Document Detail

Curli provide the template for understanding controlled amyloid propagation.
MedLine Citation:
PMID:  19098444     Owner:  NLM     Status:  MEDLINE    
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.
Xuan Wang; Matthew R Chapman
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Review     Date:  2008-04-05
Journal Detail:
Title:  Prion     Volume:  2     ISSN:  1933-690X     ISO Abbreviation:  Prion     Publication Date:    2008 Apr-Jun
Date Detail:
Created Date:  2008-12-22     Completed Date:  2009-03-19     Revised Date:  2014-09-11    
Medline Journal Info:
Nlm Unique ID:  101472305     Medline TA:  Prion     Country:  United States    
Other Details:
Languages:  eng     Pagination:  57-60     Citation Subset:  IM    
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MeSH Terms
Amyloid / genetics,  metabolism*
Bacterial Adhesion / physiology
Bacterial Proteins / genetics,  metabolism*
Escherichia coli / genetics,  metabolism*
Escherichia coli Proteins / genetics,  metabolism*
Protein Folding*
Protein Structure, Quaternary / physiology
Protein Structure, Tertiary / physiology
Grant Support
Reg. No./Substance:
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

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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