PhanerochaeteV1, Main, Exploration, bibRecord, 000392

Atypical features of a Ure2p glutathione transferase from Phanerochaete chrysosporium.

Identifieur interne : 000392 ( Main/Exploration ); précédent : 000391; suivant : 000393

Atypical features of a Ure2p glutathione transferase from Phanerochaete chrysosporium.

Auteurs : Anne Thuillier [France] ; Thomas Roret ; Frédérique Favier ; Eric Gelhaye ; Jean-Pierre Jacquot ; Claude Didierjean ; Mélanie Morel-Rouhier

Source :

FEBS letters [ 1873-3468 ] ; 2013.

RBID : pubmed:23711374

Descripteurs français

English descriptors

KwdEn :
- Crystallography, X-Ray (MeSH), Dithiothreitol (chemistry), Fungal Proteins (chemistry), Glutathione (chemistry), Glutathione Transferase (chemistry), Hydrogen Bonding (MeSH), Insulin (chemistry), Kinetics (MeSH), Models, Molecular (MeSH), Oxidation-Reduction (MeSH), Phanerochaete (enzymology), Protein Binding (MeSH), Protein Structure, Secondary (MeSH), Reducing Agents (chemistry).
MESH :
- chemical , chemistry : Dithiothreitol, Fungal Proteins, Glutathione, Glutathione Transferase, Insulin, Reducing Agents.
- enzymology : Phanerochaete.
- Crystallography, X-Ray, Hydrogen Bonding, Kinetics, Models, Molecular, Oxidation-Reduction, Protein Binding, Protein Structure, Secondary.

Abstract

Glutathione transferases (GSTs) are known to transfer glutathione onto small hydrophobic molecules in detoxification reactions. The GST Ure2pB1 from Phanerochaete chrysosporium exhibits atypical features, i.e. the presence of two glutathione binding sites and a high affinity towards oxidized glutathione. Moreover, PcUre2pB1 is able to efficiently deglutathionylate GS-phenacylacetophenone. Catalysis is not mediated by the cysteines of the protein but rather by the one of glutathione and an asparagine residue plays a key role in glutathione stabilization. Interestingly PcUre2pB1 interacts in vitro with a GST of the omega class. These properties are discussed in the physiological context of wood degrading fungi.

DOI: 10.1016/j.febslet.2013.05.031
PubMed: 23711374

Affiliations:

Links toward previous steps (curation, corpus...)

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Le document en format XML

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<author><name sortKey="Morel Rouhier, Melanie" sort="Morel Rouhier, Melanie" uniqKey="Morel Rouhier M" first="Mélanie" last="Morel-Rouhier">Mélanie Morel-Rouhier</name>
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<author><name sortKey="Morel Rouhier, Melanie" sort="Morel Rouhier, Melanie" uniqKey="Morel Rouhier M" first="Mélanie" last="Morel-Rouhier">Mélanie Morel-Rouhier</name>
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<term>Dithiothreitol (chemistry)</term>
<term>Fungal Proteins (chemistry)</term>
<term>Glutathione (chemistry)</term>
<term>Glutathione Transferase (chemistry)</term>
<term>Hydrogen Bonding (MeSH)</term>
<term>Insulin (chemistry)</term>
<term>Kinetics (MeSH)</term>
<term>Models, Molecular (MeSH)</term>
<term>Oxidation-Reduction (MeSH)</term>
<term>Phanerochaete (enzymology)</term>
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<term>Glutathion (composition chimique)</term>
<term>Glutathione transferase (composition chimique)</term>
<term>Insuline (composition chimique)</term>
<term>Liaison aux protéines (MeSH)</term>
<term>Liaison hydrogène (MeSH)</term>
<term>Modèles moléculaires (MeSH)</term>
<term>Oxydoréduction (MeSH)</term>
<term>Phanerochaete (enzymologie)</term>
<term>Protéines fongiques (composition chimique)</term>
<term>Réducteurs (composition chimique)</term>
<term>Structure secondaire des protéines (MeSH)</term>
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<term>Glutathione</term>
<term>Glutathione Transferase</term>
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<term>Reducing Agents</term>
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<term>Oxidation-Reduction</term>
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<term>Protein Structure, Secondary</term>
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<term>Cristallographie aux rayons X</term>
<term>Liaison aux protéines</term>
<term>Liaison hydrogène</term>
<term>Modèles moléculaires</term>
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<front><div type="abstract" xml:lang="en">Glutathione transferases (GSTs) are known to transfer glutathione onto small hydrophobic molecules in detoxification reactions. The GST Ure2pB1 from Phanerochaete chrysosporium exhibits atypical features, i.e. the presence of two glutathione binding sites and a high affinity towards oxidized glutathione. Moreover, PcUre2pB1 is able to efficiently deglutathionylate GS-phenacylacetophenone. Catalysis is not mediated by the cysteines of the protein but rather by the one of glutathione and an asparagine residue plays a key role in glutathione stabilization. Interestingly PcUre2pB1 interacts in vitro with a GST of the omega class. These properties are discussed in the physiological context of wood degrading fungi.</div>
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Atypical features of a Ure2p glutathione transferase from Phanerochaete chrysosporium.

Atypical features of a Ure2p glutathione transferase from Phanerochaete chrysosporium.

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English descriptors

Abstract

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