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Identification of NLR-associated amyloid signaling motifs in bacterial genomes
- Source :
- Journal of Molecular Biology, Journal of Molecular Biology, Elsevier, 2020, 432, pp.6005-6027. ⟨10.1016/j.jmb.2020.10.004⟩, Journal of Molecular Biology, 2020, 432, pp.6005-6027. ⟨10.1016/j.jmb.2020.10.004⟩
- Publication Year :
- 2020
- Publisher :
- HAL CCSD, 2020.
-
Abstract
- International audience; In filamentous fungi, amyloid signaling sequences allow Nod-like receptors (NLRs) to activate downstream cell-death inducing proteins with HeLo and HeLo-like (HELL) domains and amyloid RHIM and RHIM-related motifs control immune defense pathways in mammals and flies. Herein, we show bioinformatically that analogous amyloid signaling motifs exist in bacteria. These short motifs are found at the N-terminus of NLRs and at the C-terminus of proteins with a domain we term BELL. The corresponding NLR and BELL proteins are encoded by adjacent genes. We identify 10 families of such bacterial amyloid signaling sequences (BASS), one of which (BASS3) is homologous to RHIM and a fungal amyloid motif termed PP. BASS motifs occur nearly exclusively in bacteria forming multicellular structures (mainly in Actinobacteria and Cyanobacteria). We analyze experimentally a subset of seven of these motifs (from the most common BASS1 family and the RHIM-related BASS3 family) and find that these sequences form fibrils in vitro. Using a fungal in vivo model, we show that all tested BASS-motifs form prions and that the NLR-side motifs seed prion-formation of the corresponding BELL-side motif. We find that BASS3 motifs show partial prion cross-seeding with mammalian RHIM and fungal PP-motifs and that proline mutations on key positions of the BASS3 core motif, conserved in RHIM and PP-motifs, abolish prion formation. This work expands the paradigm of prion amyloid signaling to multicellular prokaryotes and suggests a long-term evolutionary conservation of these motifs from bacteria, to fungi and animals.
- Subjects :
- Amyloid
Prions
[SDV]Life Sciences [q-bio]
Amino Acid Motifs
Amyloidogenic Proteins
NLR Proteins
Bacterial genome size
Cyanobacteria
Conserved sequence
Evolution, Molecular
03 medical and health sciences
0302 clinical medicine
Structural Biology
Animals
Amino Acid Sequence
Molecular Biology
Gene
030304 developmental biology
Genetics
0303 health sciences
biology
C-terminus
Fungi
biology.organism_classification
Immunity, Innate
N-terminus
[SDV] Life Sciences [q-bio]
Multicellular organism
Drosophila
Signal transduction
Genome, Bacterial
030217 neurology & neurosurgery
Bacteria
Signal Transduction
Subjects
Details
- Language :
- English
- ISSN :
- 00222836 and 10898638
- Database :
- OpenAIRE
- Journal :
- Journal of Molecular Biology, Journal of Molecular Biology, Elsevier, 2020, 432, pp.6005-6027. ⟨10.1016/j.jmb.2020.10.004⟩, Journal of Molecular Biology, 2020, 432, pp.6005-6027. ⟨10.1016/j.jmb.2020.10.004⟩
- Accession number :
- edsair.doi.dedup.....4e5ca9f9a7cd48b8e1fc9611c8a4660f