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Chapter 8 : Periplasmic Chaperones and Peptidyl-Prolyl Isomerases

Author: Betton Jean-Michel1
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Affiliations: 1: Unite de Repliement et Modelisation des Proteines, Institut Pasteur—CNRS URA2185, 75724 Paris cedex 15, France
Content Type: Monograph
Publication Year: 2007

Category: Bacterial Pathogenesis; Microbial Genetics and Molecular Biology

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Periplasmic Chaperones and Peptidyl-Prolyl Isomerases, Page 1 of 2

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Abstract:

The cellular functions of molecular chaperones include protecting newly synthesized polypeptides from misfolding or aggregation, and promoting disaggregation and refolding of stress-denaturated proteins. It was debated whether periplasmic chaperones might exist that could associate with newly exported polypeptides emerging at the translocation sites to assist their folding process, as cytoplasmic chaperones do with newly synthesized polypeptides emerging from the ribosomes. Many molecular chaperones, evolutionarily conserved from humans to bacteria, were initially identified because they are induced in response to stress conditions leading to the accumulation of intracellular nonnative proteins. Although not historically classified as molecular chaperones, enzymes that catalyze two potentially rate-limiting folding reactions, or folding catalysts, are abundant in the periplasm. Two different global searches for periplasmic chaperones suggested an important role of Skp in the folding pathway of outer membrane proteins. First, Skp was retained on an affinity column with Sepharose-bound OmpF, and second, by genetic screening, mutations in the gene were isolated based on their increased σactivity. Peptidyl-prolyl isomerases (PPIases) are ubiquitous and highly conserved enzymes that catalyze prolyl isomerization, an intrinsically slow and potentially rate-limiting reaction during in vitro protein refolding. In addition to protein disulfide isomerases and proteases, the periplasm contains at least five distinct protein-folding factors, including the nonessential molecular chaperone Skp, and four PPIases (Pipe, FepA, Sure, and Paid) that are individually, but not collectively, dispensable for viability in .

Citation: Jean-Michel B. 2007. Periplasmic Chaperones and Peptidyl-Prolyl Isomerases, p 141-149. In Ehrmann M (ed), The Periplasm. ASM Press, Washington, DC. doi: 10.1128/9781555815806.ch8

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Outer Membrane Proteins
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Integral Membrane Proteins
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Tables

Periplasmic Chaperones and Peptidyl-Prolyl Isomerases
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Citation: Jean-Michel B. 2007. Periplasmic Chaperones and Peptidyl-Prolyl Isomerases, p 141-149. In Ehrmann M (ed), The Periplasm. ASM Press, Washington, DC. doi: 10.1128/9781555815806.ch8
/content/10.1128/9781555815806.ch08.ch08tab01
TABLE 1
Periplasmic chaperones and peptidyl-prolyl isomerases
Generic image for table
TABLE 1

Periplasmic chaperones and peptidyl-prolyl isomerases

Citation: Jean-Michel B. 2007. Periplasmic Chaperones and Peptidyl-Prolyl Isomerases, p 141-149. In Ehrmann M (ed), The Periplasm. ASM Press, Washington, DC. doi: 10.1128/9781555815806.ch8

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