FAST in Clostridioides difficile! Already well described in various solventogenic and acetogenic Clostridia strains, FAST is now disclosed for the first time ever in pathogenic C. difficile. A nice work by the team of Prof. Isabelle Martin-Verstraete of Institut Pasteur (Paris, France). Published in PLOS Pathogens 2024.
FAST in Clostridium difficile – PLOS Pathogens 2024
Cells exposed to oxidative stress must rapidly adapt and repair their proteins and thiols. Namely, the ubiquitous thioredoxin (Trx) reductase system plays a crucial role in the protection of cysteine from oxidation . Nonetheless, their role, relevance and modalities in the obligate anaerobic Clostridia has remained unexplored. This was the focus of the authors, analyzing three different Trx systems in spores and vegetative cells, and their biological value. Therefore, they built on the unique capability of the fluorescent protein reporter, FAST, to work in anoxic conditions. Notice that this adaptative response might be encountered not only in Clostridia but perhaps in other organisms such as Cyanobacteria or eukaryotes, which have dedicated Trx systems in mitochondria and chloroplasts.
The Twinkle Factory offers commercial fluorogens for FAST and derivatives, splitFAST, greenFAST & redFAST, frFAST. Since recently, the range of reagents also includes fluorogenic molecular glues for CATCHFIRE.
More reading on FAST in Clostridia
- ACS Synth. Biol. 2022 – Establishment of Green- and Red-Fluorescent Reporter Proteins Based on the Fluorescence-Activating and Absorption-Shifting Tag for Use in Acetogenic and Solventogenic Anaerobes
- mBio 2020 – Interspecies Microbial Fusion and Large-Scale Exchange of Cytoplasmic Proteins and RNA in a Syntrophic Clostridium Coculture
- Appl. Environ. Microbiol. 2019 – A Strongly Fluorescing Anaerobic Reporter and Protein-Tagging System for Clostridium Organisms Based on the Fluorescence-Activating and Absorption-Shifting Tag Protein (FAST)
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