期刊
SCIENCE
卷 295, 期 5556, 页码 851-855出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1067484
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资金
- NIAID NIH HHS [R01 AI029549, 1 F32 AI10502-01A1, R37 AI029549, F32 AI010502, F32 AI010502-03, AI29549, R01 AI048689, AI48689] Funding Source: Medline
- NIA NIH HHS [NIA P50 AG05681-17, P50 AG005681] Funding Source: Medline
- NIDDK NIH HHS [R01 DK051406, DK51406] Funding Source: Medline
Amyloid is associated with debilitating human ailments including Alzheimer's and prion diseases. Biochemical, biophysical, and imaging analyses revealed that fibers produced by Escherichia coli called curli were amyloid. The CsgA curlin subunit, purified in the absence of the CsgB nucleator, adopted a soluble, unstructured form that upon prolonged incubation assembled into fibers that were indistinguishable from curli. In vivo, curli biogenesis was dependent on the nucleation-precipitation machinery requiring the CsgE and CsgF chaperone-like and nucleator proteins, respectively. Unlike eukaryotic amyloid formation, curli biogenesis is a productive pathway, requiring a specific assembly machinery.
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