Common Evolutionary Origin for the Rotor Domain of Rotary Atpases and Flagellar Protein Export Apparatus
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{"title"=>"Common Evolutionary Origin for the Rotor Domain of Rotary Atpases and Flagellar Protein Export Apparatus", "type"=>"journal", "authors"=>[{"first_name"=>"Jun ichi", "last_name"=>"Kishikawa", "scopus_author_id"=>"35322447700"}, {"first_name"=>"Tatsuya", "last_name"=>"Ibuki", "scopus_author_id"=>"26021263400"}, {"first_name"=>"Shuichi", "last_name"=>"Nakamura", "scopus_author_id"=>"55468293100"}, {"first_name"=>"Astuko", "last_name"=>"Nakanishi", "scopus_author_id"=>"55751850300"}, {"first_name"=>"Tohru", "last_name"=>"Minamino", "scopus_author_id"=>"7006391123"}, {"first_name"=>"Tomoko", "last_name"=>"Miyata", "scopus_author_id"=>"7401764889"}, {"first_name"=>"Keiichi", "last_name"=>"Namba", "scopus_author_id"=>"7103162863"}, {"first_name"=>"Hiroki", "last_name"=>"Konno", "scopus_author_id"=>"7201803403"}, {"first_name"=>"Hiroshi", "last_name"=>"Ueno", "scopus_author_id"=>"55319125400"}, {"first_name"=>"Katsumi", "last_name"=>"Imada", "scopus_author_id"=>"7006628770"}, {"first_name"=>"Ken", "last_name"=>"Yokoyama", "scopus_author_id"=>"7401877239"}], "year"=>2013, "source"=>"PLoS ONE", "identifiers"=>{"pui"=>"369024933", "issn"=>"19326203", "doi"=>"10.1371/journal.pone.0064695", "scopus"=>"2-s2.0-84878377906", "pmid"=>"23724081", "sgr"=>"84878377906"}, "id"=>"81a526a7-1ba3-33d7-a644-b685b7616691", "abstract"=>"The V1- and F1- rotary ATPases contain a rotor that rotates against a catalytic A3B3 or α3β3 stator. The rotor F(1-γ) or V1-DF is composed of both anti-parallel coiled coil and globular-loop parts. The bacterial flagellar type III export apparatus contains a V1/F1-like ATPase ring structure composed of FliI6 homo-hexamer and FliJ which adopts an anti-parallel coiled coil structure without the globular-loop part. Here we report that FliJ of Salmonella enterica serovar Typhimurium shows a rotor like function in Thermus thermophilus A3B3 based on both biochemical and structural analysis. Single molecular analysis indicates that an anti-parallel coiled-coil structure protein (FliJ structure protein) functions as a rotor in A3B3. A rotary ATPase possessing an F1-γ-like protein generated by fusion of the D and F subunits of V1 rotates, suggesting F(1-γ) could be the result of a fusion of the genes encoding two separate rotor subunits. Together with sequence comparison among the globular part proteins, the data strongly suggest that the rotor domains of the rotary ATPases and the flagellar export apparatus share a common evolutionary origin.", "link"=>"http://www.mendeley.com/research/common-evolutionary-origin-rotor-domain-rotary-atpases-flagellar-protein-export-apparatus", "reader_count"=>32, "reader_count_by_academic_status"=>{"Unspecified"=>1, "Professor > Associate Professor"=>4, "Researcher"=>3, "Student > Ph. D. Student"=>13, "Student > Postgraduate"=>1, "Student > Master"=>4, "Student > Bachelor"=>3, "Professor"=>2}, "reader_count_by_user_role"=>{"Unspecified"=>1, "Professor > Associate Professor"=>4, "Researcher"=>3, "Student > Ph. D. Student"=>13, "Student > Postgraduate"=>1, "Student > Master"=>4, "Student > Bachelor"=>3, "Professor"=>2}, "reader_count_by_subject_area"=>{"Unspecified"=>1, "Biochemistry, Genetics and Molecular Biology"=>7, "Agricultural and Biological Sciences"=>16, "Medicine and Dentistry"=>2, "Physics and Astronomy"=>4, "Chemistry"=>1}, "reader_count_by_subdiscipline"=>{"Medicine and Dentistry"=>{"Medicine and Dentistry"=>2}, "Chemistry"=>{"Chemistry"=>1}, "Physics and Astronomy"=>{"Physics and Astronomy"=>4}, "Agricultural and Biological Sciences"=>{"Agricultural and Biological Sciences"=>16}, "Biochemistry, Genetics and Molecular Biology"=>{"Biochemistry, Genetics and Molecular Biology"=>7}, "Unspecified"=>{"Unspecified"=>1}}, "group_count"=>0}

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  • {"files"=>["https://ndownloader.figshare.com/files/1069022", "https://ndownloader.figshare.com/files/1069023", "https://ndownloader.figshare.com/files/1069024", "https://ndownloader.figshare.com/files/1069025", "https://ndownloader.figshare.com/files/1069026", "https://ndownloader.figshare.com/files/1069027"], "description"=>"<div><p>The V<sub>1</sub>- and F<sub>1</sub>- rotary ATPases contain a rotor that rotates against a catalytic A<sub>3</sub>B<sub>3</sub> or α<sub>3</sub>β<sub>3</sub> stator. The rotor F<sub>1</sub>-γ or V<sub>1</sub>-DF is composed of both anti-parallel coiled coil and globular-loop parts. The bacterial flagellar type III export apparatus contains a V<sub>1</sub>/F<sub>1</sub>-like ATPase ring structure composed of FliI<sub>6</sub> homo-hexamer and FliJ which adopts an anti-parallel coiled coil structure without the globular-loop part. Here we report that FliJ of <i>Salmonella enterica</i> serovar Typhimurium shows a rotor like function in <i>Thermus thermophilus</i> A<sub>3</sub>B<sub>3</sub> based on both biochemical and structural analysis. Single molecular analysis indicates that an anti-parallel coiled-coil structure protein (FliJ structure protein) functions as a rotor in A<sub>3</sub>B<sub>3</sub>. A rotary ATPase possessing an F<sub>1</sub>-γ-like protein generated by fusion of the D and F subunits of V<sub>1</sub> rotates, suggesting F<sub>1</sub>-γ could be the result of a fusion of the genes encoding two separate rotor subunits. Together with sequence comparison among the globular part proteins, the data strongly suggest that the rotor domains of the rotary ATPases and the flagellar export apparatus share a common evolutionary origin.</p> </div>", "links"=>[], "tags"=>["Biochemistry", "enzymes", "Enzyme structure", "proteins", "Protein chemistry", "protein structure", "biophysics", "Evolutionary biology", "microbiology", "bacteriology", "Bacterial biochemistry", "evolutionary", "rotor", "rotary", "atpases", "flagellar"], "article_id"=>707854, "categories"=>["Physics", "Biological Sciences"], "users"=>["Jun-ichi Kishikawa", "Tatsuya Ibuki", "Shuichi Nakamura", "Astuko Nakanishi", "Tohru Minamino", "Tomoko Miyata", "Keiichi Namba", "Hiroki Konno", "Hiroshi Ueno", "Katsumi Imada", "Ken Yokoyama"], "doi"=>["https://dx.doi.org/10.1371/journal.pone.0064695.s001", "https://dx.doi.org/10.1371/journal.pone.0064695.s002", "https://dx.doi.org/10.1371/journal.pone.0064695.s003", "https://dx.doi.org/10.1371/journal.pone.0064695.s004", "https://dx.doi.org/10.1371/journal.pone.0064695.s005", "https://dx.doi.org/10.1371/journal.pone.0064695.s006"], "stats"=>{"downloads"=>17, "page_views"=>7, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Common_Evolutionary_Origin_for_the_Rotor_Domain_of_Rotary_Atpases_and_Flagellar_Protein_Export_Apparatus_/707854", "title"=>"Common Evolutionary Origin for the Rotor Domain of Rotary Atpases and Flagellar Protein Export Apparatus", "pos_in_sequence"=>0, "defined_type"=>4, "published_date"=>"2013-05-28 02:10:54"}

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Relative Metric

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