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EcoSal Plus

Domain 5:

Responding to the Environment

Periplasmic Chaperones and Prolyl Isomerases

MyBook is a cheap paperback edition of the original book and will be sold at uniform, low price.
  • Authors: Frederick Stull1, Jean-Michel Betton2, and James C.A. Bardwell3
  • Editors: James M. Slauch4, Michael Ehrmann5
    Affiliations: 1: Dept of Molecular Cellular and Developmental Biology, Howard Hughes Medical Institute, University of Michigan, Ann Arbor, MI 48109; 2: Unité de Repliement et Modélisation des Protéines, Institut Pasteur–CNRS URA2185, 75724 Paris cedex 15, France; 3: Dept of Molecular Cellular and Developmental Biology, Howard Hughes Medical Institute, University of Michigan, Ann Arbor, MI 48109; 4: The School of Molecular and Cellular Biology, University of Illinois at Urbana-Champaign, Urbana, IL; 5: Center for Medical Biotechnology (ZMB), University of Duisburg-Essen, Essen, Germany
  • Received 05 March 2018 Accepted 30 April 2018 Published 03 July 2018
  • Address correspondence to James C.A. Bardwell, [email protected]
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  • Abstract:

    The biogenesis of periplasmic and outer membrane proteins (OMPs) in is assisted by a variety of processes that help with their folding and transport to their final destination in the cellular envelope. Chaperones are macromolecules, usually proteins, that facilitate the folding of proteins or prevent their aggregation without becoming part of the protein’s final structure. Because chaperones often bind to folding intermediates, they often (but not always) act to slow protein folding. Protein folding catalysts, on the other hand, act to accelerate specific steps in the protein folding pathway, including disulfide bond formation and peptidyl prolyl isomerization. This review is primarily concerned with and periplasmic and cellular envelope chaperones; it also discusses periplasmic proline isomerization.

  • Citation: Stull F, Betton J, Bardwell J. 2018. Periplasmic Chaperones and Prolyl Isomerases, EcoSal Plus 2018; doi:10.1128/ecosalplus.ESP-0005-2018


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The biogenesis of periplasmic and outer membrane proteins (OMPs) in is assisted by a variety of processes that help with their folding and transport to their final destination in the cellular envelope. Chaperones are macromolecules, usually proteins, that facilitate the folding of proteins or prevent their aggregation without becoming part of the protein’s final structure. Because chaperones often bind to folding intermediates, they often (but not always) act to slow protein folding. Protein folding catalysts, on the other hand, act to accelerate specific steps in the protein folding pathway, including disulfide bond formation and peptidyl prolyl isomerization. This review is primarily concerned with and periplasmic and cellular envelope chaperones; it also discusses periplasmic proline isomerization.

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Image of Figure 1
Figure 1

An overview of the chaperones and folding factors affecting protein folding in the periplasm of .

Citation: Stull F, Betton J, Bardwell J. 2018. Periplasmic Chaperones and Prolyl Isomerases, EcoSal Plus 2018; doi:10.1128/ecosalplus.ESP-0005-2018
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