Single-Molecule Fluorescence Polarization Study of Conformational Change in Archaeal Group II Chaperonin
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{"title"=>"Single-molecule fluorescence polarization study of conformational change in archaeal group II chaperonin", "type"=>"journal", "authors"=>[{"first_name"=>"Ryo", "last_name"=>"Iizuka", "scopus_author_id"=>"7103075261"}, {"first_name"=>"Taro", "last_name"=>"Ueno", "scopus_author_id"=>"8972656100"}, {"first_name"=>"Nobuhiro", "last_name"=>"Morone", "scopus_author_id"=>"7801571227"}, {"first_name"=>"Takashi", "last_name"=>"Funatsu", "scopus_author_id"=>"7006109555"}], "year"=>2011, "source"=>"PLoS ONE", "identifiers"=>{"sgr"=>"79960303392", "doi"=>"10.1371/journal.pone.0022253", "pui"=>"362137061", "pmid"=>"21779405", "scopus"=>"2-s2.0-79960303392", "issn"=>"19326203"}, "id"=>"4279e037-c994-3a16-a101-7e579bab2aec", "abstract"=>"Group II chaperonins found in archaea and in eukaryotic cytosol mediate protein folding without a GroES-like cofactor. The function of the cofactor is substituted by the helical protrusion at the tip of the apical domain, which forms a built-in lid on the central cavity. Although many studies on the change in lid conformation coupled to the binding and hydrolysis of nucleotides have been conducted, the molecular mechanism of lid closure remains poorly understood. Here, we performed a single-molecule polarization modulation to probe the rotation of the helical protrusion of a chaperonin from a hyperthermophilic archaeum, Thermococcus sp. strain KS-1. We detected approximately 35° rotation of the helical protrusion immediately after photorelease of ATP. The result suggests that the conformational change from the open lid to the closed lid state is responsible for the approximately 35° rotation of the helical protrusion.", "link"=>"http://www.mendeley.com/research/singlemolecule-fluorescence-polarization-study-conformational-change-archaeal-group-ii-chaperonin-3", "reader_count"=>19, "reader_count_by_academic_status"=>{"Professor > Associate Professor"=>2, "Researcher"=>6, "Student > Doctoral Student"=>1, "Student > Ph. D. Student"=>5, "Student > Master"=>3, "Student > Bachelor"=>1, "Professor"=>1}, "reader_count_by_user_role"=>{"Professor > Associate Professor"=>2, "Researcher"=>6, "Student > Doctoral Student"=>1, "Student > Ph. D. Student"=>5, "Student > Master"=>3, "Student > Bachelor"=>1, "Professor"=>1}, "reader_count_by_subject_area"=>{"Biochemistry, Genetics and Molecular Biology"=>4, "Agricultural and Biological Sciences"=>11, "Physics and Astronomy"=>2, "Chemistry"=>2}, "reader_count_by_subdiscipline"=>{"Chemistry"=>{"Chemistry"=>2}, "Physics and Astronomy"=>{"Physics and Astronomy"=>2}, "Agricultural and Biological Sciences"=>{"Agricultural and Biological Sciences"=>11}, "Biochemistry, Genetics and Molecular Biology"=>{"Biochemistry, Genetics and Molecular Biology"=>4}}, "reader_count_by_country"=>{"Korea (South)"=>1, "Japan"=>3, "United Kingdom"=>1}, "group_count"=>1}

Scopus | Further Information

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Figshare

  • {"files"=>["https://ndownloader.figshare.com/files/756983"], "description"=>"<p>(<b>A</b>, <b>C</b>) Time trajectory of BSR intensity in the absence (<b>A</b>) and presence of caged ATP (<b>C</b>). The UV flash occurred at 30 s (<i>arrow</i>). The trajectories of BSR intensities after subtracting the background signals were averaged over every five frames, and fitted to a quadratic cosine function (<i>solid lines</i>). <i>Black</i>, fluorescence intensity before UV flash; <i>blue</i>, fluorescence intensity after UV flash. (<b>B</b>, <b>D</b>) Distributions of Δ<i>θ</i> in the absence (<b>B</b>) and presence of caged ATP (<b>D</b>). <i>Positive angle</i>, angular displacement measured counterclockwise; <i>negative angle</i>, angular displacement measured clockwise. In the absence of caged ATP (<b>B</b>), the distribution corresponded to a Gaussian distribution with a peak of −0.42°. In the presence of caged ATP (<b>D</b>), the distribution can be fitted by a sum of three Gaussian functions, with peaks of 1.8°, 34°, and −35°.</p>", "links"=>[], "tags"=>["trajectories", "fluorescence", "calculated", "fluorophore"], "article_id"=>427352, "categories"=>["Biotechnology", "Biochemistry", "Biophysics"], "users"=>["Ryo Iizuka", "Taro Ueno", "Nobuhiro Morone", "Takashi Funatsu"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0022253.g004", "stats"=>{"downloads"=>1, "page_views"=>5, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Time_trajectories_of_the_fluorescence_intensity_and_calculated_fluorophore_angles_/427352", "title"=>"Time trajectories of the fluorescence intensity and calculated fluorophore angles.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2011-07-14 02:02:32"}
  • {"files"=>["https://ndownloader.figshare.com/files/756802"], "description"=>"<p>Optical paths for different wavelengths are distinguished by their colors. The polarization of excitation laser (<i>green</i>) was continuously modulated by a polarizer mounted on a motorized rotary holder. The polarizer was rotated at 20.01°/s. Fluorescence (<i>orange</i>) was collected through an objective, and detected with an electron multiplying charge-coupled device camera. Caged ATP was photolyzed by UV light from a Hg–Xe lamp (<i>purple</i>). BSR-CPN was directly immobilized onto the surface. ND, neutral density filter; BE, beam expander; P, polarizer; λ/4, quarter wave plate; RP, rotating polarizer; DM, dichroic mirror; EF, emission filter; UVF, UV sharp-cut filter. The figure in the ellipse connotes a specimen for microscopic observation. BSR (<i>pink star</i>) was excited using an epi-illumination configuration.</p>", "links"=>[], "tags"=>["microscopic", "modulating", "excitation"], "article_id"=>427176, "categories"=>["Biotechnology", "Biochemistry", "Biophysics"], "users"=>["Ryo Iizuka", "Taro Ueno", "Nobuhiro Morone", "Takashi Funatsu"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0022253.g003", "stats"=>{"downloads"=>0, "page_views"=>2, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Schematic_drawing_of_the_microscopic_system_for_modulating_the_excitation_polarization_/427176", "title"=>"Schematic drawing of the microscopic system for modulating the excitation polarization.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2011-07-14 01:59:36"}
  • {"files"=>["https://ndownloader.figshare.com/files/756717"], "description"=>"<p>(A) With immobilized chaperonin. The boxed area in the <i>upper panel</i> is enlarged in the <i>lower panel</i>. The particles comprise almost exclusively ring-shaped end-on views (<i>black arrowheads</i>). The white arrowhead indicates a cluster of glycerol. (B) Without immobilized chaperonin. The scale bars represent 100 nm.</p>", "links"=>[], "tags"=>["electron", "micrograph", "chaperonin", "immobilized", "coverslip"], "article_id"=>427088, "categories"=>["Biotechnology", "Biochemistry", "Biophysics"], "users"=>["Ryo Iizuka", "Taro Ueno", "Nobuhiro Morone", "Takashi Funatsu"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0022253.g002", "stats"=>{"downloads"=>0, "page_views"=>9, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Rotary_shadowed_electron_micrograph_of_chaperonin_immobilized_onto_the_coverslip_surface_/427088", "title"=>"Rotary-shadowed electron micrograph of chaperonin immobilized onto the coverslip surface.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2011-07-14 01:58:08"}
  • {"files"=>["https://ndownloader.figshare.com/files/756637"], "description"=>"<p>(<b>A</b>) Subunit structure of <i>T</i>. KS-1 α chaperonin. The subunit has three distinct domains: equatorial (<i>red</i>), intermediate (<i>blue</i>), and apical (<i>green</i> and <i>yellow</i>). The helical protrusion is color-coded in <i>yellow</i>. Asp-263 and Gln-271 (<i>black arrowheads</i>) were mutated to cysteines, and were crosslinked with a bifunctional fluorophore. A His-tag was inserted into the loop, connecting the equatorial and intermediate domains (<i>white arrowhead</i>). The coordinates are from the Protein Data Bank code 1Q3S <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0022253#pone.0022253-Shomura1\" target=\"_blank\">[12]</a>, and figures were drawn with the PyMOL program (<a href=\"http://pymol.sourceforge.net/\" target=\"_blank\">http://pymol.sourceforge.net/</a>). (<b>B</b>) Model for the conformational transition from the open lid to the closed lid state in the group II chaperonins <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0022253#pone.0022253-Pereira1\" target=\"_blank\">[13]</a>, <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0022253#pone.0022253-Huo1\" target=\"_blank\">[14]</a>, <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0022253#pone.0022253-Zhang1\" target=\"_blank\">[22]</a>. ATP drives the conformational change from the open lid to the closed lid state. At this point, the counterclockwise rotation of the apical domains (<i>green</i>) orients the helical protrusions (<i>yellow</i>) toward the center of the cavity. (<b>C</b>) Expected intensity time courses for a single fluorophore bound to the helical protrusion. When a fluorophore is immobile, the fluorescence intensity oscillates as the excitation polarization is rotated (<i>red curve</i>). A phase shift is expected after reorientation of the fluorophore as a result of the rotation of the helical protrusion. (<b>D</b>) Structure of bis-((<i>N</i>-iodoacetyl)piperazinyl)sulfonerhodamine (BSR).</p>", "links"=>[], "tags"=>["conformational", "ii", "chaperonins"], "article_id"=>427005, "categories"=>["Biotechnology", "Biochemistry", "Biophysics"], "users"=>["Ryo Iizuka", "Taro Ueno", "Nobuhiro Morone", "Takashi Funatsu"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0022253.g001", "stats"=>{"downloads"=>1, "page_views"=>15, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Model_for_the_conformational_transition_from_the_open_lid_to_the_closed_lid_state_in_group_II_chaperonins_and_experimental_design_/427005", "title"=>"Model for the conformational transition from the open lid to the closed lid state in group II chaperonins and experimental design.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2011-07-14 01:56:45"}
  • {"files"=>["https://ndownloader.figshare.com/files/757033"], "description"=>"<p>ATP induces the conformational change from the open lid to the closed lid state, which is responsible for a approximately 35° counterclockwise rotation of the helical protrusion.</p>", "links"=>[], "tags"=>["ks-1", "chaperonin"], "article_id"=>427416, "categories"=>["Biotechnology", "Biochemistry", "Biophysics"], "users"=>["Ryo Iizuka", "Taro Ueno", "Nobuhiro Morone", "Takashi Funatsu"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0022253.g005", "stats"=>{"downloads"=>0, "page_views"=>1, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Conformational_change_of_T_KS_1_chaperonin_subunits_/427416", "title"=>"Conformational change of <i>T</i>. KS-1 α chaperonin subunits.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2011-07-14 02:03:36"}
  • {"files"=>["https://ndownloader.figshare.com/files/380770", "https://ndownloader.figshare.com/files/380820", "https://ndownloader.figshare.com/files/380866", "https://ndownloader.figshare.com/files/380892"], "description"=>"<div><p>Group II chaperonins found in archaea and in eukaryotic cytosol mediate protein folding without a GroES-like cofactor. The function of the cofactor is substituted by the helical protrusion at the tip of the apical domain, which forms a built-in lid on the central cavity. Although many studies on the change in lid conformation coupled to the binding and hydrolysis of nucleotides have been conducted, the molecular mechanism of lid closure remains poorly understood. Here, we performed a single-molecule polarization modulation to probe the rotation of the helical protrusion of a chaperonin from a hyperthermophilic archaeum, <em>Thermococcus</em> sp. strain KS-1. We detected approximately 35° rotation of the helical protrusion immediately after photorelease of ATP. The result suggests that the conformational change from the open lid to the closed lid state is responsible for the approximately 35° rotation of the helical protrusion.</p> </div>", "links"=>[], "tags"=>["single-molecule", "fluorescence", "polarization", "conformational", "archaeal", "ii", "chaperonin"], "article_id"=>135233, "categories"=>["Biotechnology", "Biochemistry", "Biophysics"], "users"=>["Ryo Iizuka", "Taro Ueno", "Nobuhiro Morone", "Takashi Funatsu"], "doi"=>["https://dx.doi.org/10.1371/journal.pone.0022253.s001", "https://dx.doi.org/10.1371/journal.pone.0022253.s002", "https://dx.doi.org/10.1371/journal.pone.0022253.s003", "https://dx.doi.org/10.1371/journal.pone.0022253.s004"], "stats"=>{"downloads"=>4, "page_views"=>10, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/Single_Molecule_Fluorescence_Polarization_Study_of_Conformational_Change_in_Archaeal_Group_II_Chaperonin/135233", "title"=>"Single-Molecule Fluorescence Polarization Study of Conformational Change in Archaeal Group II Chaperonin", "pos_in_sequence"=>0, "defined_type"=>4, "published_date"=>"2011-07-14 01:27:13"}

PMC Usage Stats | Further Information

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Relative Metric

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