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Atypical protein disulfide isomerases (PDI): Comparison of the molecular and catalytic properties of poplar PDI-A and PDI-M with PDI-L1A

Protein disulfide isomerases are overwhelmingly multi-modular redox catalysts able to perform the formation, reduction or isomerisation of disulfide bonds. We present here the biochemical characterization of three different poplar PDI isoforms. PDI-A is characterized by a single catalytic Trx module... Full description

Journal Title: PLoS One Mar 2017, Vol.12(3), p.e0174753
Main Author: Selles, Benjamin
Other Authors: Zannini, Flavien , Couturier, Jérémy , Jacquot, Jean-Pierre , Rouhier, Nicolas
Format: Electronic Article Electronic Article
Language: English
Subjects:
Ph
ID: E-ISSN: 19326203 ; DOI: 10.1371/journal.pone.0174753
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title: Atypical protein disulfide isomerases (PDI): Comparison of the molecular and catalytic properties of poplar PDI-A and PDI-M with PDI-L1A
format: Article
creator:
  • Selles, Benjamin
  • Zannini, Flavien
  • Couturier, Jérémy
  • Jacquot, Jean-Pierre
  • Rouhier, Nicolas
subjects:
  • Physiology
  • Insulin
  • Thioredoxin
  • Protein Folding
  • Endoplasmic Reticulum
  • Nadp
  • Substrates
  • Catalysts
  • Oxidation
  • Isoforms
  • Ph
  • Amino Acids
  • Ribonuclease A
  • E Coli
  • Chromatography
  • Disulfide Bonds
  • Malate Dehydrogenase
  • Oxidation
  • Mutagenesis
  • Oxidation
ispartof: PLoS One, Mar 2017, Vol.12(3), p.e0174753
description: Protein disulfide isomerases are overwhelmingly multi-modular redox catalysts able to perform the formation, reduction or isomerisation of disulfide bonds. We present here the biochemical characterization of three different poplar PDI isoforms. PDI-A is characterized by a single catalytic Trx module, the so-called a domain, whereas PDI-L1a and PDI-M display an a-b-b’-a’ and a°-a-b organisation respectively. Their activities have been tested in vitro using purified recombinant proteins and a series of model substrates as insulin, NADPH thioredoxin reductase, NADP malate dehydrogenase (NADP-MDH), peroxiredoxins or RNase A. We demonstrated that PDI-A exhibited none of the usually reported activities, although the cysteines of the WCKHC active site signature are able to form a disulfide with a redox midpoint potential of -170 mV at pH 7.0. The fact that it is able to bind a [Fe2S2] cluster upon Escherichia coli expression and anaerobic purification might indicate that it does not have a function...
language: eng
source:
identifier: E-ISSN: 19326203 ; DOI: 10.1371/journal.pone.0174753
fulltext: fulltext_linktorsrc
issn:
  • 19326203
  • 1932-6203
url: Link


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titleAtypical protein disulfide isomerases (PDI): Comparison of the molecular and catalytic properties of poplar PDI-A and PDI-M with PDI-L1A
creatorSelles, Benjamin ; Zannini, Flavien ; Couturier, Jérémy ; Jacquot, Jean-Pierre ; Rouhier, Nicolas
ispartofPLoS One, Mar 2017, Vol.12(3), p.e0174753
identifierE-ISSN: 19326203 ; DOI: 10.1371/journal.pone.0174753
subjectPhysiology ; Insulin ; Thioredoxin ; Protein Folding ; Endoplasmic Reticulum ; Nadp ; Substrates ; Catalysts ; Oxidation ; Isoforms ; Ph ; Amino Acids ; Ribonuclease A ; E Coli ; Chromatography ; Disulfide Bonds ; Malate Dehydrogenase ; Oxidation ; Mutagenesis ; Oxidation
descriptionProtein disulfide isomerases are overwhelmingly multi-modular redox catalysts able to perform the formation, reduction or isomerisation of disulfide bonds. We present here the biochemical characterization of three different poplar PDI isoforms. PDI-A is characterized by a single catalytic Trx module, the so-called a domain, whereas PDI-L1a and PDI-M display an a-b-b’-a’ and a°-a-b organisation respectively. Their activities have been tested in vitro using purified recombinant proteins and a series of model substrates as insulin, NADPH thioredoxin reductase, NADP malate dehydrogenase (NADP-MDH), peroxiredoxins or RNase A. We demonstrated that PDI-A exhibited none of the usually reported activities, although the cysteines of the WCKHC active site signature are able to form a disulfide with a redox midpoint potential of -170 mV at pH 7.0. The fact that it is able to bind a [Fe2S2] cluster upon Escherichia coli expression and anaerobic purification might indicate that it does not have a function...
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titleAtypical protein disulfide isomerases (PDI): Comparison of the molecular and catalytic properties of poplar PDI-A and PDI-M with PDI-L1A
descriptionProtein disulfide isomerases are overwhelmingly multi-modular redox catalysts able to perform the formation, reduction or isomerisation of disulfide bonds. We present here the biochemical characterization of three different poplar PDI isoforms. PDI-A is characterized by a single catalytic Trx module, the so-called a domain, whereas PDI-L1a and PDI-M display an a-b-b’-a’ and a°-a-b organisation respectively. Their activities have been tested in vitro using purified recombinant proteins and a series of model substrates as insulin, NADPH thioredoxin reductase, NADP malate dehydrogenase (NADP-MDH), peroxiredoxins or RNase A. We demonstrated that PDI-A exhibited none of the usually reported activities, although the cysteines of the WCKHC active site signature are able to form a disulfide with a redox midpoint potential of -170 mV at pH 7.0. The fact that it is able to bind a [Fe2S2] cluster upon Escherichia coli expression and anaerobic purification might indicate that it does not have a function...
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titleAtypical protein disulfide isomerases (PDI): Comparison of the molecular and catalytic properties of poplar PDI-A and PDI-M with PDI-L1A
authorSelles, Benjamin ; Zannini, Flavien ; Couturier, Jérémy ; Jacquot, Jean-Pierre ; Rouhier, Nicolas
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5Nadp
6Substrates
7Catalysts
8Oxidation
9Isoforms
10Ph
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abstractProtein disulfide isomerases are overwhelmingly multi-modular redox catalysts able to perform the formation, reduction or isomerisation of disulfide bonds. We present here the biochemical characterization of three different poplar PDI isoforms. PDI-A is characterized by a single catalytic Trx module, the so-called a domain, whereas PDI-L1a and PDI-M display an a-b-b’-a’ and a°-a-b organisation respectively. Their activities have been tested in vitro using purified recombinant proteins and a series of model substrates as insulin, NADPH thioredoxin reductase, NADP malate dehydrogenase (NADP-MDH), peroxiredoxins or RNase A. We demonstrated that PDI-A exhibited none of the usually reported activities, although the cysteines of the WCKHC active site signature are able to form a disulfide with a redox midpoint potential of -170 mV at pH 7.0. The fact that it is able to bind a [Fe2S2] cluster upon Escherichia coli expression and anaerobic purification might indicate that it does not have a function...
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