Structural and enzymatic insights into Lambda glutathione transferases from Populus trichocarpa, monomeric enzymes constituting an early divergent class specific to terrestrial plants.
Identifieur interne : 002038 ( Main/Exploration ); précédent : 002037; suivant : 002039Structural and enzymatic insights into Lambda glutathione transferases from Populus trichocarpa, monomeric enzymes constituting an early divergent class specific to terrestrial plants.
Auteurs : Pierre-Alexandre Lallement ; Edgar Meux ; José M. Gualberto [France] ; Pascalita Prosper ; Claude Didierjean ; Frederick Saul [France] ; Ahmed Haouz [France] ; Nicolas Rouhier ; Arnaud HeckerSource :
- The Biochemical journal [ 1470-8728 ] ; 2014.
Descripteurs français
- KwdFr :
- Cinétique (MeSH), Cristallographie aux rayons X (MeSH), Cytoplasme (enzymologie), Glutathion (analogues et dérivés), Glutathion (métabolisme), Glutathione transferase (composition chimique), Glutathione transferase (métabolisme), Gènes de plante (MeSH), Multimérisation de protéines (MeSH), Noyau de la cellule (enzymologie), Pliage des protéines (MeSH), Populus (enzymologie), Populus (génétique), Spécificité du substrat (MeSH).
- MESH :
- analogues et dérivés : Glutathion.
- composition chimique : Glutathione transferase.
- enzymologie : Cytoplasme, Noyau de la cellule, Populus.
- génétique : Populus.
- métabolisme : Glutathion, Glutathione transferase.
- Cinétique, Cristallographie aux rayons X, Gènes de plante, Multimérisation de protéines, Pliage des protéines, Spécificité du substrat.
English descriptors
- KwdEn :
- Cell Nucleus (enzymology), Crystallography, X-Ray (MeSH), Cytoplasm (enzymology), Genes, Plant (MeSH), Glutathione (analogs & derivatives), Glutathione (metabolism), Glutathione Transferase (chemistry), Glutathione Transferase (metabolism), Kinetics (MeSH), Populus (enzymology), Populus (genetics), Protein Folding (MeSH), Protein Multimerization (MeSH), Substrate Specificity (MeSH).
- MESH :
- chemical , analogs & derivatives : Glutathione.
- chemical , chemistry : Glutathione Transferase.
- enzymology : Cell Nucleus, Cytoplasm, Populus.
- genetics : Populus.
- chemical , metabolism : Glutathione, Glutathione Transferase.
- Crystallography, X-Ray, Genes, Plant, Kinetics, Protein Folding, Protein Multimerization, Substrate Specificity.
Abstract
GSTs represent a superfamily of multifunctional proteins which play crucial roles in detoxification processes and secondary metabolism. Instead of promoting the conjugation of glutathione to acceptor molecules as do most GSTs, members of the Lambda class (GSTLs) catalyse deglutathionylation reactions via a catalytic cysteine residue. Three GSTL genes (Pt-GSTL1, Pt-GSTL2 and Pt-GSTL3) are present in Populus trichocarpa, but two transcripts, differing in their 5' extremities, were identified for Pt-GSTL3. Transcripts for these genes were primarily found in flowers, fruits, petioles and buds, but not in leaves and roots, suggesting roles associated with secondary metabolism in these organs. The expression of GFP-fusion proteins in tobacco showed that Pt-GSTL1 is localized in plastids, whereas Pt-GSTL2 and Pt-GSTL3A and Pt-GSTL3B are found in both the cytoplasm and the nucleus. The resolution of Pt-GSTL1 and Pt-GSTL3 structures by X-ray crystallography indicated that, although these proteins adopt a canonical GST fold quite similar to that found in dimeric Omega GSTs, their non-plant counterparts, they are strictly monomeric. This might explain some differences in the enzymatic properties of both enzyme types. Finally, from competition experiments between aromatic substrates and a fluorescent probe, we determined that the recognition of glutathionylated substrates is favoured over non-glutathionylated forms.
DOI: 10.1042/BJ20140390
PubMed: 24825169
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Transferase (chemistry)</term><term>Glutathione Transferase (metabolism)</term><term>Kinetics (MeSH)</term><term>Populus (enzymology)</term><term>Populus (genetics)</term><term>Protein Folding (MeSH)</term><term>Protein Multimerization (MeSH)</term><term>Substrate Specificity (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Cinétique (MeSH)</term><term>Cristallographie aux rayons X (MeSH)</term><term>Cytoplasme (enzymologie)</term><term>Glutathion (analogues et dérivés)</term><term>Glutathion (métabolisme)</term><term>Glutathione transferase (composition chimique)</term><term>Glutathione transferase (métabolisme)</term><term>Gènes de plante (MeSH)</term><term>Multimérisation de protéines (MeSH)</term><term>Noyau de la cellule (enzymologie)</term><term>Pliage des protéines (MeSH)</term><term>Populus (enzymologie)</term><term>Populus (génétique)</term><term>Spécificité du substrat (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analogs & derivatives" xml:lang="en"><term>Glutathione</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Glutathione Transferase</term></keywords><keywords scheme="MESH" qualifier="analogues et dérivés" xml:lang="fr"><term>Glutathion</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Glutathione transferase</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Cytoplasme</term><term>Noyau de la cellule</term><term>Populus</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Cell Nucleus</term><term>Cytoplasm</term><term>Populus</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Populus</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Populus</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Glutathione</term><term>Glutathione Transferase</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Glutathion</term><term>Glutathione transferase</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Crystallography, X-Ray</term><term>Genes, Plant</term><term>Kinetics</term><term>Protein Folding</term><term>Protein Multimerization</term><term>Substrate Specificity</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Cinétique</term><term>Cristallographie aux rayons X</term><term>Gènes de plante</term><term>Multimérisation de protéines</term><term>Pliage des protéines</term><term>Spécificité du substrat</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">GSTs represent a superfamily of multifunctional proteins which play crucial roles in detoxification processes and secondary metabolism. Instead of promoting the conjugation of glutathione to acceptor molecules as do most GSTs, members of the Lambda class (GSTLs) catalyse deglutathionylation reactions via a catalytic cysteine residue. Three GSTL genes (Pt-GSTL1, Pt-GSTL2 and Pt-GSTL3) are present in Populus trichocarpa, but two transcripts, differing in their 5' extremities, were identified for Pt-GSTL3. Transcripts for these genes were primarily found in flowers, fruits, petioles and buds, but not in leaves and roots, suggesting roles associated with secondary metabolism in these organs. The expression of GFP-fusion proteins in tobacco showed that Pt-GSTL1 is localized in plastids, whereas Pt-GSTL2 and Pt-GSTL3A and Pt-GSTL3B are found in both the cytoplasm and the nucleus. The resolution of Pt-GSTL1 and Pt-GSTL3 structures by X-ray crystallography indicated that, although these proteins adopt a canonical GST fold quite similar to that found in dimeric Omega GSTs, their non-plant counterparts, they are strictly monomeric. This might explain some differences in the enzymatic properties of both enzyme types. Finally, from competition experiments between aromatic substrates and a fluorescent probe, we determined that the recognition of glutathionylated substrates is favoured over non-glutathionylated forms. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">24825169</PMID><DateCompleted><Year>2014</Year><Month>09</Month><Day>29</Day></DateCompleted><DateRevised><Year>2014</Year><Month>07</Month><Day>25</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Electronic">1470-8728</ISSN><JournalIssue CitedMedium="Internet"><Volume>462</Volume><Issue>1</Issue><PubDate><Year>2014</Year><Month>Aug</Month><Day>15</Day></PubDate></JournalIssue><Title>The Biochemical journal</Title><ISOAbbreviation>Biochem J</ISOAbbreviation></Journal><ArticleTitle>Structural and enzymatic insights into Lambda glutathione transferases from Populus trichocarpa, monomeric enzymes constituting an early divergent class specific to terrestrial plants.</ArticleTitle><Pagination><MedlinePgn>39-52</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1042/BJ20140390</ELocationID><Abstract><AbstractText>GSTs represent a superfamily of multifunctional proteins which play crucial roles in detoxification processes and secondary metabolism. Instead of promoting the conjugation of glutathione to acceptor molecules as do most GSTs, members of the Lambda class (GSTLs) catalyse deglutathionylation reactions via a catalytic cysteine residue. Three GSTL genes (Pt-GSTL1, Pt-GSTL2 and Pt-GSTL3) are present in Populus trichocarpa, but two transcripts, differing in their 5' extremities, were identified for Pt-GSTL3. Transcripts for these genes were primarily found in flowers, fruits, petioles and buds, but not in leaves and roots, suggesting roles associated with secondary metabolism in these organs. The expression of GFP-fusion proteins in tobacco showed that Pt-GSTL1 is localized in plastids, whereas Pt-GSTL2 and Pt-GSTL3A and Pt-GSTL3B are found in both the cytoplasm and the nucleus. The resolution of Pt-GSTL1 and Pt-GSTL3 structures by X-ray crystallography indicated that, although these proteins adopt a canonical GST fold quite similar to that found in dimeric Omega GSTs, their non-plant counterparts, they are strictly monomeric. This might explain some differences in the enzymatic properties of both enzyme types. Finally, from competition experiments between aromatic substrates and a fluorescent probe, we determined that the recognition of glutathionylated substrates is favoured over non-glutathionylated forms. </AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Lallement</LastName><ForeName>Pierre-Alexandre</ForeName><Initials>PA</Initials></Author><Author ValidYN="Y"><LastName>Meux</LastName><ForeName>Edgar</ForeName><Initials>E</Initials></Author><Author ValidYN="Y"><LastName>Gualberto</LastName><ForeName>José M</ForeName><Initials>JM</Initials><AffiliationInfo><Affiliation>‡Institut de Biologie Moléculaire des Plantes, CNRS-UPR 2357, 67084 Strasbourg, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Prosper</LastName><ForeName>Pascalita</ForeName><Initials>P</Initials></Author><Author ValidYN="Y"><LastName>Didierjean</LastName><ForeName>Claude</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Saul</LastName><ForeName>Frederick</ForeName><Initials>F</Initials><AffiliationInfo><Affiliation>¶Institut Pasteur, Département de Biologie Structurale et Chimie, Plate-Forme de Cristallographie, CNRS-UMR3528, 75724 Paris, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Haouz</LastName><ForeName>Ahmed</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>¶Institut Pasteur, Département de Biologie Structurale et Chimie, Plate-Forme de Cristallographie, CNRS-UMR3528, 75724 Paris, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Rouhier</LastName><ForeName>Nicolas</ForeName><Initials>N</Initials></Author><Author ValidYN="Y"><LastName>Hecker</LastName><ForeName>Arnaud</ForeName><Initials>A</Initials></Author></AuthorList><Language>eng</Language><DataBankList 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Nucleus</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D018360" MajorTopicYN="N">Crystallography, X-Ray</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003593" MajorTopicYN="N">Cytoplasm</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017343" MajorTopicYN="N">Genes, Plant</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005978" MajorTopicYN="N">Glutathione</DescriptorName><QualifierName UI="Q000031" MajorTopicYN="N">analogs & derivatives</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005982" MajorTopicYN="N">Glutathione Transferase</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D032107" MajorTopicYN="N">Populus</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017510" MajorTopicYN="N">Protein Folding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D055503" MajorTopicYN="N">Protein Multimerization</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013379" MajorTopicYN="N">Substrate Specificity</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2014</Year><Month>5</Month><Day>15</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate 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sortKey="Lallement, Pierre Alexandre" sort="Lallement, Pierre Alexandre" uniqKey="Lallement P" first="Pierre-Alexandre" last="Lallement">Pierre-Alexandre Lallement</name><name sortKey="Meux, Edgar" sort="Meux, Edgar" uniqKey="Meux E" first="Edgar" last="Meux">Edgar Meux</name><name sortKey="Prosper, Pascalita" sort="Prosper, Pascalita" uniqKey="Prosper P" first="Pascalita" last="Prosper">Pascalita Prosper</name><name sortKey="Rouhier, Nicolas" sort="Rouhier, Nicolas" uniqKey="Rouhier N" first="Nicolas" last="Rouhier">Nicolas Rouhier</name></noCountry><country name="France"><region name="Grand Est"><name sortKey="Gualberto, Jose M" sort="Gualberto, Jose M" uniqKey="Gualberto J" first="José M" last="Gualberto">José M. Gualberto</name></region><name sortKey="Haouz, Ahmed" sort="Haouz, Ahmed" uniqKey="Haouz A" first="Ahmed" last="Haouz">Ahmed Haouz</name><name sortKey="Saul, Frederick" sort="Saul, Frederick" uniqKey="Saul F" first="Frederick" last="Saul">Frederick Saul</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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