ArticleScientific reports2018
Mycobacterium tuberculosis CarD, an essential global transcriptional regulator forms amyloid-like fibrils.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 27 citations in OpenAlex.
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- Widespread amyloid aggregates formation by Zika virus proteins and peptides.Protein science : a publication of the Protein Society · 2023Article
- Phosphoproteome Dynamics of Streptomyces rimosus during Submerged Growth and Antibiotic Production.mSystems · 2022Article
- Is amyloid fibrillation related to 3D domain swapping for the C-terminal domain of SARS-CoV main protease?International journal of biological macromolecules · 2022Article
- Proteomic Signatures of Microbial Adaptation to the Highest Ultraviolet-Irradiation on Earth: Lessons From a Soil Actinobacterium.Frontiers in microbiology · 2022Article
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- On the border of the amyloidogenic sequences: prefix analysis of the parallel beta sheets in the PDB_Amyloid collection.Journal of integrative bioinformatics · 2021Article
- Licensed Anti-Microbial Drugs Logical for Clinical Trials against Pathogens Currently Suspected in Alzheimer's Disease.Antibiotics (Basel, Switzerland) · 2021Article
- Redefining fundamental concepts of transcription initiation in bacteria.Nature reviews. Genetics · 2020Review
- Biological Functions of Prokaryotic Amyloids in Interspecies Interactions: Facts and Assumptions.International journal of molecular sciences · 2020Review
- Structure-Guided Designing and Evaluation of Peptides Targeting Bacterial Transcription.Frontiers in bioengineering and biotechnology · 2020Article
- Two Novel Amyloid Proteins, RopA and RopB, from the Root Nodule BacteriumBiomolecules · 2019Article
- Microbial functional amyloids serve diverse purposes for structure, adhesion and defence.Biophysical reviews · 2019Review
- Article
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Authors and funding
6 authors at 2 institutions in 4 countries.
Funding
Abstract
CarD is an essential global transcription regulator from Mycobacterium tuberculosis (Mtb) that binds RNA polymerase and activates transcription by stabilizing the transcription initiation complex. Available crystal structures have captured two distinct, monomeric and domain-swapped homodimeric, oligomeric states of CarD. However, the actual oligomeric state of CarD in solution and its biological relevance has remained unclear. Here, we confirm the presence of the homodimeric state of CarD in solution by using synchrotron-based small-angle X-ray scattering. Furthermore, by using biochemical and biophysical experiments, in addition to mass-spectrometry, transmission electron microscopy, and confocal imaging, we show that CarD is the first soluble cytosolic protein in Mtb which displays the tendency to form amyloid-like fibrils both in vitro as well as in vivo. We demonstrate that the deletion of the fourteen N-terminal residues involved in domain-swapping hampers amyloid formation, thus, suggesting that domain-swapping is crucial in amyloidogenesis. The discovery of the amyloidogenic property of an essential cytosolic global transcription regulator, CarD, in a pathogenic bacteria will further open up new frontiers in research.
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