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Amyloidogenesis of bacterial prionoid RepA-WH1 recapitulates dimer to monomer transitions of RepA in DNA replication initiation.

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  • معلومة اضافية
    • Publisher Information:
      Nature Publishing Group 2015-01-06
    • نبذة مختصرة :
      Most available structures of amyloids correspond to peptide fragments that self-assemble in extended cross b sheets. However, structures in which a whole protein domain acts as building block of an amyloid fiber are scarce, in spite of their relevance to understand amyloidogenesis. Here, we use electron microscopy (EM) and atomic force microscopy (AFM) to analyze the structure of amyloid filaments assembled by RepA-WH1, a winged-helix domain from a DNA replication initiator in bacterial plasmids. RepA-WH1 functions as a cytotoxic bacterial prionoid that recapitulates features of mammalian amyloid proteinopathies. RepA are dimers that monomerize at the origin to initiate replication, and we find that RepA-WH1 reproduces this transition to form amyloids. RepA-WH1 assembles double helical filaments by lateral association of a singlestranded precursor built by monomers. Double filaments then associate in mature fibers. The intracellular and cytotoxic RepA-WH1 aggregates might reproduce the hierarchical assembly of human amyloidogenic proteins.
    • الموضوع:
      Amyloid protein; Bacterial proteins; DNA helicase; RepA WH1 protein; artículo
    • Availability:
      Open access content. Open access content
      openAccess
    • Note:
      English
    • Other Numbers:
      CTK oai:digital.csic.es:10261/121034
      Structure 23: 183–189 (2015)
      10.1016/j.str.2014.11.007
      0969-2126
      1104776025
    • Contributing Source:
      CSIC
      From OAIster®, provided by the OCLC Cooperative.
    • الرقم المعرف:
      edsoai.on1104776025
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