Conformational plasticity of the intrinsically disordered protein asr1 modulates its function as a drought stress-responsive gene
Plants in arid zones are constantly exposed to drought stress. The ASR protein family (Abscisic, Stress, Ripening) -a subgroup of the late embryogenesis abundant superfamily-is involved in the water stress response and adaptation to dry environments. Tomato ASR1, as well as other members of this fam...
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2018
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_19326203_v13_n8_p_Wetzler http://hdl.handle.net/20.500.12110/paper_19326203_v13_n8_p_Wetzler |
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paper:paper_19326203_v13_n8_p_Wetzler2023-06-08T16:30:49Z Conformational plasticity of the intrinsically disordered protein asr1 modulates its function as a drought stress-responsive gene citrate synthase DNA glycerol macrogol proline sodium chloride transcription factor transcription factor ASR1 trehalose unclassified drug zinc ion Asr1 protein, Lycopersicon esculentum plant protein protein binding zinc alpha helix Article biophysics conformational transition dimerization DNA binding drought stress environmental change environmental factor Escherichia coli fluorescence resonance energy transfer heat shock in vitro study in vivo study low temperature nonhuman osmotic stress pH plant cell plasticity protein conformation protein folding protein interaction protein structure protein targeting salt stress chemistry cold drought growth, development and aging metabolism physiological stress protein multimerization protein secondary structure protein unfolding tomato Cold Temperature Droughts Glycerol Hydrogen-Ion Concentration Lycopersicon esculentum Plant Proteins Polyethylene Glycols Protein Binding Protein Multimerization Protein Structure, Secondary Protein Unfolding Stress, Physiological Trehalose Zinc Plants in arid zones are constantly exposed to drought stress. The ASR protein family (Abscisic, Stress, Ripening) -a subgroup of the late embryogenesis abundant superfamily-is involved in the water stress response and adaptation to dry environments. Tomato ASR1, as well as other members of this family, is an intrinsically disordered protein (IDP) that functions as a transcription factor and a chaperone. Here we employed different biophysical techniques to perform a deep in vitro characterization of ASR1 as an IDP and showed how both environmental factors and in vivo targets modulate its folding. We report that ASR1 adopts different conformations such as α-helix or polyproline type II in response to environmental changes. Low temperatures and low pH promote the polyproline type II conformation (PII). While NaCl increases PII content and slightly destabilizes α-helix conformation, PEG and glycerol have an important stabilizing effect of α-helix conformation. The binding of Zn 2 + in the low micromolar range promotes α-helix folding, while extra Zn 2+ results in homo-dimerization. The ASR1-DNA binding is sequence specific and dependent on Zn 2+ . ASR1 chaperone activity does not change upon the structure induction triggered by the addition of Zn 2+ . Furthermore, trehalose, which has no effect on the ASR1 structure by itself, showed a synergistic effect on the ASR1-driven heat shock protection towards the reporter enzyme citrate synthase (CS). These observations prompted the development of a FRET reporter to sense ASR1 folding in vivo. Its performance was confirmed in Escherichia coli under saline and osmotic stress conditions, representing a promising probe to be used in plant cells. Overall, this work supports the notion that ASR1 plasticity is a key feature that facilitates its response to drought stress and its interaction with specific targets. © 2018 Wetzler et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. 2018 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_19326203_v13_n8_p_Wetzler http://hdl.handle.net/20.500.12110/paper_19326203_v13_n8_p_Wetzler |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
citrate synthase DNA glycerol macrogol proline sodium chloride transcription factor transcription factor ASR1 trehalose unclassified drug zinc ion Asr1 protein, Lycopersicon esculentum plant protein protein binding zinc alpha helix Article biophysics conformational transition dimerization DNA binding drought stress environmental change environmental factor Escherichia coli fluorescence resonance energy transfer heat shock in vitro study in vivo study low temperature nonhuman osmotic stress pH plant cell plasticity protein conformation protein folding protein interaction protein structure protein targeting salt stress chemistry cold drought growth, development and aging metabolism physiological stress protein multimerization protein secondary structure protein unfolding tomato Cold Temperature Droughts Glycerol Hydrogen-Ion Concentration Lycopersicon esculentum Plant Proteins Polyethylene Glycols Protein Binding Protein Multimerization Protein Structure, Secondary Protein Unfolding Stress, Physiological Trehalose Zinc |
| spellingShingle |
citrate synthase DNA glycerol macrogol proline sodium chloride transcription factor transcription factor ASR1 trehalose unclassified drug zinc ion Asr1 protein, Lycopersicon esculentum plant protein protein binding zinc alpha helix Article biophysics conformational transition dimerization DNA binding drought stress environmental change environmental factor Escherichia coli fluorescence resonance energy transfer heat shock in vitro study in vivo study low temperature nonhuman osmotic stress pH plant cell plasticity protein conformation protein folding protein interaction protein structure protein targeting salt stress chemistry cold drought growth, development and aging metabolism physiological stress protein multimerization protein secondary structure protein unfolding tomato Cold Temperature Droughts Glycerol Hydrogen-Ion Concentration Lycopersicon esculentum Plant Proteins Polyethylene Glycols Protein Binding Protein Multimerization Protein Structure, Secondary Protein Unfolding Stress, Physiological Trehalose Zinc Conformational plasticity of the intrinsically disordered protein asr1 modulates its function as a drought stress-responsive gene |
| topic_facet |
citrate synthase DNA glycerol macrogol proline sodium chloride transcription factor transcription factor ASR1 trehalose unclassified drug zinc ion Asr1 protein, Lycopersicon esculentum plant protein protein binding zinc alpha helix Article biophysics conformational transition dimerization DNA binding drought stress environmental change environmental factor Escherichia coli fluorescence resonance energy transfer heat shock in vitro study in vivo study low temperature nonhuman osmotic stress pH plant cell plasticity protein conformation protein folding protein interaction protein structure protein targeting salt stress chemistry cold drought growth, development and aging metabolism physiological stress protein multimerization protein secondary structure protein unfolding tomato Cold Temperature Droughts Glycerol Hydrogen-Ion Concentration Lycopersicon esculentum Plant Proteins Polyethylene Glycols Protein Binding Protein Multimerization Protein Structure, Secondary Protein Unfolding Stress, Physiological Trehalose Zinc |
| description |
Plants in arid zones are constantly exposed to drought stress. The ASR protein family (Abscisic, Stress, Ripening) -a subgroup of the late embryogenesis abundant superfamily-is involved in the water stress response and adaptation to dry environments. Tomato ASR1, as well as other members of this family, is an intrinsically disordered protein (IDP) that functions as a transcription factor and a chaperone. Here we employed different biophysical techniques to perform a deep in vitro characterization of ASR1 as an IDP and showed how both environmental factors and in vivo targets modulate its folding. We report that ASR1 adopts different conformations such as α-helix or polyproline type II in response to environmental changes. Low temperatures and low pH promote the polyproline type II conformation (PII). While NaCl increases PII content and slightly destabilizes α-helix conformation, PEG and glycerol have an important stabilizing effect of α-helix conformation. The binding of Zn 2 + in the low micromolar range promotes α-helix folding, while extra Zn 2+ results in homo-dimerization. The ASR1-DNA binding is sequence specific and dependent on Zn 2+ . ASR1 chaperone activity does not change upon the structure induction triggered by the addition of Zn 2+ . Furthermore, trehalose, which has no effect on the ASR1 structure by itself, showed a synergistic effect on the ASR1-driven heat shock protection towards the reporter enzyme citrate synthase (CS). These observations prompted the development of a FRET reporter to sense ASR1 folding in vivo. Its performance was confirmed in Escherichia coli under saline and osmotic stress conditions, representing a promising probe to be used in plant cells. Overall, this work supports the notion that ASR1 plasticity is a key feature that facilitates its response to drought stress and its interaction with specific targets. © 2018 Wetzler et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. |
| title |
Conformational plasticity of the intrinsically disordered protein asr1 modulates its function as a drought stress-responsive gene |
| title_short |
Conformational plasticity of the intrinsically disordered protein asr1 modulates its function as a drought stress-responsive gene |
| title_full |
Conformational plasticity of the intrinsically disordered protein asr1 modulates its function as a drought stress-responsive gene |
| title_fullStr |
Conformational plasticity of the intrinsically disordered protein asr1 modulates its function as a drought stress-responsive gene |
| title_full_unstemmed |
Conformational plasticity of the intrinsically disordered protein asr1 modulates its function as a drought stress-responsive gene |
| title_sort |
conformational plasticity of the intrinsically disordered protein asr1 modulates its function as a drought stress-responsive gene |
| publishDate |
2018 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_19326203_v13_n8_p_Wetzler http://hdl.handle.net/20.500.12110/paper_19326203_v13_n8_p_Wetzler |
| _version_ |
1768544887717756928 |