ArticlePhilosophical transactions of the Royal Society of London. Series B, Biological sciences2020
Is there a role for tau glutathione transferases in tetrapyrrole metabolism and retrograde signalling in plants?
Article in Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 18 citations in OpenAlex.
- Genome-Wide Identification ofInternational journal of molecular sciences · 2024Article
- Ascorbate Peroxidase 2 (APX2) of Chlamydomonas Binds Copper and Modulates the Copper Insertion into Plastocyanin.Antioxidants (Basel, Switzerland) · 2023Article
- Genome-wide identification and characterization of glutathione S-transferase gene family in Musa acuminata L. AAA group and gaining an insight to their role in banana fruit development.Journal of applied genetics · 2022Article
- Computational insights into diverse aspects of glutathione S-transferase gene family in Papaver somniferum.Journal of plant research · 2022Article
- Iron in leaves: chemical forms, signalling, and in-cell distribution.Journal of experimental botany · 2022Review
- The Role of Tetrapyrrole- and GUN1-Dependent Signaling on Chloroplast Biogenesis.Plants (Basel, Switzerland) · 2021Review
- Glutathione S-transferase: a versatile protein family.3 Biotech · 2020Review
- Retrograde signals from endosymbiotic organelles: a common control principle in eukaryotic cells.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2020Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
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'.
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