Is there a role for tau glutathione transferases in tetrapyrrole metabolism and retrograde signalling in plants?
Identifieur interne : 000154 ( Main/Curation ); précédent : 000153; suivant : 000155Is there a role for tau glutathione transferases in tetrapyrrole metabolism and retrograde signalling in plants?
Auteurs : Elodie Sylvestre-Gonon [France] ; Mathieu Schwartz [France] ; Jean-Michel Girardet [France] ; Arnaud Hecker [France] ; Nicolas Rouhier [France]Source :
- Philosophical transactions of the Royal Society of London. Series B, Biological sciences [ 1471-2970 ] ; 2020.
Abstract
In plants, tetrapyrrole biosynthesis occurs in chloroplasts, the reactions being catalysed by stromal and membrane-bound enzymes. The tetrapyrrole moiety is a backbone for chlorophylls and cofactors such as sirohaems, haems and phytochromobilins. Owing to this diversity, the potential cytotoxicity of some precursors and the associated synthesis costs, a tight control exists to adjust the demand and the fluxes for each molecule. After synthesis, haems and phytochromobilins are incorporated into proteins found in other subcellular compartments. However, there is only very limited information about the chaperones and membrane transporters involved in the trafficking of these molecules. After summarizing evidence indicating that glutathione transferases (GST) may be part of the transport and/or degradation processes of porphyrin derivatives, we provide experimental data indicating that tau glutathione transferases (GSTU) bind protoporphyrin IX and haem moieties and use structural modelling to identify possible residues responsible for their binding in the active site hydrophobic pocket. Finally, we discuss the possible roles associated with the binding, catalytic transformation (i.e. glutathione conjugation) and/or transport of tetrapyrroles by GSTUs, considering their subcellular localization and capacity to interact with ABC transporters. This article is part of the theme issue 'Retrograde signalling from endosymbiotic organelles'.
DOI: 10.1098/rstb.2019.0404
PubMed: 32362257
PubMed Central: PMC7209958
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plants?</title><author><name sortKey="Sylvestre Gonon, Elodie" sort="Sylvestre Gonon, Elodie" uniqKey="Sylvestre Gonon E" first="Elodie" last="Sylvestre-Gonon">Elodie Sylvestre-Gonon</name><affiliation wicri:level="1"><nlm:affiliation>Université de Lorraine, INRAE, IAM, 54000 Nancy, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Université de Lorraine, INRAE, IAM, 54000 Nancy</wicri:regionArea></affiliation></author><author><name sortKey="Schwartz, Mathieu" sort="Schwartz, Mathieu" uniqKey="Schwartz M" first="Mathieu" last="Schwartz">Mathieu Schwartz</name><affiliation wicri:level="1"><nlm:affiliation>Université de Lorraine, INRAE, IAM, 54000 Nancy, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Université de Lorraine, INRAE, IAM, 54000 Nancy</wicri:regionArea></affiliation></author><author><name sortKey="Girardet, Jean Michel" sort="Girardet, Jean Michel" uniqKey="Girardet J" first="Jean-Michel" last="Girardet">Jean-Michel Girardet</name><affiliation wicri:level="1"><nlm:affiliation>Université de Lorraine, INRAE, IAM, 54000 Nancy, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Université de Lorraine, INRAE, IAM, 54000 Nancy</wicri:regionArea></affiliation></author><author><name sortKey="Hecker, Arnaud" sort="Hecker, Arnaud" uniqKey="Hecker A" first="Arnaud" last="Hecker">Arnaud Hecker</name><affiliation wicri:level="1"><nlm:affiliation>Université de Lorraine, INRAE, IAM, 54000 Nancy, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Université de Lorraine, INRAE, IAM, 54000 Nancy</wicri:regionArea></affiliation></author><author><name sortKey="Rouhier, Nicolas" sort="Rouhier, Nicolas" uniqKey="Rouhier N" first="Nicolas" last="Rouhier">Nicolas Rouhier</name><affiliation wicri:level="1"><nlm:affiliation>Université de Lorraine, INRAE, IAM, 54000 Nancy, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Université de Lorraine, INRAE, IAM, 54000 Nancy</wicri:regionArea></affiliation></author></analytic><series><title level="j">Philosophical transactions of the Royal Society of London. Series B, Biological sciences</title><idno type="eISSN">1471-2970</idno><imprint><date when="2020" type="published">2020</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">In plants, tetrapyrrole biosynthesis occurs in chloroplasts, the reactions being catalysed by stromal and membrane-bound enzymes. The tetrapyrrole moiety is a backbone for chlorophylls and cofactors such as sirohaems, haems and phytochromobilins. Owing to this diversity, the potential cytotoxicity of some precursors and the associated synthesis costs, a tight control exists to adjust the demand and the fluxes for each molecule. After synthesis, haems and phytochromobilins are incorporated into proteins found in other subcellular compartments. However, there is only very limited information about the chaperones and membrane transporters involved in the trafficking of these molecules. After summarizing evidence indicating that glutathione transferases (GST) may be part of the transport and/or degradation processes of porphyrin derivatives, we provide experimental data indicating that tau glutathione transferases (GSTU) bind protoporphyrin IX and haem moieties and use structural modelling to identify possible residues responsible for their binding in the active site hydrophobic pocket. Finally, we discuss the possible roles associated with the binding, catalytic transformation (i.e. glutathione conjugation) and/or transport of tetrapyrroles by GSTUs, considering their subcellular localization and capacity to interact with ABC transporters. This article is part of the theme issue 'Retrograde signalling from endosymbiotic organelles'.</div></front></TEI><pubmed><MedlineCitation Status="In-Process" Owner="NLM"><PMID Version="1">32362257</PMID><DateRevised><Year>2020</Year><Month>08</Month><Day>10</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1471-2970</ISSN><JournalIssue CitedMedium="Internet"><Volume>375</Volume><Issue>1801</Issue><PubDate><Year>2020</Year><Month>06</Month><Day>22</Day></PubDate></JournalIssue><Title>Philosophical transactions of the Royal Society of London. 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However, there is only very limited information about the chaperones and membrane transporters involved in the trafficking of these molecules. After summarizing evidence indicating that glutathione transferases (GST) may be part of the transport and/or degradation processes of porphyrin derivatives, we provide experimental data indicating that tau glutathione transferases (GSTU) bind protoporphyrin IX and haem moieties and use structural modelling to identify possible residues responsible for their binding in the active site hydrophobic pocket. Finally, we discuss the possible roles associated with the binding, catalytic transformation (i.e. glutathione conjugation) and/or transport of tetrapyrroles by GSTUs, considering their subcellular localization and capacity to interact with ABC transporters. 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