Mol Microbiol. 2001 Jan;39(1):199-210.

Chaperone function of FkpA, a heat shock prolyl isomerase, in the periplasm of Escherichia coli.

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Unité de Programmation Moléculaire et de Toxicologie Génétique/CNRS-URA1444, Institut Pasteur, 25 rue du Docteur Roux, 75015 Paris, France.

Abstract

The nature of molecular chaperones in the periplasm of Escherichia coli that assist newly translocated proteins to reach their native state has remained poorly defined. Here, we show that FkpA, a heat shock periplasmic peptidyl-prolyl cis/trans isomerase (PPIase), suppresses the formation of inclusion bodies from a defective-folding variant of the maltose-binding protein, MalE31. This chaperone-like activity of FkpA, which is independent of its PPIase activity, requires a full-length structure of the protein. In vitro, FkpA does not catalyse a slow rate-limiting step in the refolding of MalE31, but prevents its aggregation at stoichiometric amounts and promotes the reactivation of denaturated citrate synthase. We propose that FkpA functions as a chaperone for envelope proteins in the bacterial periplasm.

PMID:: 11123702; [PubMed - indexed for MEDLINE]

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Structural and functional studies of FkpA from Escherichia coli, a cis/trans peptidyl-prolyl isomerase with chaperone activity. [J Mol Biol. 2004]
Structural and functional studies of FkpA from Escherichia coli, a cis/trans peptidyl-prolyl isomerase with chaperone activity.
Saul FA, Arié JP, Vulliez-le Normand B, Kahn R, Betton JM, Bentley GA. J Mol Biol. 2004 Jan 9; 335(2):595-608.
High enzymatic activity and chaperone function are mechanistically related features of the dimeric E. coli peptidyl-prolyl-isomerase FkpA. [J Mol Biol. 2001]
High enzymatic activity and chaperone function are mechanistically related features of the dimeric E. coli peptidyl-prolyl-isomerase FkpA.
Ramm K, Plückthun A. J Mol Biol. 2001 Jul 6; 310(2):485-98.
The periplasmic Escherichia coli peptidylprolyl cis,trans-isomerase FkpA. II. Isomerase-independent chaperone activity in vitro. [J Biol Chem. 2000]
The periplasmic Escherichia coli peptidylprolyl cis,trans-isomerase FkpA. II. Isomerase-independent chaperone activity in vitro.
Ramm K, Plückthun A. J Biol Chem. 2000 Jun 2; 275(22):17106-13.
Review [Transport of outer membrane proteins]. [Tanpakushitsu Kakusan Koso. 2004]
Review [Transport of outer membrane proteins].
Matsuyama S, Tokuda H. Tanpakushitsu Kakusan Koso. 2004 May; 49(7 Suppl):965-6.
Review Microbial molecular chaperones. [Adv Microb Physiol. 2001]
Review Microbial molecular chaperones.
Lund PA. Adv Microb Physiol. 2001; 44:93-140.

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Trémillon N, Morello E, Llull D, Mazmouz R, Gratadoux JJ, Guillot A, Chapot-Chartier MP, Monlezun L, Solé V, Ginisty H, et al. PLoS One. 2012; 7(3):e33516. Epub 2012 Mar 19.
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Leiser OP, Charlson ES, Gerken H, Misra R. PLoS One. 2012; 7(3):e33979. Epub 2012 Mar 16.
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