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The poplar Phi class glutathione transferase: expression, activity and structure of GSTF1
Glutathione transferases (GSTs) constitute a superfamily of enzymes with essential roles in cellular detoxification and secondary metabolism in plants as in other organisms. Several plant GSTs, including those of the Phi class (GSTFs), require a conserved catalytic serine residue to perform glutathi...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Frontiers Media S.A.
2014
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4274894/ https://www.ncbi.nlm.nih.gov/pubmed/25566286 http://dx.doi.org/10.3389/fpls.2014.00712 |
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author | Pégeot, Henri Koh, Cha San Petre, Benjamin Mathiot, Sandrine Duplessis, Sébastien Hecker, Arnaud Didierjean, Claude Rouhier, Nicolas |
author_facet | Pégeot, Henri Koh, Cha San Petre, Benjamin Mathiot, Sandrine Duplessis, Sébastien Hecker, Arnaud Didierjean, Claude Rouhier, Nicolas |
author_sort | Pégeot, Henri |
collection | PubMed |
description | Glutathione transferases (GSTs) constitute a superfamily of enzymes with essential roles in cellular detoxification and secondary metabolism in plants as in other organisms. Several plant GSTs, including those of the Phi class (GSTFs), require a conserved catalytic serine residue to perform glutathione (GSH)-conjugation reactions. Genomic analyses revealed that terrestrial plants have around ten GSTFs, eight in the Populus trichocarpa genome, but their physiological functions and substrates are mostly unknown. Transcript expression analyses showed a predominant expression of all genes both in reproductive (female flowers, fruits, floral buds) and vegetative organs (leaves, petioles). Here, we show that the recombinant poplar GSTF1 (PttGSTF1) possesses peroxidase activity toward cumene hydroperoxide and GSH-conjugation activity toward model substrates such as 2,4-dinitrochlorobenzene, benzyl and phenetyl isothiocyanate, 4-nitrophenyl butyrate and 4-hydroxy-2-nonenal but interestingly not on previously identified GSTF-class substrates. In accordance with analytical gel filtration data, crystal structure of PttGSTF1 showed a canonical dimeric organization with bound GSH or 2-(N-morpholino)ethanesulfonic acid molecules. The structure of these protein-substrate complexes allowed delineating the residues contributing to both the G and H sites that form the active site cavity. In sum, the presence of GSTF1 transcripts and proteins in most poplar organs especially those rich in secondary metabolites such as flowers and fruits, together with its GSH-conjugation activity and its documented stress-responsive expression suggest that its function is associated with the catalytic transformation of metabolites and/or peroxide removal rather than with ligandin properties as previously reported for other GSTFs. |
format | Online Article Text |
id | pubmed-4274894 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-42748942015-01-06 The poplar Phi class glutathione transferase: expression, activity and structure of GSTF1 Pégeot, Henri Koh, Cha San Petre, Benjamin Mathiot, Sandrine Duplessis, Sébastien Hecker, Arnaud Didierjean, Claude Rouhier, Nicolas Front Plant Sci Plant Science Glutathione transferases (GSTs) constitute a superfamily of enzymes with essential roles in cellular detoxification and secondary metabolism in plants as in other organisms. Several plant GSTs, including those of the Phi class (GSTFs), require a conserved catalytic serine residue to perform glutathione (GSH)-conjugation reactions. Genomic analyses revealed that terrestrial plants have around ten GSTFs, eight in the Populus trichocarpa genome, but their physiological functions and substrates are mostly unknown. Transcript expression analyses showed a predominant expression of all genes both in reproductive (female flowers, fruits, floral buds) and vegetative organs (leaves, petioles). Here, we show that the recombinant poplar GSTF1 (PttGSTF1) possesses peroxidase activity toward cumene hydroperoxide and GSH-conjugation activity toward model substrates such as 2,4-dinitrochlorobenzene, benzyl and phenetyl isothiocyanate, 4-nitrophenyl butyrate and 4-hydroxy-2-nonenal but interestingly not on previously identified GSTF-class substrates. In accordance with analytical gel filtration data, crystal structure of PttGSTF1 showed a canonical dimeric organization with bound GSH or 2-(N-morpholino)ethanesulfonic acid molecules. The structure of these protein-substrate complexes allowed delineating the residues contributing to both the G and H sites that form the active site cavity. In sum, the presence of GSTF1 transcripts and proteins in most poplar organs especially those rich in secondary metabolites such as flowers and fruits, together with its GSH-conjugation activity and its documented stress-responsive expression suggest that its function is associated with the catalytic transformation of metabolites and/or peroxide removal rather than with ligandin properties as previously reported for other GSTFs. Frontiers Media S.A. 2014-12-23 /pmc/articles/PMC4274894/ /pubmed/25566286 http://dx.doi.org/10.3389/fpls.2014.00712 Text en Copyright © 2014 Pégeot, Koh, Petre, Mathiot, Duplessis, Hecker, Didierjean and Rouhier. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
spellingShingle | Plant Science Pégeot, Henri Koh, Cha San Petre, Benjamin Mathiot, Sandrine Duplessis, Sébastien Hecker, Arnaud Didierjean, Claude Rouhier, Nicolas The poplar Phi class glutathione transferase: expression, activity and structure of GSTF1 |
title | The poplar Phi class glutathione transferase: expression, activity and structure of GSTF1 |
title_full | The poplar Phi class glutathione transferase: expression, activity and structure of GSTF1 |
title_fullStr | The poplar Phi class glutathione transferase: expression, activity and structure of GSTF1 |
title_full_unstemmed | The poplar Phi class glutathione transferase: expression, activity and structure of GSTF1 |
title_short | The poplar Phi class glutathione transferase: expression, activity and structure of GSTF1 |
title_sort | poplar phi class glutathione transferase: expression, activity and structure of gstf1 |
topic | Plant Science |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4274894/ https://www.ncbi.nlm.nih.gov/pubmed/25566286 http://dx.doi.org/10.3389/fpls.2014.00712 |
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