A5091176160- Prion Diseases and Protein Misfolding
- Alzheimer's disease research and treatments
- Neurological diseases and metabolism
- Trace Elements in Health
- Enzyme Structure and Function
- RNA and protein synthesis mechanisms
- Microbial Metabolic Engineering and Bioproduction
- Computational Drug Discovery Methods
- Biofuel production and bioconversion
- Protein Structure and Dynamics
- Cholinesterase and Neurodegenerative Diseases
- Bacterial Genetics and Biotechnology
- Healthcare and Venom Research
- Viral Infections and Immunology Research
- Metalloenzymes and iron-sulfur proteins
- Monoclonal and Polyclonal Antibodies Research
- Escherichia coli research studies
- RNA Research and Splicing
Centre National de la Recherche Scientifique
2002-2021
Université de Toulouse
2012-2021
Université Toulouse III - Paul Sabatier
2012-2021
Institut de Pharmacologie et de Biologie Structurale
2019-2021
Uppsala University
2008-2011
Institut de Biochimie et Génétique Cellulaires
2002-2007
Université de Bordeaux
2002-2007
Institut Européen de Chimie et Biologie
2003
The [Het-s] infectious element of the filamentous fungus Podospora anserina is a prion. We have recently reported that recombinant HET-s protein aggregates in vitro into amyloid fibers. In vivo , specifically prion strains. Here, we show biolistic introduction aggregated fungal cells induces emergence with high frequency. Thus, demonstrate infectivity can be created de novo from this system. Although filaments formed could transmit efficiently, neither soluble form nor amorphous would do so....
The HET-s protein of Podospora anserina is a fungal prion. This behaves as an infectious cytoplasmic element that transmitted horizontally from one strain to another. Under the prion form, forms aggregates in vivo. specificity this model compared with yeast prions resides fact under form causes growth inhibition and cell death reaction when co-expressed HET-S which it differs by 13 residues. Herein we describe purification initial characterization recombinant expressed Escherichia coli....
Background6-Aminophenanthridine (6AP) and Guanabenz (GA, a drug currently in use for the treatment of hypertension) were isolated as antiprion drugs using yeast-based assay. These structurally unrelated molecules are also active against mammalian prion several cell-based assays vivo mouse model prion-based diseases.Methodology/Principal FindingsHere we report identification cellular targets these drugs. Using affinity chromatography matrices both drugs, demonstrate an RNA-dependent...
Alzheimer's disease, characterized by deposits of amyloid β-peptide (Aβ), is the most common neurodegenerative but it still lacks a specific treatment. We have discovered five chemically unrelated inhibitors in vitro aggregation Aβ17–40 peptide screening two commercial chemical libraries. Four them (1–4) exhibit relatively low MCCs toward HeLa cells (17–184 μM). The usefulness compounds 1–4 to inhibit vivo Aβ1–42 has been demonstrated using fungi models, Saccharomyces cerevisiae and...
The [Het-s] prion of the fungus Podospora anserina propagates as a self-perpetuating amyloid form HET-s protein. This protein triggers cell death reaction termed heterokaryon incompatibility when interacting with HET-S protein, an allelic variant HET-s. displays two distinct domains, N-terminal globular domain and C-terminal unstructured prion-forming (residues 218-289). Here, we describe characterization HET-s(157-289), truncated bearing extensive deletion in but retaining full activity...
The [Het-s] infectious element of the filamentous fungus Podospora anserina corresponds to prion form HET-s protein. (289 amino acids in length) aggregates into amyloid fibers vitro. Such obtained vitro are infectious, indicating that can propagate as a self-perpetuating aggregate Previous analyses have suggested only limited region protein is involved formation and propagation. To document conformational transition occurring upon aggregation HET-s, we developed method involving...
Abstract SecB chaperones assist protein export by binding both unfolded proteins and the SecA motor. Certain homologs can also control toxin-antitoxin (TA) systems known to modulate bacterial growth in response stress. In such TA-chaperone (TAC) systems, assists folding prevents degradation of antitoxin, thus facilitating toxin inhibition. Chaperone dependency is conferred a C-terminal extension antitoxin as chaperone addiction (ChAD) sequence, which makes aggregation-prone Using TAC...
The chaperones of the ClpB/HSP100 family play a central role in thermotolerance bacteria, plants, and fungi by ensuring solubilization heat-induced protein aggregates. In addition yeast, Hsp104 was found to be required for prion propagation. Herein, we analyze Podospora anserina (PaHsp104) formation propagation [Het-s] prion. We show that DeltaPaHsp104 strains propagate [Het-s], making first native fungal propagated absence Hsp104. Nevertheless, [Het-s]-propagon numbers, rate, spontaneous...
Abstract Clostridium acetobutylicum is a promising biocatalyst for the production of n-butanol at high yield from renewable resources. Several metabolic strategies have already been developed to increase butanol yields, most often based on carbon pathway redirection. However, it was previously demonstrated that activities both ferredoxin-NADP+ reductase and ferredoxin-NAD+ reductase, whose encoding genes remained unknown until this study, were necessary produce NADPH extra NADH needed...