Function of FlhB, a Membrane Protein Implicated in the Bacterial Flagellar Type III Secretion System
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{"title"=>"Function of FlhB, a Membrane Protein Implicated in the Bacterial Flagellar Type III Secretion System", "type"=>"journal", "authors"=>[{"first_name"=>"Vladimir A.", "last_name"=>"Meshcheryakov", "scopus_author_id"=>"36798332900"}, {"first_name"=>"Clive S.", "last_name"=>"Barker", "scopus_author_id"=>"8092935300"}, {"first_name"=>"Alla S.", "last_name"=>"Kostyukova", "scopus_author_id"=>"6701577562"}, {"first_name"=>"Fadel A.", "last_name"=>"Samatey", "scopus_author_id"=>"6602980345"}], "year"=>2013, "source"=>"PLoS ONE", "identifiers"=>{"pui"=>"369305016", "sgr"=>"84880072941", "issn"=>"19326203", "pmid"=>"23874605", "scopus"=>"2-s2.0-84880072941", "doi"=>"10.1371/journal.pone.0068384"}, "id"=>"c602084d-bf49-3b18-a90e-4c04fa8582ae", "abstract"=>"The membrane protein FlhB is a highly conserved component of the flagellar secretion system, and it plays an active role in the regulation of protein export. In this study conserved properties of FlhB that are important for its function were investigated. Replacing the flhB gene (or part of the gene) in Salmonella typhimurium with the flhB gene of the distantly related bacterium Aquifex aeolicus greatly reduces motility. However, motility can be restored to some extent by spontaneous mutations in the part of flhB gene coding for the cytoplasmic domain of Aquifex FlhB. Structural analysis suggests that these mutations destabilize the structure. The secondary structure and stability of the mutated cytoplasmic fragments of FlhB have been studied by circular dichroism spectroscopy. The results suggest that conformational flexibility could be important for FlhB function. An extragenic suppressor mutation in the fliS gene, which decreases the affinity of FliS to FliC, partially restores motility of the FlhB substitution mutants.", "link"=>"http://www.mendeley.com/research/function-flhb-membrane-protein-implicated-bacterial-flagellar-type-iii-secretion-system-1", "reader_count"=>14, "reader_count_by_academic_status"=>{"Unspecified"=>1, "Researcher"=>3, "Student > Ph. D. Student"=>3, "Student > Master"=>5, "Student > Bachelor"=>2}, "reader_count_by_user_role"=>{"Unspecified"=>1, "Researcher"=>3, "Student > Ph. D. Student"=>3, "Student > Master"=>5, "Student > Bachelor"=>2}, "reader_count_by_subject_area"=>{"Unspecified"=>1, "Environmental Science"=>1, "Biochemistry, Genetics and Molecular Biology"=>2, "Agricultural and Biological Sciences"=>9, "Chemistry"=>1}, "reader_count_by_subdiscipline"=>{"Chemistry"=>{"Chemistry"=>1}, "Agricultural and Biological Sciences"=>{"Agricultural and Biological Sciences"=>9}, "Biochemistry, Genetics and Molecular Biology"=>{"Biochemistry, Genetics and Molecular Biology"=>2}, "Unspecified"=>{"Unspecified"=>1}, "Environmental Science"=>{"Environmental Science"=>1}}, "group_count"=>0}

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Figshare

  • {"files"=>["https://ndownloader.figshare.com/files/1116982"], "description"=>"<p>(A) Ribbon diagram of <i>Aquifex</i> FlhB<sub>C</sub> with the suppressor mutations shown as sticks. Panels (B) to (E) show close-up views of the mutated residues and their surroundings.</p>", "links"=>[], "tags"=>["Biochemistry", "proteins", "Protein interactions", "protein structure", "Transmembrane proteins", "Macromolecular assemblies", "biophysics", "Cell motility", "Flagellar motility", "Protein chemistry", "Protein folding", "genetics", "gene expression", "Molecular genetics", "genomics", "Genome sequencing", "suppressor", "mutations", "accession"], "article_id"=>744064, "categories"=>["Physics", "Biological Sciences"], "users"=>["Vladimir A. Meshcheryakov", "Clive S. Barker", "Alla S. Kostyukova", "Fadel A. Samatey"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0068384.g006", "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Mapping_of_the_suppressor_mutations_in_Aquifex_FlhB_C_PDB_accession_code_3B1S_/744064", "title"=>"Mapping of the suppressor mutations in <i>Aquifex</i> FlhB<sub>C</sub> (PDB accession code: 3B1S).", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-07-11 02:14:30"}
  • {"files"=>["https://ndownloader.figshare.com/files/1116991"], "description"=>"a<p>Restriction sites are underlined.</p>", "links"=>[], "tags"=>["Biochemistry", "proteins", "Protein interactions", "protein structure", "Transmembrane proteins", "Macromolecular assemblies", "biophysics", "Cell motility", "Flagellar motility", "Protein chemistry", "Protein folding", "genetics", "gene expression", "Molecular genetics", "genomics", "Genome sequencing", "plasmid"], "article_id"=>744073, "categories"=>["Physics", "Biological Sciences"], "users"=>["Vladimir A. Meshcheryakov", "Clive S. Barker", "Alla S. Kostyukova", "Fadel A. Samatey"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0068384.t004", "stats"=>{"downloads"=>1, "page_views"=>7, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Oligonucleotides_used_in_the_strain_and_plasmid_constructions_/744073", "title"=>"Oligonucleotides used in the strain and plasmid constructions.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2013-07-11 02:14:30"}
  • {"files"=>["https://ndownloader.figshare.com/files/1116989"], "description"=>"a<p>CGSC, <i>Escherichia coli</i> Genetic Stock Center, Yale University, USA.</p>b<p>FBS, School of Frontier Biosciences, Osaka University, Japan.</p>c<p>SGSC, <i>Salmonella</i> Genetic Stock Centre, University of Calgary, Canada.</p>", "links"=>[], "tags"=>["Biochemistry", "proteins", "Protein interactions", "protein structure", "Transmembrane proteins", "Macromolecular assemblies", "biophysics", "Cell motility", "Flagellar motility", "Protein chemistry", "Protein folding", "genetics", "gene expression", "Molecular genetics", "genomics", "Genome sequencing"], "article_id"=>744071, "categories"=>["Physics", "Biological Sciences"], "users"=>["Vladimir A. Meshcheryakov", "Clive S. Barker", "Alla S. Kostyukova", "Fadel A. Samatey"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0068384.t002", "stats"=>{"downloads"=>1, "page_views"=>1, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Strains_used_in_this_study_/744071", "title"=>"Strains used in this study.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2013-07-11 02:14:30"}
  • {"files"=>["https://ndownloader.figshare.com/files/1116990"], "description"=>"<p>Secondary structure content of various FlhB<sub>C</sub>. Secondary structure content was calculated from the CD spectra using a multilinear regression <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0068384#pone.0068384-Greenfield1\" target=\"_blank\">[36]</a>.</p>", "links"=>[], "tags"=>["Biochemistry", "proteins", "Protein interactions", "protein structure", "Transmembrane proteins", "Macromolecular assemblies", "biophysics", "Cell motility", "Flagellar motility", "Protein chemistry", "Protein folding", "genetics", "gene expression", "Molecular genetics", "genomics", "Genome sequencing", "calculated", "cd", "spectra", "multilinear", "regression"], "article_id"=>744072, "categories"=>["Physics", "Biological Sciences"], "users"=>["Vladimir A. Meshcheryakov", "Clive S. Barker", "Alla S. Kostyukova", "Fadel A. Samatey"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0068384.t001", "stats"=>{"downloads"=>1, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Secondary_structure_content_of_various_FlhB_C_Secondary_structure_content_was_calculated_from_the_CD_spectra_using_a_multilinear_regression_36_/744072", "title"=>"Secondary structure content of various FlhB<sub>C</sub>. Secondary structure content was calculated from the CD spectra using a multilinear regression [36].", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2013-07-11 02:14:30"}
  • {"files"=>["https://ndownloader.figshare.com/files/1116971"], "description"=>"<p>Identical residues are shown with a teal background; similar residues are colored red. Suppressor mutations found in this study are marked by red stars (for point mutations) and black arrows (for frame shift mutations).</p>", "links"=>[], "tags"=>["Biochemistry", "proteins", "Protein interactions", "protein structure", "Transmembrane proteins", "Macromolecular assemblies", "biophysics", "Cell motility", "Flagellar motility", "Protein chemistry", "Protein folding", "genetics", "gene expression", "Molecular genetics", "genomics", "Genome sequencing", "alignment", "flhb"], "article_id"=>744053, "categories"=>["Physics", "Biological Sciences"], "users"=>["Vladimir A. Meshcheryakov", "Clive S. Barker", "Alla S. Kostyukova", "Fadel A. Samatey"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0068384.g001", "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Amino_acid_sequence_alignment_of_FlhB_from_S_typhimurium_SALTY_FlhB_and_A_aeolicus_AQUAE_FlhB_/744053", "title"=>"Amino acid sequence alignment of FlhB from <i>S. typhimurium</i> (SALTY_FlhB) and <i>A. aeolicus</i> (AQUAE_FlhB).", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-07-11 02:14:30"}
  • {"files"=>["https://ndownloader.figshare.com/files/1116988"], "description"=>"<p>CGSC, <i>Escherichia coli</i> Genetic Stock Center, Yale University, USA.</p>", "links"=>[], "tags"=>["Biochemistry", "proteins", "Protein interactions", "protein structure", "Transmembrane proteins", "Macromolecular assemblies", "biophysics", "Cell motility", "Flagellar motility", "Protein chemistry", "Protein folding", "genetics", "gene expression", "Molecular genetics", "genomics", "Genome sequencing"], "article_id"=>744070, "categories"=>["Physics", "Biological Sciences"], "users"=>["Vladimir A. Meshcheryakov", "Clive S. Barker", "Alla S. Kostyukova", "Fadel A. Samatey"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0068384.t003", "stats"=>{"downloads"=>1, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Plasmids_used_in_this_study_/744070", "title"=>"Plasmids used in this study.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2013-07-11 02:14:30"}
  • {"files"=>["https://ndownloader.figshare.com/files/1116985"], "description"=>"<p>Circular dichroism measurements of <i>Aquifex</i> FlhB<sub>C</sub>, <i>Aquifex</i> FlhB<sub>C</sub> mutants, and <i>Salmonella</i> FlhB<sub>C</sub>.</p>", "links"=>[], "tags"=>["Biochemistry", "proteins", "Protein interactions", "protein structure", "Transmembrane proteins", "Macromolecular assemblies", "biophysics", "Cell motility", "Flagellar motility", "Protein chemistry", "Protein folding", "genetics", "gene expression", "Molecular genetics", "genomics", "Genome sequencing", "dichroism"], "article_id"=>744067, "categories"=>["Physics", "Biological Sciences"], "users"=>["Vladimir A. Meshcheryakov", "Clive S. Barker", "Alla S. Kostyukova", "Fadel A. Samatey"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0068384.g008", "stats"=>{"downloads"=>1, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Circular_dichroism_measurements_of_Aquifex_FlhB_C_Aquifex_FlhB_C_mutants_and_Salmonella_FlhB_C_/744067", "title"=>"Circular dichroism measurements of <i>Aquifex</i> FlhB<sub>C</sub>, <i>Aquifex</i> FlhB<sub>C</sub> mutants, and <i>Salmonella</i> FlhB<sub>C</sub>.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-07-11 02:14:30"}
  • {"files"=>["https://ndownloader.figshare.com/files/1116984"], "description"=>"<p>Protein unfolding was monitored by ellipticity at 222 nm.</p>", "links"=>[], "tags"=>["Biochemistry", "proteins", "Protein interactions", "protein structure", "Transmembrane proteins", "Macromolecular assemblies", "biophysics", "Cell motility", "Flagellar motility", "Protein chemistry", "Protein folding", "genetics", "gene expression", "Molecular genetics", "genomics", "Genome sequencing", "denaturation"], "article_id"=>744066, "categories"=>["Physics", "Biological Sciences"], "users"=>["Vladimir A. Meshcheryakov", "Clive S. Barker", "Alla S. Kostyukova", "Fadel A. Samatey"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0068384.g007", "stats"=>{"downloads"=>1, "page_views"=>1, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Urea_denaturation_of_Salmonella_and_Aquifex_FlhB_C_and_various_Aquifex_FlhB_C_mutants_/744066", "title"=>"Urea denaturation of <i>Salmonella</i> and <i>Aquifex</i> FlhB<sub>C</sub> and various <i>Aquifex</i> FlhB<sub>C</sub> mutants.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-07-11 02:14:30"}
  • {"files"=>["https://ndownloader.figshare.com/files/1116979"], "description"=>"<p>Soft agar plate containing 0.1 mM IPTG was incubated at 30°C for 5 hours.</p>", "links"=>[], "tags"=>["Biochemistry", "proteins", "Protein interactions", "protein structure", "Transmembrane proteins", "Macromolecular assemblies", "biophysics", "Cell motility", "Flagellar motility", "Protein chemistry", "Protein folding", "genetics", "gene expression", "Molecular genetics", "genomics", "Genome sequencing", "motility", "wild-type", "sjw1103", "transformed", "plasmids", "encoding", "flhb"], "article_id"=>744061, "categories"=>["Physics", "Biological Sciences"], "users"=>["Vladimir A. Meshcheryakov", "Clive S. Barker", "Alla S. Kostyukova", "Fadel A. Samatey"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0068384.g004", "stats"=>{"downloads"=>5, "page_views"=>16, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Dominance_effect_on_motility_of_wild_type_Salmonella_strain_SJW1103_transformed_with_the_plasmids_encoding_different_FlhB_proteins_/744061", "title"=>"Dominance effect on motility of wild-type <i>Salmonella</i> strain SJW1103 transformed with the plasmids encoding different FlhB proteins.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-07-11 02:14:30"}
  • {"files"=>["https://ndownloader.figshare.com/files/1116974"], "description"=>"<p>(A) Motility of Δ<i>flhB Salmonella</i> strain transformed with plasmids coding for different variants of FlhB. The asterisk “*” marks the previous emplacement for the wild type strain that was removed because it would have overgrown after 46 hours. (B) Rescue of motility by mutations in the cytoplasmic domain of FlhB. The plates were incubated at 30°C for the indicated time. Indicated plasmids carry genes of the following proteins: wild-type SalFlhB (WT); AquFlhB (pTAB32); Sal/AquFlhB (pTB334); Sal/AquFlhB347 (pTB335); Sal/AquFlhB357 (pTB336); Sal/AquFlhB V341 frame-shift (pTB337); Sal/AquFlhB F343 frame-shift (pTB342); Sal/AquFlhB357 V259E (pTB341); Sal/AquFlhB347 F330L (pTB338); Sal/AquFlhB347 V307G (pTB339); Sal/AquFlhB347 ΔKG(288–289) (pTB340).</p>", "links"=>[], "tags"=>["Biochemistry", "proteins", "Protein interactions", "protein structure", "Transmembrane proteins", "Macromolecular assemblies", "biophysics", "Cell motility", "Flagellar motility", "Protein chemistry", "Protein folding", "genetics", "gene expression", "Molecular genetics", "genomics", "Genome sequencing", "motility"], "article_id"=>744056, "categories"=>["Physics", "Biological Sciences"], "users"=>["Vladimir A. Meshcheryakov", "Clive S. Barker", "Alla S. Kostyukova", "Fadel A. Samatey"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0068384.g003", "stats"=>{"downloads"=>4, "page_views"=>10, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Swimming_motility_assay_/744056", "title"=>"Swimming motility assay.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-07-11 02:14:30"}
  • {"files"=>["https://ndownloader.figshare.com/files/1116987"], "description"=>"<p>FliS (or FliS A22T) of various concentrations was flowed over the sensor surface with immobilized ligand (AquFlhB<sub>C</sub> or FliC) in Biacore buffer (10 mM HEPES pH 7.4, 150 mM NaCl, 0.05% (v/v) Surfactant P20). Response at steady state was plotted against analyte concentration. K<sub>D</sub> is measured as the protein concentration that gives response equal to 50% saturation.</p>", "links"=>[], "tags"=>["Biochemistry", "proteins", "Protein interactions", "protein structure", "Transmembrane proteins", "Macromolecular assemblies", "biophysics", "Cell motility", "Flagellar motility", "Protein chemistry", "Protein folding", "genetics", "gene expression", "Molecular genetics", "genomics", "Genome sequencing", "plasmon", "resonance", "flis", "binding"], "article_id"=>744069, "categories"=>["Physics", "Biological Sciences"], "users"=>["Vladimir A. Meshcheryakov", "Clive S. Barker", "Alla S. Kostyukova", "Fadel A. Samatey"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0068384.g010", "stats"=>{"downloads"=>1, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Steady_state_surface_plasmon_resonance_analysis_of_FliS_binding_to_Aquifex_FlhB_C_and_FliC_/744069", "title"=>"Steady-state surface plasmon resonance analysis of FliS binding to <i>Aquifex</i> FlhB<sub>C</sub> and FliC.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-07-11 02:14:30"}
  • {"files"=>["https://ndownloader.figshare.com/files/1116972"], "description"=>"<p>Black and white bars indicate the <i>Salmonella</i> and <i>Aquifex</i> parts of FlhB, respectively. Triangles mark the positions of point and deletion suppressor mutations. Numbers in parentheses show the total number of amino acids in each protein.</p>", "links"=>[], "tags"=>["Biochemistry", "proteins", "Protein interactions", "protein structure", "Transmembrane proteins", "Macromolecular assemblies", "biophysics", "Cell motility", "Flagellar motility", "Protein chemistry", "Protein folding", "genetics", "gene expression", "Molecular genetics", "genomics", "Genome sequencing", "representations", "flhb", "encoded", "plasmids", "motility"], "article_id"=>744054, "categories"=>["Physics", "Biological Sciences"], "users"=>["Vladimir A. Meshcheryakov", "Clive S. Barker", "Alla S. Kostyukova", "Fadel A. Samatey"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0068384.g002", "stats"=>{"downloads"=>1, "page_views"=>4, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Schematic_representations_of_FlhB_products_encoded_by_the_plasmids_used_for_the_motility_assay_/744054", "title"=>"Schematic representations of FlhB products encoded by the plasmids used for the motility assay.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-07-11 02:14:30"}
  • {"files"=>["https://ndownloader.figshare.com/files/1116986"], "description"=>"<p>Cells were transformed with pTrc99A-based plasmids encoding various FlhB proteins. Soft agar plates were incubated at 30°C for the indicated time. (A) Motility of Δ<i>flhB Salmonella</i> strains producing Sal/AquFlhB F343 frame shift. One of the strains contains additional mutation in <i>fliS</i>. 1 - empty vector, 2 - wild type <i>Salmonella</i> FlhB, 3 - Sal/AquFlhB F343 frame shift, 4 - Sal/AquFlhB F343 frame shift plus FliS (A22T). The asterisk “*” marks the previous emplacement for the wild type strain that was removed because it would have overgrown after 20 hours. (B) Comparison of the motility of Δ<i>flhB</i> and Δ<i>flhB fliS</i>(A22T) <i>Salmonella</i> strains producing different FlhB variants.</p>", "links"=>[], "tags"=>["Biochemistry", "proteins", "Protein interactions", "protein structure", "Transmembrane proteins", "Macromolecular assemblies", "biophysics", "Cell motility", "Flagellar motility", "Protein chemistry", "Protein folding", "genetics", "gene expression", "Molecular genetics", "genomics", "Genome sequencing", "mutation", "motility"], "article_id"=>744068, "categories"=>["Physics", "Biological Sciences"], "users"=>["Vladimir A. Meshcheryakov", "Clive S. Barker", "Alla S. Kostyukova", "Fadel A. Samatey"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0068384.g009", "stats"=>{"downloads"=>1, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Effect_of_fliS_mutation_on_motility_of_Salmonella_cells_/744068", "title"=>"Effect of <i>fliS</i> mutation on motility of <i>Salmonella</i> cells.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-07-11 02:14:30"}
  • {"files"=>["https://ndownloader.figshare.com/files/1116981"], "description"=>"<p>Cells carrying the plasmids encoding different FlhB proteins were grown at 37°C until OD<sub>600</sub> = 0.5–0.6. Protein expression was induced by 0.1 mM IPTG. After 2 hours cells were harvested by centrifugation and analyzed by immunoblotting using polyclonal antibodies against full-length <i>Aquifex</i> and <i>Salmonella</i> FlhB.</p>", "links"=>[], "tags"=>["Biochemistry", "proteins", "Protein interactions", "protein structure", "Transmembrane proteins", "Macromolecular assemblies", "biophysics", "Cell motility", "Flagellar motility", "Protein chemistry", "Protein folding", "genetics", "gene expression", "Molecular genetics", "genomics", "Genome sequencing"], "article_id"=>744063, "categories"=>["Physics", "Biological Sciences"], "users"=>["Vladimir A. Meshcheryakov", "Clive S. Barker", "Alla S. Kostyukova", "Fadel A. Samatey"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0068384.g005", "stats"=>{"downloads"=>1, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Autocleavage_properties_of_FlhB_/744063", "title"=>"Autocleavage properties of FlhB.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-07-11 02:14:30"}

PMC Usage Stats | Further Information

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Relative Metric

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