements the altered morphological characteristics (e.g., colony and ascospore color), the defect in gametangia development, and the increased lifespan of the pleiotropic mutant grisea. A molecular analysis revealed that grisea is a discontinuous gene with a single intron. The deduced amino acid sequence shows significant homology to MAC1, ACE1 and AMT1, indicating that GRISEA, like the proteins from Saccharomyces cerevisiae (MAC1 and ACE1) and Candida glabrata (AMT1), codes for a copper-activated transcription factor. This conclusion is consistent with the pleiotropic nature of the grisea phenotype. We suggest that the gerontoprotein GRISEA is one component of a transcription apparatus involved in the genetic control of morphogenesis and aging.

Amino Acid Sequence↗
PubMed1996

Induction of longevity by cytoplasmic transfer of a linear plasmid in Podospora anserina.

In Podospora anserina the longevity inducing linear plasmid pAL2-1 was transferred from the extrachromosomal long-lived mutant AL2 to the short-lived wild-type strain A. The resulting strain, AL2-IV, exhibited the long-lived phenotype. In the short-lived progeny of crosses between this strain and wild-type strain A, the plasmid was absent. In contrast, all long-lived progeny contained both the autonomous plasmid as well as copies of it integrated in the mitochondrial DNA (mtDNA). Molecular analysis revealed that the integrated plasmid copies most likely resulted from a de novo integration of the autonomous element and the generation of AT-linker sequences at the integration site. We conclude that once the plasmid is present in mitochondria of a particular genetic background, it is able to integrate into the mtDNA and to induce longevity.

Ascomycota↗
PubMed1976

Regulation of proteolytic enzymes in Podospora anserina: selection and properties of self-lysing mutant strains.

Previous results showed that cell disintegration in the fungus Podospora anserina occured through the action of two proteases, enzymes whose messengers were normally latent during the extension stage of the thallus. We selected three mutant strains in which the constitutive activity of the protease messengers was expressed by an arrest of growth early in development (10 to 30 hours after spore germination) and a reaction of cell disintegration, in the thallus, suppressible with beta-phenyl pyruvic acid, a protease inhibitor. The mutant character is recessive in one strain. In the case of the two strains in which the mutant trait is dominant, reversion studies have revealed that the deregulation resulted from the specific interaction between two genes and we have succeded in creating two non allelic incompatibility systems comparable to the non allelic gene interactions responsible for the incompatibility phenomena found between wild type races. We know, on the whole, that 11 loci are involved in the regulation of the proteases: five were revealed as incompatibility loci and six were discovered from investigations on four self-lysing mutant strains. It is suspected that all these genes act at the post-transcriptionnal level of the synthesis of specific proteolytic enzymes. We propose that the products of two genes act as "repressors" to prevent the protease messengers from being constitutively translated and that the products of the nine remaining genes exert a positive control by inducing translation, at the appropriate time, through the action of effectors resulting from specific interloci cooperation.

Alleles↗