scholarly journals The Glyoxysomal Protease LON2 Is Involved in Fruiting-Body Development, Ascosporogenesis and Stress Resistance in Sordaria macrospora

2021 ◽  
Vol 7 (2) ◽  
pp. 82
Author(s):  
Antonia Werner ◽  
Kolja Otte ◽  
Gertrud Stahlhut ◽  
Leon M. Hanke ◽  
Stefanie Pöggeler
Keyword(s):  
Quality Control ◽  
Fruiting Body ◽  
Protein Quality ◽  
Model Organism ◽  
Protein Quality Control ◽  
Stress Conditions ◽  
Dual Function ◽  
Sordaria Macrospora ◽  
Body Development ◽  
Fruiting Body Development

Microbodies, including peroxisomes, glyoxysomes and Woronin bodies, are ubiquitous dynamic organelles that play important roles in fungal development. The ATP-dependent chaperone and protease family Lon that maintain protein quality control within the organelle significantly regulate the functionality of microbodies. The filamentous ascomycete Sordaria macrospora is a model organism for studying fruiting-body development. The genome of S. macrospora encodes one Lon protease with the C-terminal peroxisomal targeting signal (PTS1) serine-arginine-leucine (SRL) for import into microbodies. Here, we investigated the function of the protease SmLON2 in sexual development and during growth under stress conditions. Localization studies revealed a predominant localization of SmLON2 in glyoxysomes. This localization depends on PTS1, since a variant without the C-terminal SRL motif was localized in the cytoplasm. A ΔSmlon2 mutant displayed a massive production of aerial hyphae, and produced a reduced number of fruiting bodies and ascospores. In addition, the growth of the ΔSmlon2 mutant was completely blocked under mild oxidative stress conditions. Most of the defects could be complemented with both variants of SmLON2, with and without PTS1, suggesting a dual function of SmLON2, not only in microbody, but also in cytosolic protein quality control.

scholarly journals Cdc48 regulates intranuclear quality control sequestration of the Hsh155 splicing factor

2020 ◽  
Author(s):  
Veena Mathew ◽  
Arun Kumar ◽  
Yangyang Kate Jiang ◽  
Kyra West ◽  
Annie S Tam ◽  
...  
Keyword(s):  
Quality Control ◽  
Essential Role ◽  
Protein Quality ◽  
Protein Quality Control ◽  
Genotoxic Stress ◽  
Stress Conditions ◽  
Splicing Factor ◽  
Misfolded Proteins ◽  
Dna Complexes ◽  
Partner Proteins

Cdc48/VCP is a highly conserved ATPase chaperone that plays an essential role in the assembly or disassembly of protein-DNA complexes and in degradation of misfolded proteins. We find that Cdc48 accumulates during cellular stress at intranuclear protein quality control (INQ) sites. Cdc48 function is required to suppress INQ formation under non-stress conditions and to promote recovery following genotoxic stress. Cdc48 physically associates with the INQ substrate and splicing factor Hsh155 and regulates its assembly with partner proteins. Accordingly, cdc48 mutants have defects in splicing and show spontaneous distribution of Hsh155 to INQ aggregates where it is stabilized. Overall, this study shows that Cdc48 regulates deposition of proteins at INQ and suggests a previously unknown role for Cdc48 in the regulation or stability of splicing subcomplexes.

scholarly journals Functional Characterization of MAT1-1-Specific Mating-Type Genes in the Homothallic Ascomycete Sordaria macrospora Provides New Insights into Essential and Nonessential Sexual Regulators

2010 ◽  
Vol 9 (6) ◽  
pp. 894-905 ◽  
Author(s):  
V. Klix ◽  
M. Nowrousian ◽  
C. Ringelberg ◽  
J. J. Loros ◽  
J. C. Dunlap ◽  
...  
Keyword(s):  
Mating Type ◽  
Sexual Development ◽  
Fruiting Body ◽  
Content Type ◽  
Sordaria Macrospora ◽  
Body Development ◽  
Protein Encoding ◽  
Fruiting Body Development ◽  
Mating Type Genes ◽  
Domain Protein

ABSTRACT Mating-type genes in fungi encode regulators of mating and sexual development. Heterothallic ascomycete species require different sets of mating-type genes to control nonself-recognition and mating of compatible partners of different mating types. Homothallic (self-fertile) species also carry mating-type genes in their genome that are essential for sexual development. To analyze the molecular basis of homothallism and the role of mating-type genes during fruiting-body development, we deleted each of the three genes, SmtA-1 (MAT1-1-1), SmtA-2 (MAT1-1-2), and SmtA-3 (MAT1-1-3), contained in the MAT1-1 part of the mating-type locus of the homothallic ascomycete species Sordaria macrospora. Phenotypic analysis of deletion mutants revealed that the PPF domain protein-encoding gene SmtA-2 is essential for sexual reproduction, whereas the α domain protein-encoding genes SmtA-1 and SmtA-3 play no role in fruiting-body development. By means of cross-species microarray analysis using Neurospora crassa oligonucleotide microarrays hybridized with S. macrospora targets and quantitative real-time PCR, we identified genes expressed under the control of SmtA-1 and SmtA-2. Both genes are involved in the regulation of gene expression, including that of pheromone genes.

scholarly journals The pro1+ Gene From Sordaria macrospora Encodes a C6 Zinc Finger Transcription Factor Required for Fruiting Body Development

Genetics ◽  
1999 ◽  
Vol 152 (1) ◽  
pp. 191-199 ◽  
Author(s):  
Sandra Masloff ◽  
Stefanie Pöggeler ◽  
Ulrich Kück
Keyword(s):  
Zinc Finger ◽  
Fruiting Body ◽  
Molecular Mechanisms ◽  
Developmental Process ◽  
Open Reading Frame ◽  
Cosmid Library ◽  
Reading Frame ◽  
Sordaria Macrospora ◽  
Body Development ◽  
Fruiting Body Development

Abstract During sexual morphogenesis, the filamentous ascomycete Sordaria macrospora differentiates into multicellular fruiting bodies called perithecia. Previously it has been shown that this developmental process is under polygenic control. To further understand the molecular mechanisms involved in fruiting body formation, we generated the protoperithecia forming mutant pro1, in which the normal development of protoperithecia into perithecia has been disrupted. We succeeded in isolating a cosmid clone from an indexed cosmid library, which was able to complement the pro1- mutation. Deletion analysis, followed by DNA sequencing, subsequently demonstrated that fertility was restored to the pro1 mutant by an open reading frame encoding a 689-amino-acid polypeptide, which we named PRO1. A region from this polypeptide shares significant homology with the DNA-binding domains found in fungal C6 zinc finger transcription factors, such as the GAL4 protein from yeast. However, other typical regions of C6 zinc finger proteins, such as dimerization elements, are absent in PRO1. The involvement of the pro1+ gene in fruiting body development was further confirmed by trying to complement the mutant phenotype with in vitro mutagenized and truncated versions of the pro1 open reading frame. Southern hybridization experiments also indicated that pro1+ homologues are present in other sexually propagating filamentous ascomycetes.

New insights from an old mutant: SPADIX4 governs fruiting body development but not hyphal fusion in Sordaria macrospora

2016 ◽  
Vol 292 (1) ◽  
pp. 93-104 ◽  
Author(s):  
Ines Teichert ◽  
Miriam Lutomski ◽  
Ramona Märker ◽  
Minou Nowrousian ◽  
Ulrich Kück
Keyword(s):  
Fruiting Body ◽  
Hyphal Fusion ◽  
Sordaria Macrospora ◽  
Body Development ◽  
Fruiting Body Development

scholarly journals Protein Quality Control under Oxidative Stress Conditions

2015 ◽  
Vol 427 (7) ◽  
pp. 1549-1563 ◽  
Author(s):  
Jan-Ulrik Dahl ◽  
Michael J. Gray ◽  
Ursula Jakob
Keyword(s):  
Oxidative Stress ◽  
Quality Control ◽  
Protein Quality ◽  
Protein Quality Control ◽  
Stress Conditions

scholarly journals Mechanismen und Funktionen von bakteriellen AAA+­Entfaltungsmaschinen

BIOspektrum ◽  
2021 ◽  
Vol 27 (1) ◽  
pp. 22-24
Author(s):  
Axel Mogk
Keyword(s):  
Quality Control ◽  
Drug Target ◽  
Protein Quality ◽  
Protein Quality Control ◽  
Stress Conditions ◽  
Misfolded Proteins ◽  
Antibacterial Drug ◽  
Protein Homeostasis ◽  
Antibacterial Drug Target

AbstractBacterial AAA+ proteins play crucial roles in proteostasis networks and ensure protein homeostasis during stress conditions. They function as ATP-dependent components of proteolytic complexes degrading misfolded proteins or as disaggregases reactivating aggregated proteins. AAA+ proteins generate an ATP-fueled threading force driving substrate unfolding and translocation. Their central functions in protein quality control qualify them as antibacterial drug target.

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