Geibel, Sebastien and Waksman, Gabriel (2014) The molecular dissection of the Chaperone-Usher Pathway. Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 1843 (8), pp. 1559-1567. ISSN 0167-4889.
Abstract
Secretion systems are specialized in transport of proteins, DNA or nutrients across the cell envelope of bacteria and enable them to communicate with their environment. The chaperone-usher (CU) pathway is used for assembly and secretion of a large family of long adhesive protein polymers, termed pili, and is widespread among Gram-negative pathogens [1]. Moreover, recent evidence has indicated that CU secretion systems are also involved in sporulation [2] and [3]. In this review we focus on the structural biology of the paradigmatic type 1 and P pili CU systems encoded by uropathogenic Escherichia coli (UPEC), where recent progress has provided unprecedented insights into pilus assembly and secretion mechanism. This article is part of a Special Issue entitled:Protein trafficking & Secretion.
Metadata
| Item Type: | Article |
|---|---|
| Keyword(s) / Subject(s): | urinary tract infection, chaperone usher pathway, type I pilus, P pilus, adhesin, chaperone, usher, donor strand complementation, donor strand exchange |
| School: | Birkbeck Faculties and Schools > Faculty of Science > School of Natural Sciences |
| Research Centres and Institutes: | Structural Molecular Biology, Institute of (ISMB) |
| Depositing User: | Administrator |
| Date Deposited: | 16 Oct 2013 16:05 |
| Last Modified: | 02 Aug 2023 17:08 |
| URI: | https://eprints.bbk.ac.uk/id/eprint/8481 |
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