| Curli provide the template for understanding controlled amyloid propagation. | |
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MedLine Citation:
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PMID: 19098444 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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The uncontrolled formation of amyloid fibers is the hallmark of more than twenty human diseases. In contrast to disease-associated amyloids, which are the products of protein misfolding, E. coli assembles functional amyloid fibers called curli on its surface using an elegant biogenesis machine. Composed of a major subunit, CsgA, and a minor subunit, CsgB, curli play important roles in host cell adhesion, long-term survival and other bacterial community behaviors. Assembly of curli fibers is a template-directed conversion process where membrane-tethered CsgB initiates CsgA polymerization. The CsgA amyloid core is composed of five imperfect repeating units. In a series of in vivo and in vitro experiments, we determined the sequence and structural determinants that guide the initiation and propagation of CsgA polymers. The CsgA N- and C-terminal repeating units govern its polymerization and responsiveness to CsgB. Specifically, conserved glutamine and asparagine residues present in the CsgA N- and C-terminal repeating units are required for CsgB-mediated nucleation and efficient self-assembly. |
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Authors:
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Xuan Wang; Matthew R Chapman |
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Publication Detail:
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Type: Journal Article; Research Support, N.I.H., Extramural; Review Date: 2008-04-05 |
Journal Detail:
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Title: Prion Volume: 2 ISSN: 1933-690X ISO Abbreviation: Prion Publication Date: 2008 Apr-Jun |
Date Detail:
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Created Date: 2008-12-22 Completed Date: 2009-03-19 Revised Date: 2012-01-23 |
Medline Journal Info:
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Nlm Unique ID: 101472305 Medline TA: Prion Country: United States |
Other Details:
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Languages: eng Pagination: 57-60 Citation Subset: IM |
Affiliation:
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Department of Molecular, Cellular and Developmental Biology, University of Michigan, Ann Arbor, Michigan 48109, USA. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Amyloid
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genetics,
metabolism* Animals Bacterial Adhesion / physiology Bacterial Proteins / genetics, metabolism* Escherichia coli / genetics, metabolism* Escherichia coli Proteins / genetics, metabolism* Humans Protein Folding* Protein Structure, Quaternary / physiology Protein Structure, Tertiary / physiology |
| Grant Support | |
ID/Acronym/Agency:
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AI073847-01/AI/NIAID NIH HHS; R01 AI073847-02/AI/NIAID NIH HHS; R01 AI073847-03/AI/NIAID NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Amyloid; 0/Bacterial Proteins; 0/CsgB protein, E coli; 0/Escherichia coli Proteins; 0/csgA protein, E coli; 148349-72-8/Crl protein, Bacteria |
| Comments/Corrections | |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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