In vitro polymerization of a functional Escherichia coli amyloid protein.

In vitro polymerization of a functional Escherichia coli amyloid protein. Research Abstract Details 

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In vitro polymerization of a functional Escherichia coli amyloid protein. Abstract Text:

Xuan Wang,Daniel R Smith,Jonathan W Jones,Matthew R Chapman,

Amyloid formation is characterized by the conversion of soluble proteins into biochemically and structurally distinct fibers. Although amyloid formation is traditionally associated with diseases such as Alzheimer disease, a number of biologically functional amyloids have recently been described. Curli are amyloid fibers produced by Escherichia coli that contribute to biofilm formation and other important physiological processes. We characterized the polymerization properties of the major curli subunit protein CsgA. CsgA polymerizes into an amyloid fiber in a sigmoidal kinetic fashion with a distinct lag, growth, and stationary phase. Adding sonicated preformed CsgA fibers to the polymerization reaction can significantly shorten the duration of the lag phase. We also demonstrate that the conversion of soluble CsgA into an insoluble fiber involves the transient formation of an intermediate similar to that characterized for several disease-associated amyloids. The CsgA core amyloid domain can be divided into five repeating units that share sequence and structural hallmarks. We show that peptides representing three of these repeating units are amyloidogenic in vitro. Although the defining characteristics of CsgA polymerization appear conserved with disease-associated amyloids, these proteins evolved in diverse systems and for different purposes. Therefore, amyloidogenesis appears to be an innate protein folding pathway that can be capitalized on to fulfill normal physiological tasks.

In vitro polymerization of a functional Escherichia coli amyloid protein. Publishing Authors By Initials

X Wang,DR Smith,JW Jones,MR Chapman,

For similar serum amyloid a protein research abstracts see: serum amyloid a protein research

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In vitro polymerization of a functional Escherichia coli amyloid protein. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: The Journal of biological chemistry

VOLUME: 282

Page Numbers: 3713-9

Journal Abbreviation: J. Biol. Chem.

ISSN: 0021-9258

DAY: 12

MONTH: 12

YEAR: 2006

In vitro polymerization of a functional Escherichia coli amyloid protein. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 2985121

In vitro polymerization of a functional Escherichia coli amyloid protein. Keywords Mesh Terms:

KEYWORDS: Serum Amyloid A Protein

MESH TERMS: ultrastructure

Chemical & Substance for Abstract: In vitro polymerization of a functional Escherichia coli amyloid protein. Information

Substance Name: Crl protein, Bacteria

Registry Number: 148349-72-8

Grant and Affiliation Information for In vitro polymerization of a functional Escherichia coli amyloid protein.

AFFILIATION: Department of Molecular, Cellular and Developmental Biology, University of Michigan, Ann Arbor, Michigan 48109, USA.

Country: United States

AGENCY: United States PHS

GRANT: P50-A608671

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MEDLINETA: J Biol Chem

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