Phosphorylation Alters the Interaction of the Arabidopsis Phosphotransfer Protein AHP1 with Its Sensor Kinase ETR1
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{"title"=>"Phosphorylation alters the interaction of the Arabidopsis phosphotransfer protein AHP1 with its sensor kinase ETR1", "type"=>"journal", "authors"=>[{"first_name"=>"Benjamin", "last_name"=>"Scharein", "scopus_author_id"=>"23986232100"}, {"first_name"=>"Georg", "last_name"=>"Groth", "scopus_author_id"=>"7003400609"}], "year"=>2011, "source"=>"PLoS ONE", "identifiers"=>{"pui"=>"362489465", "issn"=>"19326203", "doi"=>"10.1371/journal.pone.0024173", "scopus"=>"2-s2.0-80052421225", "sgr"=>"80052421225", "isbn"=>"1932-6203 (Electronic)\\n1932-6203 (Linking)", "pmid"=>"21912672"}, "id"=>"8945e3ab-6346-336e-8507-4b17ad991eb3", "abstract"=>"The ethylene receptor ethylene response 1 (ETR1) and the Arabidopsis histidine-containing phosphotransfer protein 1 (AHP1) form a tight complex in vitro. According to our current model ETR1 and AHP1 together with a response regulator form a phosphorelay system controlling the gene expression response to the plant hormone ethylene, similar to the two-component signaling in bacteria. The model implies that ETR1 functions as a sensor kinase and is autophosphorylated in the absence of ethylene. The phosphoryl group is then transferred onto a histidine at the canonical phosphorylation site in AHP1. For phosphoryl group transfer both binding partners need to form a tight complex. After ethylene binding the receptor is switched to the non-phosphorylated state. This switch is accompanied by a conformational change that decreases the affinity to the phosphorylated AHP1. To test this model we used fluorescence polarization and examined how the phosphorylation status of the proteins affects formation of the suggested ETR1-AHP1 signaling complex. We have employed various mutants of ETR1 and AHP1 mimicking permanent phosphorylation or preventing phosphorylation, respectively. Our results show that phosphorylation plays an important role in complex formation as affinity is dramatically reduced when the signaling partners are either both in their non-phosphorylated form or both in their phosphorylated form. On the other hand, affinity is greatly enhanced when either protein is in the phosphorylated state and the corresponding partner in its non-phosphorylated form. Our results indicate that interaction of ETR1 and AHP1 requires that ETR1 is a dimer, as in its functional state as receptor in planta.", "link"=>"http://www.mendeley.com/research/phosphorylation-alters-interaction-arabidopsis-phosphotransfer-protein-ahp1-sensor-kinase-etr1", "reader_count"=>22, "reader_count_by_academic_status"=>{"Professor > Associate Professor"=>1, "Librarian"=>1, "Researcher"=>4, "Student > Doctoral Student"=>2, "Student > Ph. D. Student"=>9, "Student > Postgraduate"=>1, "Student > Master"=>2, "Student > Bachelor"=>2}, "reader_count_by_user_role"=>{"Professor > Associate Professor"=>1, "Librarian"=>1, "Researcher"=>4, "Student > Doctoral Student"=>2, "Student > Ph. D. Student"=>9, "Student > Postgraduate"=>1, "Student > Master"=>2, "Student > Bachelor"=>2}, "reader_count_by_subject_area"=>{"Biochemistry, Genetics and Molecular Biology"=>3, "Agricultural and Biological Sciences"=>17, "Arts and Humanities"=>1, "Chemistry"=>1}, "reader_count_by_subdiscipline"=>{"Chemistry"=>{"Chemistry"=>1}, "Agricultural and Biological Sciences"=>{"Agricultural and Biological Sciences"=>17}, "Biochemistry, Genetics and Molecular Biology"=>{"Biochemistry, Genetics and Molecular Biology"=>3}, "Arts and Humanities"=>{"Arts and Humanities"=>1}}, "reader_count_by_country"=>{"United States"=>1, "United Kingdom"=>1, "Italy"=>1}, "group_count"=>3}

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Figshare

  • {"files"=>["https://ndownloader.figshare.com/files/738746"], "description"=>"<p>Measurements were performed in a buffer containing 50 mM Tris-HCl pH 7.5, 100 mM potassium chloride, 0.1% (w/v) β-D-dodecylmaltoside and 0.002% (w/v) phenylmethylsulfonyl fluoride at temperatures between 10°C and 30°C and glycerol concentrations of 10% (w/v) (Δ) and 20% (w/v) (▴). Closed circles (•) correspond to measurements at 0% (w/v) glycerol. At these conditions an increase in the molecular volume of the GFP-fusion protein is observed at temperatures below 17°C probably due to protein aggregation.</p>", "links"=>[], "tags"=>["purified", "recombinant"], "article_id"=>409122, "categories"=>["Biochemistry", "Biophysics", "Plant Biology"], "users"=>["Benjamin Scharein", "Georg Groth"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0024173.g003", "stats"=>{"downloads"=>0, "page_views"=>1, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Perrin_plot_analysis_of_purified_recombinant_AHP1_GFP_/409122", "title"=>"Perrin plot analysis of purified recombinant AHP1-GFP.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2011-09-02 02:32:02"}
  • {"files"=>["https://ndownloader.figshare.com/files/738812"], "description"=>"<p>Purified proteins were dansylated and fluorescence anisotropy was recorded in 0.2 M potassium phosphate pH 8.0, 0.05% (w/v) β-D-dodecylmaltoside and 10 mM β-cyclodextrin at temperatures between 5°C and 25°C. Curves correspond to data obtained with 0.2 µM dansylated AHP1 (•), 0.2 µM dansylated ETR1 (○) and 2 µM ETR1 together with 0.2 µM dansylated AHP1 (▴).</p>", "links"=>[], "tags"=>["recombinant", "ahp1"], "article_id"=>409190, "categories"=>["Biochemistry", "Biophysics", "Plant Biology"], "users"=>["Benjamin Scharein", "Georg Groth"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0024173.g004", "stats"=>{"downloads"=>1, "page_views"=>4, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Perrin_plot_analysis_of_recombinant_ETR1_AHP1_and_ETR1_8722_AHP1_complex_/409190", "title"=>"Perrin plot analysis of recombinant ETR1, AHP1 and ETR1−AHP1 complex.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2011-09-02 02:33:10"}
  • {"files"=>["https://ndownloader.figshare.com/files/373668"], "description"=>"<div><p>The ethylene receptor ethylene response 1 (ETR1) and the <em>Arabidopsis</em> histidine-containing phosphotransfer protein 1 (AHP1) form a tight complex <em>in vitro</em>. According to our current model ETR1 and AHP1 together with a response regulator form a phosphorelay system controlling the gene expression response to the plant hormone ethylene, similar to the two-component signaling in bacteria. The model implies that ETR1 functions as a sensor kinase and is autophosphorylated in the absence of ethylene. The phosphoryl group is then transferred onto a histidine at the canonical phosphorylation site in AHP1. For phosphoryl group transfer both binding partners need to form a tight complex. After ethylene binding the receptor is switched to the non-phosphorylated state. This switch is accompanied by a conformational change that decreases the affinity to the phosphorylated AHP1. To test this model we used fluorescence polarization and examined how the phosphorylation status of the proteins affects formation of the suggested ETR1−AHP1 signaling complex. We have employed various mutants of ETR1 and AHP1 mimicking permanent phosphorylation or preventing phosphorylation, respectively. Our results show that phosphorylation plays an important role in complex formation as affinity is dramatically reduced when the signaling partners are either both in their non-phosphorylated form or both in their phosphorylated form. On the other hand, affinity is greatly enhanced when either protein is in the phosphorylated state and the corresponding partner in its non-phosphorylated form. Our results indicate that interaction of ETR1 and AHP1 requires that ETR1 is a dimer, as in its functional state as receptor <em>in planta</em>.</p> </div>", "links"=>[], "tags"=>["phosphorylation", "alters", "arabidopsis", "phosphotransfer", "ahp1", "kinase", "etr1"], "article_id"=>133799, "categories"=>["Biochemistry", "Biophysics", "Cell Biology"], "users"=>["Benjamin Scharein", "Georg Groth"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0024173", "stats"=>{"downloads"=>2, "page_views"=>19, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/Phosphorylation_Alters_the_Interaction_of_the_Arabidopsis_Phosphotransfer_Protein_AHP1_with_Its_Sensor_Kinase_ETR1/133799", "title"=>"Phosphorylation Alters the Interaction of the Arabidopsis Phosphotransfer Protein AHP1 with Its Sensor Kinase ETR1", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2011-09-02 01:03:19"}
  • {"files"=>["https://ndownloader.figshare.com/files/738694"], "description"=>"<p>Measurements were done in the presence of 100 µM ethephon (•) or 100 µM potassium cyanide (○). In a control experiment (▴) the cofactor copper essential for ethylene binding was omitted. The dashed grey curve (—) represents a fit to these data according to Equation 2 corresponding to a dissociation constant of 1.4 µM <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0024173#pone.0024173-Scharein1\" target=\"_blank\">[18]</a>. Binding curves fitted to the experimental data obtained in the presence of ethephon (——) or in the presence of cyanide (——) correspond to dissociation constants of 7.7 µM and 9 µM, respectively.</p>", "links"=>[], "tags"=>["curves", "kinase", "etr1", "histidine"], "article_id"=>409067, "categories"=>["Biochemistry", "Biophysics", "Plant Biology"], "users"=>["Benjamin Scharein", "Georg Groth"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0024173.g002", "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Binding_curves_of_the_sensor_kinase_ETR1_and_histidine_transfer_protein_AHP1_/409067", "title"=>"Binding curves of the sensor kinase ETR1 and histidine transfer protein AHP1.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2011-09-02 02:31:07"}
  • {"files"=>["https://ndownloader.figshare.com/files/738891"], "description"=>"<p>A structural model of AHP1 was built using <i>MODELLER </i><a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0024173#pone.0024173-Sali1\" target=\"_blank\">[44]</a> interfaced by <i>EASYMODELLER </i><a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0024173#pone.0024173-Kuntal1\" target=\"_blank\">[45]</a> with default options using the 3D structure of the histidine-containing phosphotransfer protein OsHP1, from rice (PDB code 1YVI). In this method the 3D-structure is generated in such a way that a set of spatial and empirically determined restraints are optimally satisfied. Electrostatic potentials for this model were calculated using <i>PDB2PQR </i><a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0024173#pone.0024173-Dolinsky1\" target=\"_blank\">[46]</a> and <i>APBS </i><a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0024173#pone.0024173-Baker1\" target=\"_blank\">[47]</a>. Images were generated with <i>PyMOL </i><a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0024173#pone.0024173-DeLano1\" target=\"_blank\">[48]</a>. Solvent-accessible surface is colored according to the electrostatic potential [−5 kT/e red, +5 kT/e blue]. (A) and (C) side view, (B) and (D) top view. Catalytic residue H79 and residues defining the negative (residues D40-D65) and positive electrostatic surface potential (residues R114-K135) are labelled.</p>", "links"=>[], "tags"=>["histidine", "phospho-transfer"], "article_id"=>409269, "categories"=>["Biochemistry", "Biophysics", "Plant Biology"], "users"=>["Benjamin Scharein", "Georg Groth"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0024173.g005", "stats"=>{"downloads"=>1, "page_views"=>11, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Electrostatic_surface_potential_of_the_histidine_phospho_transfer_protein_AHP1_/409269", "title"=>"Electrostatic surface potential of the histidine phospho-transfer protein AHP1.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2011-09-02 02:34:29"}
  • {"files"=>["https://ndownloader.figshare.com/files/738644"], "description"=>"<p>Purified recombinant ETR1(D659A) or ETR1(D659E) at concentrations from 0.04 µM to 20 µM were added to 8 nM fluorescent AHP1-GFP(S65T) in a medium consisting of 50 mM Tris-HCl pH 7.5, 100 mM potassium chloride, 0.1% (w/v) β-D-dodecylmaltoside and 0.002% (w/v) phenylmethylsulfonyl fluoride. For the fluorescent AHP1 either non-phosphorylatable mutant AHP1(H79A)-GFP(S65T) or mutant AHP1(H79E)-GFP(S65T) mimicking permanent phosphorylation were used. Dissociation constants of the mutant ETR1−AHP1 complexes were calculated from the binding curves by Equation 2. ETR1(D659A) and AHP1(H79E)-GFP(S65T) show a K<sub>d</sub> of 3.6 µM (Δ,——), ETR1(D659E) and AHP1(H79A)-GFP(S65T) a K<sub>d</sub> of 2.6 µM (▴,——), ETR1(D659E) and AHP1(H79E)-GFP(S65T) a K<sub>d</sub> of 16.3 µM (•,——) and ETR1(D659A) and AHP1(H79A)-GFP(S65T) a K<sub>d</sub> of 15.4 µM (○,——). The dashed grey curve (—) corresponds to the binding characteristics of wild type ETR1 and wild type AHP1 <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0024173#pone.0024173-Scharein1\" target=\"_blank\">[18]</a>.</p>", "links"=>[], "tags"=>["curves", "phosphorylation", "mutants", "kinase", "etr1", "histidine"], "article_id"=>409014, "categories"=>["Biochemistry", "Biophysics", "Plant Biology"], "users"=>["Benjamin Scharein", "Georg Groth"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0024173.g001", "stats"=>{"downloads"=>3, "page_views"=>6, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Binding_curves_of_phosphorylation_mutants_of_the_sensor_kinase_ETR1_and_the_histidine_transfer_protein_AHP1_/409014", "title"=>"Binding curves of phosphorylation mutants of the sensor kinase ETR1 and the histidine transfer protein AHP1.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2011-09-02 02:30:14"}
  • {"files"=>["https://ndownloader.figshare.com/files/739081"], "description"=>"<p>Oligonucleotides used for mutagenesis.</p>", "links"=>[], "tags"=>["plant biology", "biophysics", "Biochemistry"], "article_id"=>409464, "categories"=>["Biochemistry", "Biophysics", "Plant Biology"], "users"=>["Benjamin Scharein", "Georg Groth"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0024173.t001", "stats"=>{"downloads"=>1, "page_views"=>4, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Oligonucleotides_used_for_mutagenesis_/409464", "title"=>"Oligonucleotides used for mutagenesis.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2011-09-02 02:37:44"}
  • {"files"=>["https://ndownloader.figshare.com/files/739001"], "description"=>"<p>In the absence of ethylene autophosphorylation of the sensor kinase ETR1 ensures low affinity of the receptor to phosphorylated HPt proteins. On the other hand, non-phosphorylated AHP1 binds to the phosphorylated ETR1 receptor with high affinity enabling phosphoryl group transfer to the HPt protein. After ethylene binding the receptor is switched to the non-phosphorylated state. This switch is accompanied by a conformational change that decreases the affinity to the phosphorylated AHP1. The transfer protein, AHP1-P is released and can move to the nucleus for further signal transfer onto response regulator proteins causing gene response. Binding of non-phosphorylated AHP1 to the activated form of the receptor is prevented by the conformational change caused in the receiver domain of the receptor by the binding of the plant hormone.</p>", "links"=>[], "tags"=>["plant biology", "biophysics", "Biochemistry"], "article_id"=>409375, "categories"=>["Biochemistry", "Biophysics", "Plant Biology"], "users"=>["Benjamin Scharein", "Georg Groth"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0024173.g006", "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Schematic_model_of_ETR1_8722_AHP1_signaling_/409375", "title"=>"Schematic model of ETR1−AHP1 signaling.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2011-09-02 02:36:15"}

PMC Usage Stats | Further Information

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  • {"unique-ip"=>"5", "full-text"=>"7", "pdf"=>"0", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"1", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2016", "month"=>"11"}
  • {"unique-ip"=>"3", "full-text"=>"1", "pdf"=>"0", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"1", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2017", "month"=>"1"}

Relative Metric

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