Nature communications, 2020-01, Vol.11 (1), p.241-241, Article 241
2020
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- Autor(en) / Beteiligte
- Titel
- Assembly and substrate recognition of curli biogenesis system
- Ist Teil von
- Nature communications, 2020-01, Vol.11 (1), p.241-241, Article 241
- Ort / Verlag
- London: Nature Publishing Group UK
- Erscheinungsjahr
- 2020
- Quelle
- MEDLINE
- Beschreibungen/Notizen
- A major component of bacterial biofilms is curli amyloid fibrils secreted by the curli biogenesis system. Understanding the curli biogenesis mechanism is critical for developing therapeutic agents for biofilm-related infections. Here we report a systematic study of the curli biogenesis system, highlighted by structural, biochemical and functional analysis of the secretion channel complexes (CsgF-CsgG) with and without the curli substrate. The dual-pore architecture of the CsgF-CsgG complex was observed and used to develop an approach to inhibit the curli secretion by physically reducing the size of the CsgF pore. We further elucidated the assembly of the CsgFG complex with curli components (CsgA and CsgB) and curli-cell association through CsgF. Importantly, the recognition of the CsgA substrate by CsgG was uncovered. Nine crevices outside of the CsgG channel provide specific and highly-conserved recognition sites for CsgA N-terminus. Together with analysis of CsgE, our study provides comprehensive insights into curli biogenesis. A major component of bacterial biofilms is curli amyloid fibrils secreted by the curli biogenesis system. Here authors use cryo-EM to visualize the secretion channel complexes (CsgF-CsgG) with and without the curli substrate and provide insights into curli biogenesis.
- Sprache
- Englisch
- Identifikatoren
- ISSN: 2041-1723eISSN: 2041-1723DOI: 10.1038/s41467-019-14145-7Titel-ID: cdi_doaj_primary_oai_doaj_org_article_19f841225ae740398e4682f0391a5534
- Format
- –
- Schlagworte
- 101/28, 631/326/41/2180, 631/326/46, 631/535/1258/1259, 631/57, Amyloid - antagonists & inhibitors, Amyloid - metabolism, Assembly, Bacterial Secretion Systems - chemistry, Bacterial Secretion Systems - metabolism, Binding Sites, Biofilms, Biosynthesis, Chemical compounds, Cryoelectron Microscopy, Escherichia coli K12 - drug effects, Escherichia coli K12 - metabolism, Escherichia coli Proteins - antagonists & inhibitors, Escherichia coli Proteins - metabolism, Fibrils, Functional analysis, Humanities and Social Sciences, Models, Molecular, multidisciplinary, Mutation, N-Terminus, Peptides - pharmacology, Pharmacology, Protein Binding, Protein Conformation, Protein Multimerization, Recognition, Science, Science (multidisciplinary), Secretion, Structure-function relationships, Substrates