Comparative structural and functional analysis of phi class glutathione transferases involved in multiple-herbicide resistance of grass weeds and crops
Multiple-herbicide resistant (MHR) weeds are a global problem and a looming threat to weed control in crops. MHR weeds express a specific phi class glutathione transferase (MHR-GSTF) which seems to contribute to herbicide resistance. The present work aims to investigate the structure and catalytic p...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Georgakis, Nikolaos [verfasserIn] |
|---|
| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2020transfer abstract |
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| Schlagwörter: |
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| Umfang: |
11 |
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| Übergeordnetes Werk: |
Enthalten in: Generalized finite difference method with irregular mesh for a class of three-dimensional variable-order time-fractional advection-diffusion equations - Wang, Zhaoyang ELSEVIER, 2021, PPB : an official journal of the Federation of European Societies of Plant Physiology, Amsterdam [u.a.] |
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| Übergeordnetes Werk: |
volume:149 ; year:2020 ; pages:266-276 ; extent:11 |
| Links: |
|---|
| DOI / URN: |
10.1016/j.plaphy.2020.02.012 |
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ELV049613928 |
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| 520 | |a Multiple-herbicide resistant (MHR) weeds are a global problem and a looming threat to weed control in crops. MHR weeds express a specific phi class glutathione transferase (MHR-GSTF) which seems to contribute to herbicide resistance. The present work aims to investigate the structure and catalytic properties of the MHR-GSTFs from different grass weeds and crops (Alopecurus myosuroides, Lolium rigidum, Hordeum vulgare, Triticum aestivum). Recombinant MHR-GSTFs were expressed in E. coli and purified by affinity chromatography. Kinetic analysis of substrate specificity using a range of thiol substrates and xenobiotic compounds suggested that all enzymes display a broad range of specificity and are capable of detoxifying major stress-induced toxic products. Notably, all tested enzymes exhibited high activity towards organic hydroperoxides. The crystal structure of MHR-GSTF from Alopecurus myosuroides (AmGSTF) was determined by molecular replacement at 1.33 Å resolution. The enzyme was resolved with bound glutathione sulfenic acid (GSOH) at the G-site and succinic acid at the H-site. The enzyme shows conserved structural features compared to other Phi class GSTs. However, some differences were observed at the C-terminal helix H9 that may affect substrate specificity. The structural and functional features of AmGSTF were compared with those of the homologue crop enzymes (HvGSTF and TaGSTF) and discussed in light of their contribution to the MHR mechanism. | ||
| 520 | |a Multiple-herbicide resistant (MHR) weeds are a global problem and a looming threat to weed control in crops. MHR weeds express a specific phi class glutathione transferase (MHR-GSTF) which seems to contribute to herbicide resistance. The present work aims to investigate the structure and catalytic properties of the MHR-GSTFs from different grass weeds and crops (Alopecurus myosuroides, Lolium rigidum, Hordeum vulgare, Triticum aestivum). Recombinant MHR-GSTFs were expressed in E. coli and purified by affinity chromatography. Kinetic analysis of substrate specificity using a range of thiol substrates and xenobiotic compounds suggested that all enzymes display a broad range of specificity and are capable of detoxifying major stress-induced toxic products. Notably, all tested enzymes exhibited high activity towards organic hydroperoxides. The crystal structure of MHR-GSTF from Alopecurus myosuroides (AmGSTF) was determined by molecular replacement at 1.33 Å resolution. The enzyme was resolved with bound glutathione sulfenic acid (GSOH) at the G-site and succinic acid at the H-site. The enzyme shows conserved structural features compared to other Phi class GSTs. However, some differences were observed at the C-terminal helix H9 that may affect substrate specificity. The structural and functional features of AmGSTF were compared with those of the homologue crop enzymes (HvGSTF and TaGSTF) and discussed in light of their contribution to the MHR mechanism. | ||
| 650 | 7 | |a Abiotic stress |2 Elsevier | |
| 650 | 7 | |a Glutathione transferase |2 Elsevier | |
| 650 | 7 | |a Multiple-herbicide resistance |2 Elsevier | |
| 650 | 7 | |a Pesticide metabolism |2 Elsevier | |
| 700 | 1 | |a Poudel, Nirmal |4 oth | |
| 700 | 1 | |a Papageorgiou, Anastassios C. |4 oth | |
| 700 | 1 | |a Labrou, Nikolaos E. |4 oth | |
| 773 | 0 | 8 | |i Enthalten in |n Elsevier Science |a Wang, Zhaoyang ELSEVIER |t Generalized finite difference method with irregular mesh for a class of three-dimensional variable-order time-fractional advection-diffusion equations |d 2021 |d PPB : an official journal of the Federation of European Societies of Plant Physiology |g Amsterdam [u.a.] |w (DE-627)ELV006529712 |
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10.1016/j.plaphy.2020.02.012 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000000948.pica (DE-627)ELV049613928 (ELSEVIER)S0981-9428(20)30066-8 DE-627 ger DE-627 rakwb eng 690 620 VZ 50.03 bkl Georgakis, Nikolaos verfasserin aut Comparative structural and functional analysis of phi class glutathione transferases involved in multiple-herbicide resistance of grass weeds and crops 2020transfer abstract 11 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Multiple-herbicide resistant (MHR) weeds are a global problem and a looming threat to weed control in crops. MHR weeds express a specific phi class glutathione transferase (MHR-GSTF) which seems to contribute to herbicide resistance. The present work aims to investigate the structure and catalytic properties of the MHR-GSTFs from different grass weeds and crops (Alopecurus myosuroides, Lolium rigidum, Hordeum vulgare, Triticum aestivum). Recombinant MHR-GSTFs were expressed in E. coli and purified by affinity chromatography. Kinetic analysis of substrate specificity using a range of thiol substrates and xenobiotic compounds suggested that all enzymes display a broad range of specificity and are capable of detoxifying major stress-induced toxic products. Notably, all tested enzymes exhibited high activity towards organic hydroperoxides. The crystal structure of MHR-GSTF from Alopecurus myosuroides (AmGSTF) was determined by molecular replacement at 1.33 Å resolution. The enzyme was resolved with bound glutathione sulfenic acid (GSOH) at the G-site and succinic acid at the H-site. The enzyme shows conserved structural features compared to other Phi class GSTs. However, some differences were observed at the C-terminal helix H9 that may affect substrate specificity. The structural and functional features of AmGSTF were compared with those of the homologue crop enzymes (HvGSTF and TaGSTF) and discussed in light of their contribution to the MHR mechanism. Multiple-herbicide resistant (MHR) weeds are a global problem and a looming threat to weed control in crops. MHR weeds express a specific phi class glutathione transferase (MHR-GSTF) which seems to contribute to herbicide resistance. The present work aims to investigate the structure and catalytic properties of the MHR-GSTFs from different grass weeds and crops (Alopecurus myosuroides, Lolium rigidum, Hordeum vulgare, Triticum aestivum). Recombinant MHR-GSTFs were expressed in E. coli and purified by affinity chromatography. Kinetic analysis of substrate specificity using a range of thiol substrates and xenobiotic compounds suggested that all enzymes display a broad range of specificity and are capable of detoxifying major stress-induced toxic products. Notably, all tested enzymes exhibited high activity towards organic hydroperoxides. The crystal structure of MHR-GSTF from Alopecurus myosuroides (AmGSTF) was determined by molecular replacement at 1.33 Å resolution. The enzyme was resolved with bound glutathione sulfenic acid (GSOH) at the G-site and succinic acid at the H-site. The enzyme shows conserved structural features compared to other Phi class GSTs. However, some differences were observed at the C-terminal helix H9 that may affect substrate specificity. The structural and functional features of AmGSTF were compared with those of the homologue crop enzymes (HvGSTF and TaGSTF) and discussed in light of their contribution to the MHR mechanism. Abiotic stress Elsevier Glutathione transferase Elsevier Multiple-herbicide resistance Elsevier Pesticide metabolism Elsevier Poudel, Nirmal oth Papageorgiou, Anastassios C. oth Labrou, Nikolaos E. oth Enthalten in Elsevier Science Wang, Zhaoyang ELSEVIER Generalized finite difference method with irregular mesh for a class of three-dimensional variable-order time-fractional advection-diffusion equations 2021 PPB : an official journal of the Federation of European Societies of Plant Physiology Amsterdam [u.a.] (DE-627)ELV006529712 volume:149 year:2020 pages:266-276 extent:11 https://doi.org/10.1016/j.plaphy.2020.02.012 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U 50.03 Methoden und Techniken der Ingenieurwissenschaften VZ AR 149 2020 266-276 11 |
| spelling |
10.1016/j.plaphy.2020.02.012 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000000948.pica (DE-627)ELV049613928 (ELSEVIER)S0981-9428(20)30066-8 DE-627 ger DE-627 rakwb eng 690 620 VZ 50.03 bkl Georgakis, Nikolaos verfasserin aut Comparative structural and functional analysis of phi class glutathione transferases involved in multiple-herbicide resistance of grass weeds and crops 2020transfer abstract 11 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Multiple-herbicide resistant (MHR) weeds are a global problem and a looming threat to weed control in crops. MHR weeds express a specific phi class glutathione transferase (MHR-GSTF) which seems to contribute to herbicide resistance. The present work aims to investigate the structure and catalytic properties of the MHR-GSTFs from different grass weeds and crops (Alopecurus myosuroides, Lolium rigidum, Hordeum vulgare, Triticum aestivum). Recombinant MHR-GSTFs were expressed in E. coli and purified by affinity chromatography. Kinetic analysis of substrate specificity using a range of thiol substrates and xenobiotic compounds suggested that all enzymes display a broad range of specificity and are capable of detoxifying major stress-induced toxic products. Notably, all tested enzymes exhibited high activity towards organic hydroperoxides. The crystal structure of MHR-GSTF from Alopecurus myosuroides (AmGSTF) was determined by molecular replacement at 1.33 Å resolution. The enzyme was resolved with bound glutathione sulfenic acid (GSOH) at the G-site and succinic acid at the H-site. The enzyme shows conserved structural features compared to other Phi class GSTs. However, some differences were observed at the C-terminal helix H9 that may affect substrate specificity. The structural and functional features of AmGSTF were compared with those of the homologue crop enzymes (HvGSTF and TaGSTF) and discussed in light of their contribution to the MHR mechanism. Multiple-herbicide resistant (MHR) weeds are a global problem and a looming threat to weed control in crops. MHR weeds express a specific phi class glutathione transferase (MHR-GSTF) which seems to contribute to herbicide resistance. The present work aims to investigate the structure and catalytic properties of the MHR-GSTFs from different grass weeds and crops (Alopecurus myosuroides, Lolium rigidum, Hordeum vulgare, Triticum aestivum). Recombinant MHR-GSTFs were expressed in E. coli and purified by affinity chromatography. Kinetic analysis of substrate specificity using a range of thiol substrates and xenobiotic compounds suggested that all enzymes display a broad range of specificity and are capable of detoxifying major stress-induced toxic products. Notably, all tested enzymes exhibited high activity towards organic hydroperoxides. The crystal structure of MHR-GSTF from Alopecurus myosuroides (AmGSTF) was determined by molecular replacement at 1.33 Å resolution. The enzyme was resolved with bound glutathione sulfenic acid (GSOH) at the G-site and succinic acid at the H-site. The enzyme shows conserved structural features compared to other Phi class GSTs. However, some differences were observed at the C-terminal helix H9 that may affect substrate specificity. The structural and functional features of AmGSTF were compared with those of the homologue crop enzymes (HvGSTF and TaGSTF) and discussed in light of their contribution to the MHR mechanism. Abiotic stress Elsevier Glutathione transferase Elsevier Multiple-herbicide resistance Elsevier Pesticide metabolism Elsevier Poudel, Nirmal oth Papageorgiou, Anastassios C. oth Labrou, Nikolaos E. oth Enthalten in Elsevier Science Wang, Zhaoyang ELSEVIER Generalized finite difference method with irregular mesh for a class of three-dimensional variable-order time-fractional advection-diffusion equations 2021 PPB : an official journal of the Federation of European Societies of Plant Physiology Amsterdam [u.a.] (DE-627)ELV006529712 volume:149 year:2020 pages:266-276 extent:11 https://doi.org/10.1016/j.plaphy.2020.02.012 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U 50.03 Methoden und Techniken der Ingenieurwissenschaften VZ AR 149 2020 266-276 11 |
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10.1016/j.plaphy.2020.02.012 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000000948.pica (DE-627)ELV049613928 (ELSEVIER)S0981-9428(20)30066-8 DE-627 ger DE-627 rakwb eng 690 620 VZ 50.03 bkl Georgakis, Nikolaos verfasserin aut Comparative structural and functional analysis of phi class glutathione transferases involved in multiple-herbicide resistance of grass weeds and crops 2020transfer abstract 11 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Multiple-herbicide resistant (MHR) weeds are a global problem and a looming threat to weed control in crops. MHR weeds express a specific phi class glutathione transferase (MHR-GSTF) which seems to contribute to herbicide resistance. The present work aims to investigate the structure and catalytic properties of the MHR-GSTFs from different grass weeds and crops (Alopecurus myosuroides, Lolium rigidum, Hordeum vulgare, Triticum aestivum). Recombinant MHR-GSTFs were expressed in E. coli and purified by affinity chromatography. Kinetic analysis of substrate specificity using a range of thiol substrates and xenobiotic compounds suggested that all enzymes display a broad range of specificity and are capable of detoxifying major stress-induced toxic products. Notably, all tested enzymes exhibited high activity towards organic hydroperoxides. The crystal structure of MHR-GSTF from Alopecurus myosuroides (AmGSTF) was determined by molecular replacement at 1.33 Å resolution. The enzyme was resolved with bound glutathione sulfenic acid (GSOH) at the G-site and succinic acid at the H-site. The enzyme shows conserved structural features compared to other Phi class GSTs. However, some differences were observed at the C-terminal helix H9 that may affect substrate specificity. The structural and functional features of AmGSTF were compared with those of the homologue crop enzymes (HvGSTF and TaGSTF) and discussed in light of their contribution to the MHR mechanism. Multiple-herbicide resistant (MHR) weeds are a global problem and a looming threat to weed control in crops. MHR weeds express a specific phi class glutathione transferase (MHR-GSTF) which seems to contribute to herbicide resistance. The present work aims to investigate the structure and catalytic properties of the MHR-GSTFs from different grass weeds and crops (Alopecurus myosuroides, Lolium rigidum, Hordeum vulgare, Triticum aestivum). Recombinant MHR-GSTFs were expressed in E. coli and purified by affinity chromatography. Kinetic analysis of substrate specificity using a range of thiol substrates and xenobiotic compounds suggested that all enzymes display a broad range of specificity and are capable of detoxifying major stress-induced toxic products. Notably, all tested enzymes exhibited high activity towards organic hydroperoxides. The crystal structure of MHR-GSTF from Alopecurus myosuroides (AmGSTF) was determined by molecular replacement at 1.33 Å resolution. The enzyme was resolved with bound glutathione sulfenic acid (GSOH) at the G-site and succinic acid at the H-site. The enzyme shows conserved structural features compared to other Phi class GSTs. However, some differences were observed at the C-terminal helix H9 that may affect substrate specificity. The structural and functional features of AmGSTF were compared with those of the homologue crop enzymes (HvGSTF and TaGSTF) and discussed in light of their contribution to the MHR mechanism. Abiotic stress Elsevier Glutathione transferase Elsevier Multiple-herbicide resistance Elsevier Pesticide metabolism Elsevier Poudel, Nirmal oth Papageorgiou, Anastassios C. oth Labrou, Nikolaos E. oth Enthalten in Elsevier Science Wang, Zhaoyang ELSEVIER Generalized finite difference method with irregular mesh for a class of three-dimensional variable-order time-fractional advection-diffusion equations 2021 PPB : an official journal of the Federation of European Societies of Plant Physiology Amsterdam [u.a.] (DE-627)ELV006529712 volume:149 year:2020 pages:266-276 extent:11 https://doi.org/10.1016/j.plaphy.2020.02.012 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U 50.03 Methoden und Techniken der Ingenieurwissenschaften VZ AR 149 2020 266-276 11 |
| allfieldsGer |
10.1016/j.plaphy.2020.02.012 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000000948.pica (DE-627)ELV049613928 (ELSEVIER)S0981-9428(20)30066-8 DE-627 ger DE-627 rakwb eng 690 620 VZ 50.03 bkl Georgakis, Nikolaos verfasserin aut Comparative structural and functional analysis of phi class glutathione transferases involved in multiple-herbicide resistance of grass weeds and crops 2020transfer abstract 11 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Multiple-herbicide resistant (MHR) weeds are a global problem and a looming threat to weed control in crops. MHR weeds express a specific phi class glutathione transferase (MHR-GSTF) which seems to contribute to herbicide resistance. The present work aims to investigate the structure and catalytic properties of the MHR-GSTFs from different grass weeds and crops (Alopecurus myosuroides, Lolium rigidum, Hordeum vulgare, Triticum aestivum). Recombinant MHR-GSTFs were expressed in E. coli and purified by affinity chromatography. Kinetic analysis of substrate specificity using a range of thiol substrates and xenobiotic compounds suggested that all enzymes display a broad range of specificity and are capable of detoxifying major stress-induced toxic products. Notably, all tested enzymes exhibited high activity towards organic hydroperoxides. The crystal structure of MHR-GSTF from Alopecurus myosuroides (AmGSTF) was determined by molecular replacement at 1.33 Å resolution. The enzyme was resolved with bound glutathione sulfenic acid (GSOH) at the G-site and succinic acid at the H-site. The enzyme shows conserved structural features compared to other Phi class GSTs. However, some differences were observed at the C-terminal helix H9 that may affect substrate specificity. The structural and functional features of AmGSTF were compared with those of the homologue crop enzymes (HvGSTF and TaGSTF) and discussed in light of their contribution to the MHR mechanism. Multiple-herbicide resistant (MHR) weeds are a global problem and a looming threat to weed control in crops. MHR weeds express a specific phi class glutathione transferase (MHR-GSTF) which seems to contribute to herbicide resistance. The present work aims to investigate the structure and catalytic properties of the MHR-GSTFs from different grass weeds and crops (Alopecurus myosuroides, Lolium rigidum, Hordeum vulgare, Triticum aestivum). Recombinant MHR-GSTFs were expressed in E. coli and purified by affinity chromatography. Kinetic analysis of substrate specificity using a range of thiol substrates and xenobiotic compounds suggested that all enzymes display a broad range of specificity and are capable of detoxifying major stress-induced toxic products. Notably, all tested enzymes exhibited high activity towards organic hydroperoxides. The crystal structure of MHR-GSTF from Alopecurus myosuroides (AmGSTF) was determined by molecular replacement at 1.33 Å resolution. The enzyme was resolved with bound glutathione sulfenic acid (GSOH) at the G-site and succinic acid at the H-site. The enzyme shows conserved structural features compared to other Phi class GSTs. However, some differences were observed at the C-terminal helix H9 that may affect substrate specificity. The structural and functional features of AmGSTF were compared with those of the homologue crop enzymes (HvGSTF and TaGSTF) and discussed in light of their contribution to the MHR mechanism. Abiotic stress Elsevier Glutathione transferase Elsevier Multiple-herbicide resistance Elsevier Pesticide metabolism Elsevier Poudel, Nirmal oth Papageorgiou, Anastassios C. oth Labrou, Nikolaos E. oth Enthalten in Elsevier Science Wang, Zhaoyang ELSEVIER Generalized finite difference method with irregular mesh for a class of three-dimensional variable-order time-fractional advection-diffusion equations 2021 PPB : an official journal of the Federation of European Societies of Plant Physiology Amsterdam [u.a.] (DE-627)ELV006529712 volume:149 year:2020 pages:266-276 extent:11 https://doi.org/10.1016/j.plaphy.2020.02.012 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U 50.03 Methoden und Techniken der Ingenieurwissenschaften VZ AR 149 2020 266-276 11 |
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10.1016/j.plaphy.2020.02.012 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000000948.pica (DE-627)ELV049613928 (ELSEVIER)S0981-9428(20)30066-8 DE-627 ger DE-627 rakwb eng 690 620 VZ 50.03 bkl Georgakis, Nikolaos verfasserin aut Comparative structural and functional analysis of phi class glutathione transferases involved in multiple-herbicide resistance of grass weeds and crops 2020transfer abstract 11 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Multiple-herbicide resistant (MHR) weeds are a global problem and a looming threat to weed control in crops. MHR weeds express a specific phi class glutathione transferase (MHR-GSTF) which seems to contribute to herbicide resistance. The present work aims to investigate the structure and catalytic properties of the MHR-GSTFs from different grass weeds and crops (Alopecurus myosuroides, Lolium rigidum, Hordeum vulgare, Triticum aestivum). Recombinant MHR-GSTFs were expressed in E. coli and purified by affinity chromatography. Kinetic analysis of substrate specificity using a range of thiol substrates and xenobiotic compounds suggested that all enzymes display a broad range of specificity and are capable of detoxifying major stress-induced toxic products. Notably, all tested enzymes exhibited high activity towards organic hydroperoxides. The crystal structure of MHR-GSTF from Alopecurus myosuroides (AmGSTF) was determined by molecular replacement at 1.33 Å resolution. The enzyme was resolved with bound glutathione sulfenic acid (GSOH) at the G-site and succinic acid at the H-site. The enzyme shows conserved structural features compared to other Phi class GSTs. However, some differences were observed at the C-terminal helix H9 that may affect substrate specificity. The structural and functional features of AmGSTF were compared with those of the homologue crop enzymes (HvGSTF and TaGSTF) and discussed in light of their contribution to the MHR mechanism. Multiple-herbicide resistant (MHR) weeds are a global problem and a looming threat to weed control in crops. MHR weeds express a specific phi class glutathione transferase (MHR-GSTF) which seems to contribute to herbicide resistance. The present work aims to investigate the structure and catalytic properties of the MHR-GSTFs from different grass weeds and crops (Alopecurus myosuroides, Lolium rigidum, Hordeum vulgare, Triticum aestivum). Recombinant MHR-GSTFs were expressed in E. coli and purified by affinity chromatography. Kinetic analysis of substrate specificity using a range of thiol substrates and xenobiotic compounds suggested that all enzymes display a broad range of specificity and are capable of detoxifying major stress-induced toxic products. Notably, all tested enzymes exhibited high activity towards organic hydroperoxides. The crystal structure of MHR-GSTF from Alopecurus myosuroides (AmGSTF) was determined by molecular replacement at 1.33 Å resolution. The enzyme was resolved with bound glutathione sulfenic acid (GSOH) at the G-site and succinic acid at the H-site. The enzyme shows conserved structural features compared to other Phi class GSTs. However, some differences were observed at the C-terminal helix H9 that may affect substrate specificity. The structural and functional features of AmGSTF were compared with those of the homologue crop enzymes (HvGSTF and TaGSTF) and discussed in light of their contribution to the MHR mechanism. Abiotic stress Elsevier Glutathione transferase Elsevier Multiple-herbicide resistance Elsevier Pesticide metabolism Elsevier Poudel, Nirmal oth Papageorgiou, Anastassios C. oth Labrou, Nikolaos E. oth Enthalten in Elsevier Science Wang, Zhaoyang ELSEVIER Generalized finite difference method with irregular mesh for a class of three-dimensional variable-order time-fractional advection-diffusion equations 2021 PPB : an official journal of the Federation of European Societies of Plant Physiology Amsterdam [u.a.] (DE-627)ELV006529712 volume:149 year:2020 pages:266-276 extent:11 https://doi.org/10.1016/j.plaphy.2020.02.012 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U 50.03 Methoden und Techniken der Ingenieurwissenschaften VZ AR 149 2020 266-276 11 |
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Enthalten in Generalized finite difference method with irregular mesh for a class of three-dimensional variable-order time-fractional advection-diffusion equations Amsterdam [u.a.] volume:149 year:2020 pages:266-276 extent:11 |
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comparative structural and functional analysis of phi class glutathione transferases involved in multiple-herbicide resistance of grass weeds and crops |
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Comparative structural and functional analysis of phi class glutathione transferases involved in multiple-herbicide resistance of grass weeds and crops |
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Multiple-herbicide resistant (MHR) weeds are a global problem and a looming threat to weed control in crops. MHR weeds express a specific phi class glutathione transferase (MHR-GSTF) which seems to contribute to herbicide resistance. The present work aims to investigate the structure and catalytic properties of the MHR-GSTFs from different grass weeds and crops (Alopecurus myosuroides, Lolium rigidum, Hordeum vulgare, Triticum aestivum). Recombinant MHR-GSTFs were expressed in E. coli and purified by affinity chromatography. Kinetic analysis of substrate specificity using a range of thiol substrates and xenobiotic compounds suggested that all enzymes display a broad range of specificity and are capable of detoxifying major stress-induced toxic products. Notably, all tested enzymes exhibited high activity towards organic hydroperoxides. The crystal structure of MHR-GSTF from Alopecurus myosuroides (AmGSTF) was determined by molecular replacement at 1.33 Å resolution. The enzyme was resolved with bound glutathione sulfenic acid (GSOH) at the G-site and succinic acid at the H-site. The enzyme shows conserved structural features compared to other Phi class GSTs. However, some differences were observed at the C-terminal helix H9 that may affect substrate specificity. The structural and functional features of AmGSTF were compared with those of the homologue crop enzymes (HvGSTF and TaGSTF) and discussed in light of their contribution to the MHR mechanism. |
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Multiple-herbicide resistant (MHR) weeds are a global problem and a looming threat to weed control in crops. MHR weeds express a specific phi class glutathione transferase (MHR-GSTF) which seems to contribute to herbicide resistance. The present work aims to investigate the structure and catalytic properties of the MHR-GSTFs from different grass weeds and crops (Alopecurus myosuroides, Lolium rigidum, Hordeum vulgare, Triticum aestivum). Recombinant MHR-GSTFs were expressed in E. coli and purified by affinity chromatography. Kinetic analysis of substrate specificity using a range of thiol substrates and xenobiotic compounds suggested that all enzymes display a broad range of specificity and are capable of detoxifying major stress-induced toxic products. Notably, all tested enzymes exhibited high activity towards organic hydroperoxides. The crystal structure of MHR-GSTF from Alopecurus myosuroides (AmGSTF) was determined by molecular replacement at 1.33 Å resolution. The enzyme was resolved with bound glutathione sulfenic acid (GSOH) at the G-site and succinic acid at the H-site. The enzyme shows conserved structural features compared to other Phi class GSTs. However, some differences were observed at the C-terminal helix H9 that may affect substrate specificity. The structural and functional features of AmGSTF were compared with those of the homologue crop enzymes (HvGSTF and TaGSTF) and discussed in light of their contribution to the MHR mechanism. |
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Multiple-herbicide resistant (MHR) weeds are a global problem and a looming threat to weed control in crops. MHR weeds express a specific phi class glutathione transferase (MHR-GSTF) which seems to contribute to herbicide resistance. The present work aims to investigate the structure and catalytic properties of the MHR-GSTFs from different grass weeds and crops (Alopecurus myosuroides, Lolium rigidum, Hordeum vulgare, Triticum aestivum). Recombinant MHR-GSTFs were expressed in E. coli and purified by affinity chromatography. Kinetic analysis of substrate specificity using a range of thiol substrates and xenobiotic compounds suggested that all enzymes display a broad range of specificity and are capable of detoxifying major stress-induced toxic products. Notably, all tested enzymes exhibited high activity towards organic hydroperoxides. The crystal structure of MHR-GSTF from Alopecurus myosuroides (AmGSTF) was determined by molecular replacement at 1.33 Å resolution. The enzyme was resolved with bound glutathione sulfenic acid (GSOH) at the G-site and succinic acid at the H-site. The enzyme shows conserved structural features compared to other Phi class GSTs. However, some differences were observed at the C-terminal helix H9 that may affect substrate specificity. The structural and functional features of AmGSTF were compared with those of the homologue crop enzymes (HvGSTF and TaGSTF) and discussed in light of their contribution to the MHR mechanism. |
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