The curli nucleator protein, CsgB, contains an amyloidogenic domain that directs CsgA polymerization.

The curli nucleator protein, CsgB, contains an amyloidogenic domain that directs CsgA polymerization. Research Abstract Details 

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The curli nucleator protein, CsgB, contains an amyloidogenic domain that directs CsgA polymerization. Abstract Text:

Neal D Hammer,Jens C Schmidt,Matthew R Chapman,

Curli are functional amyloid fibers assembled by enteric bacteria such as Escherichia coli and Salmonella spp. In E. coli, the polymerization of the major curli fiber subunit protein CsgA into an amyloid fiber depends on the minor curli subunit protein, CsgB. The outer membrane-localized CsgB protein shares approximately 30% sequence identity with the amyloid-forming protein CsgA, suggesting that CsgB might also have amyloidogenic properties. Here, we characterized the biochemical properties of CsgB and the molecular basis for CsgB-mediated nucleation of CsgA. Deletion analysis revealed that a CsgB molecule missing 19 amino acids from its C terminus (CsgB(trunc)) was not outer membrane-associated, but secreted away from the cell. CsgB(trunc) was overexpressed and purified from the extracellular milieu of cells as an SDS-soluble, nonaggregated protein. Soluble CsgB(trunc) assembled into fibers that bound to the amyloid-specific dyes Congo red and thioflavin-T. CsgB(trunc) fibers were able to seed soluble CsgA polymerization in vitro. CsgB(trunc) displayed modest nucleator activity in vivo, as demonstrated by its ability to convert extracellular CsgA into an amyloid fiber. Unlike WT CsgB, CsgB(trunc) was only able to act as a nucleator when cells were genetically manipulated to secrete higher concentrations of CsgA. This work represents a unique demonstration of functional amyloid nucleation and it suggests an elegant model for how E. coli guides efficient amyloid fiber formation on the cell surface.

The curli nucleator protein, CsgB, contains an amyloidogenic domain that directs CsgA polymerization. Publishing Authors By Initials

ND Hammer,JC Schmidt,MR Chapman,

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The curli nucleator protein, CsgB, contains an amyloidogenic domain that directs CsgA polymerization. Journal Published:

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

Journal: Proceedings of the National Academy of Sciences of

VOLUME: 104

Page Numbers: 12494-9

Journal Abbreviation: Proc. Natl. Acad. Sci. U.S.A.

ISSN: 0027-8424

DAY: 16

MONTH: 07

YEAR: 2007

The curli nucleator protein, CsgB, contains an amyloidogenic domain that directs CsgA polymerization. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 7505876

The curli nucleator protein, CsgB, contains an amyloidogenic domain that directs CsgA polymerization. Keywords Mesh Terms:

KEYWORDS: Molecular Sequence Data

MESH TERMS: ultrastructure

Chemical & Substance for Abstract: The curli nucleator protein, CsgB, contains an amyloidogenic domain that directs CsgA polymerization. Information

Substance Name: Crl protein, Bacteria

Registry Number: 148349-72-8

Grant and Affiliation Information for The curli nucleator protein, CsgB, contains an amyloidogenic domain that directs CsgA polymerization.

AFFILIATION: Department of Molecular, Cellular, and Developmental Biology, University of Michigan College of Literature, Science, and the Arts, 830 North University, Ann Arbor, MI 48109-0620, USA.

Country: United States

AGENCY: United States PHS

GRANT: P50-A608671

ACRONYM: AI

MEDLINETA: Proc Natl Acad Sci U S A

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