An allele of an ancestral transcription factor dependent on a horizontally acquired gene product
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{"title"=>"An Allele of an Ancestral Transcription Factor Dependent on a Horizontally Acquired Gene Product", "type"=>"journal", "authors"=>[{"first_name"=>"H. Deborah", "last_name"=>"Chen", "scopus_author_id"=>"48760939500"}, {"first_name"=>"Mollie W.", "last_name"=>"Jewett", "scopus_author_id"=>"13612896700"}, {"first_name"=>"Eduardo A.", "last_name"=>"Groisman", "scopus_author_id"=>"35586565400"}], "year"=>2012, "source"=>"PLoS Genetics", "identifiers"=>{"issn"=>"15537390", "sgr"=>"84872015960", "scopus"=>"2-s2.0-84872015960", "pui"=>"368067322", "doi"=>"10.1371/journal.pgen.1003060", "pmid"=>"23300460"}, "id"=>"3e6463a0-c0b7-3355-abd0-0ee6bcf15e20", "abstract"=>"<title>Author Summary</title><p>Horizontally acquired genes are typically viewed as independent units that confer new traits when introduced into different bacterial species. However, preexisting proteins in a bacterium can impact the ability of horizontally acquired gene products to bring about new functions when they target ancestral pathways. Here, we establish that a single amino acid difference in the ancestral transcription factor PmrA alters its dependence on the horizontally acquired gene product PmrD to promote gene expression within closely related <italic>Salmonella</italic> serovars. Consequently, <italic>S. enterica</italic> serovar Typhimurium, which infects a wide range of animals, expresses PmrA-dependent genes and displays antibiotic resistance in conditions that activate the PmrA and/or PmrD proteins. By contrast, the human-adapted <italic>S. enterica</italic> serovar Paratyphi B only does so in the presence of both PmrA- and PmrD-activating conditions. Bacteria harboring the Paratyphi B <italic>pmrA</italic> gene also exhibited enhanced biofilm formation, which may contribute to serovar Paratyphi B's persistent infection of the gallbladder. Our findings demonstrate that the ability of horizontally acquired genes to confer new traits can be affected by ancestral proteins, even within one bacterial species. Therefore, a protein's function in a given organism must be appreciated in the context of other proteins operating within the same genetic network.</p>", "link"=>"http://www.mendeley.com/research/allele-ancestral-transcription-factor-dependent-horizontally-acquired-gene-product", "reader_count"=>23, "reader_count_by_academic_status"=>{"Professor > Associate Professor"=>1, "Researcher"=>5, "Student > Doctoral Student"=>1, "Student > Ph. D. Student"=>5, "Student > Master"=>4, "Other"=>2, "Student > Bachelor"=>2, "Professor"=>2, "Student > Postgraduate"=>1}, "reader_count_by_user_role"=>{"Professor > Associate Professor"=>1, "Researcher"=>5, "Student > Doctoral Student"=>1, "Student > Ph. D. Student"=>5, "Student > Master"=>4, "Other"=>2, "Student > Bachelor"=>2, "Professor"=>2, "Student > Postgraduate"=>1}, "reader_count_by_subject_area"=>{"Biochemistry, Genetics and Molecular Biology"=>5, "Agricultural and Biological Sciences"=>15, "Medicine and Dentistry"=>1, "Veterinary Science and Veterinary Medicine"=>1, "Immunology and Microbiology"=>1}, "reader_count_by_subdiscipline"=>{"Medicine and Dentistry"=>{"Medicine and Dentistry"=>1}, "Immunology and Microbiology"=>{"Immunology and Microbiology"=>1}, "Agricultural and Biological Sciences"=>{"Agricultural and Biological Sciences"=>15}, "Biochemistry, Genetics and Molecular Biology"=>{"Biochemistry, Genetics and Molecular Biology"=>5}, "Veterinary Science and Veterinary Medicine"=>{"Veterinary Science and Veterinary Medicine"=>1}}, "reader_count_by_country"=>{"United States"=>1, "Ireland"=>1}, "group_count"=>0}

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Figshare

  • {"files"=>["https://ndownloader.figshare.com/files/280407", "https://ndownloader.figshare.com/files/280470", "https://ndownloader.figshare.com/files/280500", "https://ndownloader.figshare.com/files/280558", "https://ndownloader.figshare.com/files/280601", "https://ndownloader.figshare.com/files/280655", "https://ndownloader.figshare.com/files/280766", "https://ndownloader.figshare.com/files/280846"], "description"=>"<div><p>Changes in gene regulatory circuits often give rise to phenotypic differences among closely related organisms. In bacteria, these changes can result from alterations in the ancestral genome and/or be brought about by genes acquired by horizontal transfer. Here, we identify an allele of the ancestral transcription factor PmrA that requires the horizontally acquired <em>pmrD</em> gene product to promote gene expression. We determined that a single amino acid difference between the PmrA proteins from the human adapted <em>Salmonella enterica</em> serovar Paratyphi B and the broad host range <em>S. enterica</em> serovar Typhimurium rendered transcription of PmrA-activated genes dependent on the PmrD protein in the former but not the latter serovar. Bacteria harboring the serovar Typhimurium allele exhibited polymyxin B resistance under PmrA- or under PmrA- and PmrD-inducing conditions. By contrast, isogenic strains with the serovar Paratyphi B allele displayed PmrA-regulated polymyxin B resistance only when experiencing activating conditions for both PmrA and PmrD. We establish that the two PmrA orthologs display quantitative differences in several biochemical properties. Strains harboring the serovar Paratyphi B allele showed enhanced biofilm formation, a property that might promote serovar Paratyphi B's chronic infection of the gallbladder. Our findings illustrate how subtle differences in ancestral genes can impact the ability of horizontally acquired genes to confer new properties.</p> </div>", "links"=>[], "tags"=>["allele", "ancestral", "transcription", "horizontally", "acquired", "product"], "article_id"=>115294, "categories"=>["Microbiology"], "users"=>["H. Deborah Chen", "Mollie W. Jewett", "Eduardo A. Groisman"], "doi"=>["https://dx.doi.org/10.1371/journal.pgen.1003060.s001", "https://dx.doi.org/10.1371/journal.pgen.1003060.s002", "https://dx.doi.org/10.1371/journal.pgen.1003060.s003", "https://dx.doi.org/10.1371/journal.pgen.1003060.s004", "https://dx.doi.org/10.1371/journal.pgen.1003060.s005", "https://dx.doi.org/10.1371/journal.pgen.1003060.s006", "https://dx.doi.org/10.1371/journal.pgen.1003060.s007", "https://dx.doi.org/10.1371/journal.pgen.1003060.s008"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/An_Allele_of_an_Ancestral_Transcription_Factor_Dependent_on_a_Horizontally_Acquired_Gene_Product__/115294", "title"=>"An Allele of an Ancestral Transcription Factor Dependent on a Horizontally Acquired Gene Product", "pos_in_sequence"=>0, "defined_type"=>4, "published_date"=>"2012-12-27 01:28:14"}
  • {"files"=>["https://ndownloader.figshare.com/files/516932"], "description"=>"<p>Transcription of PmrA-activated genes is promoted in response to Fe<sup>3+</sup> sensed by the PmrB protein. The sensor PhoQ responds to low Mg<sup>2+</sup> by promoting the phosphorylated state of PhoP, which activates transcription of the <i>pmrD</i> gene. The PmrD protein binds to PmrA-P, the active form of the PmrA protein, and protects it from dephosphorylation by PmrB. PmrA-P is a transcriptional repressor of the <i>pmrD</i> promoter.</p>", "links"=>[], "tags"=>["interactions", "systems", "serovar"], "article_id"=>187430, "categories"=>["Microbiology"], "users"=>["H. Deborah Chen", "Mollie W. Jewett", "Eduardo A. Groisman"], "doi"=>["https://dx.doi.org/10.1371/journal.pgen.1003060.g001"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Model_of_the_regulatory_interactions_between_the_PhoP_PhoQ_and_PmrA_PmrB_systems_in_S_enterica_serovar_Typhimurium_/187430", "title"=>"Model of the regulatory interactions between the PhoP/PhoQ and PmrA/PmrB systems in <i>S. enterica</i> serovar Typhimurium.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2012-12-27 02:03:50"}
  • {"files"=>["https://ndownloader.figshare.com/files/517025"], "description"=>"<p>(A) Growth of <i>S. typhimurium</i> (14028s) and <i>S. paratyphi</i> B (SARA46) on plates containing polymyxin B (5 µg/ml) and low Mg<sup>2+</sup> (i.e., 10 µM), or polymyxin B (5 µg/ml), low Mg<sup>2+</sup> (i.e., 10 µM) and high Fe<sup>3+</sup> (i.e., 100 µM). (B) β-galactosidase activity (Miller units) produced from a <i>pbgP-lac</i> transcriptional fusion in <i>S. paratyphi</i> B (SPV) (SARA42, SARA43, SARA45 and SARA46), <i>S. typhimurium</i> (14028s, SARA10, SARA15, SARA18), <i>S. paratyphi</i> B (EPV) (SARA52 and SARA56) and <i>S. typhi</i> (s3333) strains. The inset shows β-galactosidase activity (Miller units) produced from a <i>pbgP-lac</i> transcriptional fusion in <i>S. paratyphi</i> B (SPV) SARA41. Bacteria were grown for 4 h in N-minimal medium at pH 7.7 with low Mg<sup>2+</sup> (i.e., 10 µM), high Mg<sup>2+</sup> (i.e., 10 mM) or low Mg<sup>2+</sup> (i.e., 10 µM) and high Fe<sup>3+</sup> (i.e., 100 µM). Data correspond to the mean values of three independent experiments performed in duplicate, and error bars show standard deviation. (C) mRNA levels of the PhoP-activated <i>pmrD</i> gene from <i>S. paratyphi</i> B SARA46 grown as described in (B) were determined by reverse-transcription-qPCR analysis. Expression levels were normalized to those of the 16S ribosomal RNA gene. Data correspond to the mean values of three independent experiments and error bars show standard deviation.</p>", "links"=>[], "tags"=>["susceptible", "polymyxin", "transcribe"], "article_id"=>187527, "categories"=>["Microbiology"], "users"=>["H. Deborah Chen", "Mollie W. Jewett", "Eduardo A. Groisman"], "doi"=>["https://dx.doi.org/10.1371/journal.pgen.1003060.g002"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_S_paratyphi_B_is_susceptible_to_polymyxin_B_and_does_not_transcribe_pbgP_during_growth_in_low_Mg_2_/187527", "title"=>"<i>S. paratyphi</i> B is susceptible to polymyxin B and does not transcribe <i>pbgP</i> during growth in low Mg<sup>2+</sup>.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2012-12-27 02:05:27"}
  • {"files"=>["https://ndownloader.figshare.com/files/517213"], "description"=>"<p>(A) β-galactosidase activity (Miller units) produced from a <i>pbgP-lac</i> transcriptional fusion in the following strains: <i>S. typhimurium</i> (EG9241), <i>S. paratyphi</i> B (EG16652), <i>S. paratyphi</i> B <i>(pmrA G211</i>) (EG16275), <i>S. paratyphi</i> B Δ<i>pmrD</i> (EG16277), <i>S. paratyphi</i> B <i>pmrA</i> (<i>G211</i>) Δ<i>pmrD</i> (EG16276), and <i>S. paratyphi</i> B Δ<i>pmrA</i> (DC167). Bacteria were grown in N-minimal medium at pH 7.7 with low Mg<sup>2+</sup>, high Mg<sup>2+</sup> or low Mg<sup>2+</sup> and high Fe<sup>3+</sup>. Data correspond to the mean values of three independent experiments performed in duplicate, and error bars show standard deviation. Asterisks indicate statistically significant differences based on a two-tailed Student t-test (p<0.05). (B) β-galactosidase activity (Miller units) produced from a <i>pbgP-lac</i> transcriptional fusion in isogenic <i>pmrD<sup>+</sup></i> or <i>pmrD<sup>−</sup> S. typhimurium</i> strains harboring either the <i>pmrA</i> (<i>E211</i>) or (<i>G211</i>) allele (EG9241, EG11775, EG14331 and DC300) were determined as described in (A). (C–D) Growth of <i>S. enterica</i> strains harboring either the <i>pmrA</i> (<i>E211</i>) or the <i>pmrA</i> (<i>G211</i>) allele in the presence of the antibiotic polymyxin B (2.5 µg/ml) on plates containing 10 µM Mg<sup>2+</sup> and 100 µM Fe<sup>3+</sup>. <i>S. paratyphi</i> B growth was determined in the wild-type (SARA46), in a strain harboring either the <i>pmrA</i> (<i>E211</i>) (DC282) or <i>pmrA</i> (<i>G211</i>) (DC280) gene, in a Δ<i>pmrD</i> mutant expressing the <i>pmrA</i> (<i>E211</i>) (DC165 and DC287) or <i>pmrA</i> (<i>G211</i>) gene (DC285), and in a Δ<i>pmrA</i> mutant (DC167) (C). As a control, growth of <i>S. typhimurium</i> 14028s was monitored on the same plate (C). <i>S. typhimurium</i> growth was determined in the wild-type (14028s), in a strain harboring a 3′ FLAG-tagged <i>S. typhimurium pmrD</i> gene and the <i>pmrA</i> (<i>E211</i>) (EG16279) or <i>pmrA</i> (<i>G211</i>) (EG13404) allele, in a Δ<i>pmrD</i> mutant expressing the <i>pmrA</i> (<i>E211</i>) (DC46) or <i>pmrA</i> (<i>G211</i>) (EG14088) gene, and in a <i>pmrA</i> mutant (EG7139) (D).</p>", "links"=>[], "tags"=>["requires", "pmrd", "pmra-dependent", "genes", "polymyxin"], "article_id"=>187707, "categories"=>["Microbiology"], "users"=>["H. Deborah Chen", "Mollie W. Jewett", "Eduardo A. Groisman"], "doi"=>["https://dx.doi.org/10.1371/journal.pgen.1003060.g003"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_S_paratyphi_B_requires_PmrD_to_express_PmrA_dependent_genes_and_to_resist_polymyxin_B_during_growth_in_Fe_3_/187707", "title"=>"<i>S. paratyphi</i> B requires PmrD to express PmrA-dependent genes and to resist polymyxin B during growth in Fe<sup>3+</sup>.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2012-12-27 02:08:27"}
  • {"files"=>["https://ndownloader.figshare.com/files/517328"], "description"=>"<p>(A) Electrophoretic mobility shift assays carried out with a DNA fragment carrying the <i>pbgP</i> promoter region and increasing amounts of purified phosphorylated PmrA (G211) or PmrA (E211) proteins. Excess unlabeled <i>pbgP</i> DNA (cold probe) released the labeled probe from the retarded complex. Addition of excess unlabeled <i>ompX</i> or <i>mgtA</i> DNA did not release the labeled probe. (B) Levels of PmrA protein determined by Western blotting analyses from <i>S. typhimurium</i> strains expressing C-terminally HA-tagged versions of the PmrA (G211) (EG18052) or PmrA (E211) (DC53) proteins. Bacteria were grown in N-minimal medium at pH 7.7 with low Mg<sup>2+</sup> (i.e., 10 µM), or low Mg<sup>2+</sup> (i.e., 10 µM) and high Fe<sup>3+</sup> (i.e., 100 µM). The levels of RpoB were used as loading controls.</p>", "links"=>[], "tags"=>["affinity", "pmra-p", "promoters", "controls", "pmra", "levels"], "article_id"=>187822, "categories"=>["Microbiology"], "users"=>["H. Deborah Chen", "Mollie W. Jewett", "Eduardo A. Groisman"], "doi"=>["https://dx.doi.org/10.1371/journal.pgen.1003060.g004"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_The_affinity_of_PmrA_P_for_its_target_promoters_controls_PmrA_levels_in_vivo_/187822", "title"=>"The affinity of PmrA-P for its target promoters controls PmrA levels <i>in vivo</i>.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2012-12-27 02:10:22"}
  • {"files"=>["https://ndownloader.figshare.com/files/517458"], "description"=>"<p>(A–B) Levels of PmrA-P following incubation of PmrA (G211)-P or PmrA (E211)-P (10 µM) with PmrB<sub>c</sub> (5 µM) in the presence of 2.5 µM (A) or 1.25 µM (B) PmrD for the indicated times. The graph depicts the level of PmrA-P at the indicated times relative to levels at the start of the reaction. Data correspond to the mean values of at least three independent experiments and error bars show standard deviation. (C) Levels of phosphorylated versus unphosphorylated PmrA protein determined by Phos-tag gel analyses from <i>S. typhimurium</i> expressing C-terminally HA-tagged versions of the PmrA (G211) (EG18052) or PmrA (E211) (DC53) proteins. Bacteria were grown in N-minimal medium at pH 7.7 with low Mg<sup>2+</sup> (i.e., 10 µM) and high Fe<sup>3+</sup> (i.e., 100 µM). The total amounts of PmrA protein were determined on the same gels by boiling the samples to hydrolyze the phospho-Asp from PmrA-P. (D) Quantitation of the Western blot analyses shown in (C). The graph depicts the level of PmrA-P relative to total PmrA protein. Data correspond to the mean values of four independent experiments and error bars show standard deviation. These results are significantly different as determined by a two-tailed Student t-test (p<0.05). (E) β-galactosidase activity (Miller units) produced from a <i>pbgP-lac</i> transcriptional fusion in the following <i>S. typhimurium</i> 14028s strains: <i>pmrA</i> (<i>G211</i>) (EG9241), <i>pmrA</i> (<i>R81H G211</i>) (DC294), <i>pmrA</i> (<i>E211</i>) (EG11775), <i>pmrA</i> (<i>R81H E211</i>) (DC296), <i>pmrA</i> (<i>G211</i>) Δ<i>pmrD</i> (EG14331), <i>pmrA</i> (<i>R81H G211</i>) Δ<i>pmrD</i> (DC302), <i>pmrA</i> (<i>E211</i>) Δ<i>pmrD</i> (DC300), <i>pmrA</i> (<i>R81H E211</i>) Δ<i>pmrD</i> (DC304). Bacteria were grown in N-minimal medium at pH 7.7 with low Mg<sup>2+</sup> (i.e., 10 µM), high Mg<sup>2+</sup> (i.e., 10 mM) or low Mg<sup>2+</sup> (i.e., 10 µM) and high Fe<sup>3+</sup> (i.e., 100 µM). Data correspond to the mean values of three independent experiments performed in duplicate, and error bars show standard deviation.</p>", "links"=>[], "tags"=>["levels", "higher", "typhimurium", "pmra", "experiencing", "pmrd-", "pmra-inducing"], "article_id"=>187947, "categories"=>["Microbiology"], "users"=>["H. Deborah Chen", "Mollie W. Jewett", "Eduardo A. Groisman"], "doi"=>["https://dx.doi.org/10.1371/journal.pgen.1003060.g005"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_PmrA_P_levels_are_higher_in_S_typhimurium_pmrA_E211_than_in_S_typhimurium_pmrA_G211_experiencing_PmrD_and_PmrA_inducing_conditions_/187947", "title"=>"PmrA-P levels are higher in <i>S. typhimurium pmrA (E211)</i> than in <i>S. typhimurium pmrA</i> (<i>G211</i>) experiencing PmrD- and PmrA-inducing conditions.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2012-12-27 02:12:27"}
  • {"files"=>["https://ndownloader.figshare.com/files/517590"], "description"=>"<p>(A–D) mRNA levels of the PmrA-activated <i>pbgP</i> (A, C) and <i>pmrC</i> (B, D) genes from isogenic <i>S. typhimurium</i> 14028s strains expressing either the <i>pmrA</i> (<i>G211</i>) gene (EG13404) or the <i>pmrA</i> (<i>E211</i>) gene (EG16279) (A, B) and from isogenic <i>S. typhimurium</i> Δ<i>pmrD</i> strains expressing either the <i>pmrA</i> (<i>G211</i>) gene (EG14088) or the <i>pmrA</i> (<i>E211</i>) gene (DC46) (C, D) determined by reverse-transcription-qPCR analysis. Bacteria were grown in medium containing 10 mM Mg<sup>2+</sup>, shifted to medium containing 10 µM Mg<sup>2+</sup> and 100 µM Fe<sup>3+</sup> and harvested at the designated times to prepare RNA. Expression levels were normalized to those of the 16S ribosomal RNA gene. Data correspond to at least three independent experiments and error bars show standard deviation.</p>", "links"=>[], "tags"=>["affinity", "pmra", "promoters", "controls"], "article_id"=>188089, "categories"=>["Microbiology"], "users"=>["H. Deborah Chen", "Mollie W. Jewett", "Eduardo A. Groisman"], "doi"=>["https://dx.doi.org/10.1371/journal.pgen.1003060.g006"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_The_affinity_of_PmrA_for_its_target_promoters_controls_gene_expression_kinetics_/188089", "title"=>"The affinity of PmrA for its target promoters controls gene expression kinetics.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2012-12-27 02:14:49"}
  • {"files"=>["https://ndownloader.figshare.com/files/517724"], "description"=>"<p>(A) Ability of isogenic <i>S. paratyphi</i> B SARA46 strains to attach to cholesterol-coated surfaces in a tube biofilm assay. The ability of bacteria to form biofilms was determined in the SARA46 strain harboring either the <i>pmrA</i> (<i>E211</i>) (DC282) or <i>pmrA</i> (<i>G211</i>) gene (DC280), in a Δ<i>pmrD</i> mutant expressing the <i>pmrA</i> (<i>E211</i>) (DC287) or <i>pmrA</i> (<i>G211</i>) gene (DC285), and in a Δ<i>pmrA</i> mutant (DC167). Data correspond to the mean values of three independent experiments. Asterisks indicate statistically significant differences based on a two-tailed Student t-test (p<0.05). (B) Ability of isogenic <i>S. typhimurium</i> strains to attach to cholesterol-coated surfaces in a tube biofilm assay. The ability of bacteria to form biofilms was determined in the wild-type (14028s), in a strain harboring a 3′ FLAG-tagged <i>S. typhimurium pmrD</i> gene and either the <i>pmrA</i> (<i>E211</i>) (EG16279) or <i>pmrA</i> (<i>G211</i>) gene (EG13404), in a Δ<i>pmrD</i> mutant expressing the <i>pmrA</i> (<i>E211</i>) (DC46) or the <i>pmrA</i> (<i>G211</i>) gene (EG14088), and in a <i>pmrA</i> mutant (EG7139). Data correspond to the mean values of three independent experiments and error bars show standard deviation. Asterisks indicate statistically significant differences based on a two-tailed Student t-test (p<0.05).</p>", "links"=>[], "tags"=>["strains", "harboring", "allele", "enhanced", "biofilm"], "article_id"=>188221, "categories"=>["Microbiology"], "users"=>["H. Deborah Chen", "Mollie W. Jewett", "Eduardo A. Groisman"], "doi"=>["https://dx.doi.org/10.1371/journal.pgen.1003060.g007"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_S_enterica_strains_harboring_the_S_paratyphi_B_pmrA_allele_display_enhanced_biofilm_formation_/188221", "title"=>"<i>S. enterica</i> strains harboring the <i>S. paratyphi</i> B <i>pmrA</i> allele display enhanced biofilm formation.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2012-12-27 02:17:01"}
  • {"files"=>["https://ndownloader.figshare.com/files/517803"], "description"=>"<p>The PmrA (E211) protein displays a lower proportion of dimers than the PmrA (G211) protein.</p>", "links"=>[], "tags"=>["pmra", "displays", "dimers"], "article_id"=>188299, "categories"=>["Microbiology"], "users"=>["H. Deborah Chen", "Mollie W. Jewett", "Eduardo A. Groisman"], "doi"=>["https://dx.doi.org/10.1371/journal.pgen.1003060.t001"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_The_PmrA_E211_protein_displays_a_lower_proportion_of_dimers_than_the_PmrA_G211_protein_/188299", "title"=>"The PmrA (E211) protein displays a lower proportion of dimers than the PmrA (G211) protein.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2012-12-27 02:18:19"}

PMC Usage Stats | Further Information

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