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GroEL‐Mediated protein folding

Authors

Wayne A. Fenton, Arthur L. Horwich

Abstract

  • I
    Architecture of GroEL and GroES and the reaction pathway
    • A.
      Architecture of the chaperonins
    • B.
      Reaction pathway of GroEL‐GroES‐mediated folding
  • II.
    Polypeptide binding
    • A.
      A parallel network of chaperones binding polypeptides in vivo
    • B.
      Polypeptide binding in vitro
      • 1.
        Role of hydrophobicity in recognition
      • 2.
        Homologous proteins with differing recognition—differences in primary structure versus effects on folding pathway
      • 3.
        Conformations recognized by GroEL
        • a.
          Refolding studies
        • b.
          Binding of metastable intermediates
        • c.
          Conformations while stably bound at GroEL
      • 4.
        Binding constants and rates of association
      • 5.
        Conformational changes in the substrate protein associated with binding by GroEL
        • a.
          Observations
        • b.
          Kinetic versus thermodynamic action of GroEL in mediating unfolding
        • c.
          Crossing the energy landscape in the presence of GroEL
  • III.
    ATP binding and hydrolysis—driving the reaction cycle
  • IV.
    GroEL‐GroES‐polypeptide ternary complexes—the folding‐active cis complex
    • A.
      Cis and trans ternary complexes
    • B.
      Symmetric complexes
    • C.
      The folding‐active intermediate of a chaperonin reaction—cis ternary complex
    • D.
      The role of the cis space in the folding reaction
    • E.
      Folding governed by a “timer” mechanism
    • F.
      Release of nonnative polypeptides during the GroEL‐GroES reaction
    • G.
      Release of both native and nonnative forms under physiologic conditions
    • H.
      A role for ATP binding, as well as hydrolysis, in the folding cycle
  • V.
    Concluding remarks

Digital Object Identifier (DOI)

10.1002/pro.5560060401 About DOI

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