Eubacterial SpoVG Homologs Constitute a New Family of Site-Specific DNA-Binding Proteins
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{"title"=>"Eubacterial SpoVG Homologs Constitute a New Family of Site-Specific DNA-Binding Proteins", "type"=>"journal", "authors"=>[{"first_name"=>"Brandon L.", "last_name"=>"Jutras", "scopus_author_id"=>"35388335400"}, {"first_name"=>"Alicia M.", "last_name"=>"Chenail", "scopus_author_id"=>"36469835800"}, {"first_name"=>"Christi L.", "last_name"=>"Rowland", "scopus_author_id"=>"56050294600"}, {"first_name"=>"Dustin", "last_name"=>"Carroll", "scopus_author_id"=>"55771135800"}, {"first_name"=>"M. Clarke", "last_name"=>"Miller", "scopus_author_id"=>"35618993500"}, {"first_name"=>"Tomasz", "last_name"=>"Bykowski", "scopus_author_id"=>"56616143700"}, {"first_name"=>"Brian", "last_name"=>"Stevenson", "scopus_author_id"=>"7103399193"}], "year"=>2013, "source"=>"PLoS ONE", "identifiers"=>{"pui"=>"369158034", "sgr"=>"84879253115", "pmid"=>"23818957", "scopus"=>"2-s2.0-84879253115", "doi"=>"10.1371/journal.pone.0066683", "issn"=>"19326203"}, "id"=>"4dadb9bc-dede-3163-a209-37d23549a785", "abstract"=>"A site-specific DNA-binding protein was purified from Borrelia burgdorferi cytoplasmic extracts, and determined to be a member of the highly conserved SpoVG family. This is the first time a function has been attributed to any of these ubiquitous bacterial proteins. Further investigations into SpoVG orthologues indicated that the Staphylococcus aureus protein also binds DNA, but interacts preferentially with a distinct nucleic acid sequence. Site-directed mutagenesis and domain swapping between the S. aureus and B. burgdorferi proteins identified that a 6-residue stretch of the SpoVG α-helix contributes to DNA sequence specificity. Two additional, highly conserved amino acid residues on an adjacent β-sheet are essential for DNA-binding, apparently by contacts with the DNA phosphate backbone. Results of these studies thus identified a novel family of bacterial DNA-binding proteins, developed a model of SpoVG-DNA interactions, and provide direction for future functional studies on these wide-spread proteins.", "link"=>"http://www.mendeley.com/research/eubacterial-spovg-homologs-constitute-new-family-sitespecific-dnabinding-proteins", "reader_count"=>12, "reader_count_by_academic_status"=>{"Student > Doctoral Student"=>2, "Researcher"=>2, "Student > Ph. D. Student"=>7, "Other"=>1}, "reader_count_by_user_role"=>{"Student > Doctoral Student"=>2, "Researcher"=>2, "Student > Ph. D. Student"=>7, "Other"=>1}, "reader_count_by_subject_area"=>{"Biochemistry, Genetics and Molecular Biology"=>3, "Agricultural and Biological Sciences"=>7, "Medicine and Dentistry"=>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"=>7}, "Biochemistry, Genetics and Molecular Biology"=>{"Biochemistry, Genetics and Molecular Biology"=>3}}, "reader_count_by_country"=>{"United States"=>1}, "group_count"=>0}

Scopus | Further Information

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Figshare

  • {"files"=>["https://ndownloader.figshare.com/files/1094992"], "description"=>"<p>(<b>A</b>) Schematic of the <i>vlsE</i> expression locus and DNAs uses for EMSA. In the upper illustration of the <i>vlsE</i> ORF, the gray areas represent the invariable regions, the white area represents the hypervariable region, and the black bars indicate the direct repeat sequences. Below that, the location of each labeled or unlabeled EMSA DNA is represented by thick or thin black horizontal lines, respectively. “DR” indicates the directly-repeated sequences bordering the variable region of <i>vlsE</i>. (<b>B</b>) EMSAs using <i>B. burgdorferi</i> cytoplasmic extracts. Lane 1–6∶1 nM of labeled probe F27B-R10. Lane 2–6∶10 µg cell-free cytoplasmic extract. Lane 3∶100-fold molar excess unlabeled competitor F35-R14. Lane 4∶100-fold molar excess unlabeled competitor F27–R10. Lane 5∶100-fold molar excess unlabeled competitor F29–R16. Lane 6∶100-fold molar excess unlabeled competitor F33–R22.</p>", "links"=>[], "tags"=>["Biochemistry", "proteins", "DNA-binding proteins", "protein structure", "microbiology", "bacteriology", "Bacterial biochemistry", "Bacterial physiology", "Microbial physiology", "Infectious diseases", "Bacterial diseases", "cytoplasmic", "binds", "dna"], "article_id"=>726660, "categories"=>["Medicine", "Biological Sciences"], "users"=>["Brandon L. Jutras", "Alicia M. Chenail", "Christi L. Rowland", "Dustin Carroll", "M. Clarke Miller", "Tomasz Bykowski", "Brian Stevenson"], "doi"=>["https://dx.doi.org/10.1371/journal.pone.0066683.g001"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_A_B_burgdorferi_cytoplasmic_protein_binds_DNA_within_the_vlsE_open_reading_frame_/726660", "title"=>"A <i>B. burgdorferi</i> cytoplasmic protein binds DNA within the <i>vlsE</i> open reading frame.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-06-20 01:51:00"}
  • {"files"=>["https://ndownloader.figshare.com/files/1094993"], "description"=>"<p>Eluates were separated by SDS PAGE, stained with Sypro Ruby. M. Molecular mass standards. Lanes 1–3. Proteins eluted with 500, 750, and 1000 mM NaCl elution, respectively.</p>", "links"=>[], "tags"=>["Biochemistry", "proteins", "DNA-binding proteins", "protein structure", "microbiology", "bacteriology", "Bacterial biochemistry", "Bacterial physiology", "Microbial physiology", "Infectious diseases", "Bacterial diseases", "chromatographically", "purified", "probe", "affixed", "beads", "incubated", "cell-free", "extracts", "bound", "eluted", "titration", "concentrations"], "article_id"=>726661, "categories"=>["Medicine", "Biological Sciences"], "users"=>["Brandon L. Jutras", "Alicia M. Chenail", "Christi L. Rowland", "Dustin Carroll", "M. Clarke Miller", "Tomasz Bykowski", "Brian Stevenson"], "doi"=>["https://dx.doi.org/10.1371/journal.pone.0066683.g002"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_DNA_affinity_chromatographically_purified_SpoVG_Bb_vlsE_probe_affixed_to_magnetic_beads_was_incubated_with_cell_free_extracts_and_bound_protein_were_eluted_by_titration_with_increasing_concentrations_of_NaCl_/726661", "title"=>"DNA-affinity chromatographically purified SpoVG<i><sub>Bb</sub></i>. <i>vlsE</i> probe affixed to magnetic beads was incubated with cell-free extracts and bound protein were eluted by titration with increasing concentrations of NaCl.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-06-20 01:51:01"}
  • {"files"=>["https://ndownloader.figshare.com/files/1094996"], "description"=>"<p><b>Illustrated is an alignment of the predicted sequences of SpoVG proteins from 19 different families of 6 different phyla.</b> Alignment was performed using Geneious software, Pfam 200, with 1000 iterations. Identical or homologous amino acids found in the same position of multiple proteins are indicated by same-colored boxes. Note that these analyses grouped the SpoVG protein of the opportunistic oral pathogen <i>Prevotella dentalis</i> with the Gram-positive <i>Bacilli</i> class, although it is currently considered to be a member of the <i>Bacteroides</i>. Consistent with these results, <i>P. dentalis</i> has morphological and biochemical features which differ from other species in the genus <i>Prevotella</i> and class <i>Bacteroides </i><a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0066683#pone.0066683-Willems1\" target=\"_blank\">[51]</a>. Red arrows indicate residues demonstrated to be involved in SpoVG-DNA interactions. Green asterisks denote conserved residues that were found to be not required for binding DNA. The magenta box indicates residues of SpoVG<i><sub>Bb</sub></i> and SpoVG<i><sub>Sa</sub></i> involved in DNA sequence specificity.</p>", "links"=>[], "tags"=>["Biochemistry", "proteins", "DNA-binding proteins", "protein structure", "microbiology", "bacteriology", "Bacterial biochemistry", "Bacterial physiology", "Microbial physiology", "Infectious diseases", "Bacterial diseases", "conserved", "eubacteria"], "article_id"=>726662, "categories"=>["Medicine", "Biological Sciences"], "users"=>["Brandon L. Jutras", "Alicia M. Chenail", "Christi L. Rowland", "Dustin Carroll", "M. Clarke Miller", "Tomasz Bykowski", "Brian Stevenson"], "doi"=>["https://dx.doi.org/10.1371/journal.pone.0066683.g003"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_SpoVG_is_a_highly_conserved_Eubacteria_protein_/726662", "title"=>"SpoVG is a highly conserved Eubacteria protein.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-06-20 01:51:02"}
  • {"files"=>["https://ndownloader.figshare.com/files/1094999"], "description"=>"<p>Recombinant SpoVG<i><sub>Bb</sub></i> binds specifically to an 18 bp sequence of the <i>vlsE</i> open reading frame. (<b>A</b>) Lanes 1–3∶1 nM of labeled F27B-R10. Lane 2∶300 nM SpoVG<i><sub>Bb</sub></i>. Lane 3∶600 nM SpoVG<i><sub>Bb</sub></i>. (<b>B</b>) Lanes 1–3∶1 nM of labeled F77B-R10. Lane 2∶300 nM SpoVG<i><sub>Bb</sub></i>. Lane 3∶600 nM SpoVG<i><sub>Bb</sub></i>. (<b>C</b>) Lanes 1–3∶1 nM of labeled F27B-R4. Lane 2∶300 nM SpoVG<i><sub>Bb</sub></i>. Lane 3∶600 nM SpoVG<i><sub>Bb</sub></i>. (<b>D</b>) Lanes 1–3∶1 nM of labeled <i>erp</i> Operator DNA. Lane 2∶300 nM SpoVG<i><sub>Bb</sub></i>. Lane 3∶600 nM SpoVG<i><sub>Bb</sub></i>.</p>", "links"=>[], "tags"=>["Biochemistry", "proteins", "DNA-binding proteins", "protein structure", "microbiology", "bacteriology", "Bacterial biochemistry", "Bacterial physiology", "Microbial physiology", "Infectious diseases", "Bacterial diseases", "high-affinity", "binding"], "article_id"=>726663, "categories"=>["Medicine", "Biological Sciences"], "users"=>["Brandon L. Jutras", "Alicia M. Chenail", "Christi L. Rowland", "Dustin Carroll", "M. Clarke Miller", "Tomasz Bykowski", "Brian Stevenson"], "doi"=>["https://dx.doi.org/10.1371/journal.pone.0066683.g004"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Identification_of_a_SpoVG_Bb_high_affinity_binding_site_/726663", "title"=>"Identification of a SpoVG<b><i><sub>Bb</sub></i></b> high-affinity binding site.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-06-20 01:51:03"}
  • {"files"=>["https://ndownloader.figshare.com/files/1095000"], "description"=>"<p>Illustrated are EMSAs with <i>S. aureus</i> SpoVG<i><sub>Sa</sub></i>, labeled <i>cap5</i> 5′ non-coding DNA, and various unlabeled competitor DNAs. <b>Lanes 1–12</b>∶5 nM of labeled <i>capA</i> promoter DNA. <b>Lanes 2–4</b>: Increasing amounts of SpoVG<i><sub>Sa</sub></i> (0.2 µg, 0.4 µg, and 0.6 µg, respectively). <b>Lanes 5–12</b>∶0.8 µg of SpoVG<i><sub>Sa</sub></i>. <b>Lanes 5–8</b>∶50-fold molar excess of unlabeled <i>fmtB, lukED, esxA,</i> or <i>cap5</i> 5′ non-coding DNAs, respectively. <b>Lane 9</b>∶50-fold molar excess of <i>esxA</i> ORF DNA. <b>Lane 10</b>∶50-fold molar excess of <i>cap5A</i> ORF DNA. <b>Lane </b><b>11:</b> SpoVG<i><sub>Sa</sub></i> was heated to 99°C for 5 minutes before use in EMSA. <b>Lane 12</b>: SpoVG<i><sub>Sa</sub></i> was preincubated with 5 mg/ml of Proteinase K before use in EMSA.</p>", "links"=>[], "tags"=>["Biochemistry", "proteins", "DNA-binding proteins", "protein structure", "microbiology", "bacteriology", "Bacterial biochemistry", "Bacterial physiology", "Microbial physiology", "Infectious diseases", "Bacterial diseases", "binds", "aureus", "dnas", "adjacent"], "article_id"=>726664, "categories"=>["Medicine", "Biological Sciences"], "users"=>["Brandon L. Jutras", "Alicia M. Chenail", "Christi L. Rowland", "Dustin Carroll", "M. Clarke Miller", "Tomasz Bykowski", "Brian Stevenson"], "doi"=>["https://dx.doi.org/10.1371/journal.pone.0066683.g005"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_SpoVG_Sa_binds_specifically_to_S_aureus_cap5_fmtB_lukED_and_saeX_DNAs_adjacent_to_the_promoter_/726664", "title"=>"SpoVG<i><sub>Sa</sub></i> binds specifically to <i>S. aureus cap5, fmtB, lukED,</i> and <i>saeX</i> DNAs adjacent to the promoter.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-06-20 01:51:04"}
  • {"files"=>["https://ndownloader.figshare.com/files/1095001"], "description"=>"<p>EMSA with a labeled 62 bp probe derived from of <i>cap5</i> 5-non-coding DNA (cap41) and different concentration of 28 bp cold competitors. <b>Lanes 1–7</b>∶7.5 nM cap41 probe (−142 through −84 from translational start site). <b>Lanes 2–7∶</b>0.8 µg SpoVG. <b>Lane 3–5∶</b>10-, 25-, and 50-fold molar excess of competitor A respectively. <b>Lane 6</b>∶50-fold molar excess of competitor B. <b>Lane 7</b>∶50-fold molar excess of competitor C.</p>", "links"=>[], "tags"=>["Biochemistry", "proteins", "DNA-binding proteins", "protein structure", "microbiology", "bacteriology", "Bacterial biochemistry", "Bacterial physiology", "Microbial physiology", "Infectious diseases", "Bacterial diseases", "interacts", "28", "bp", "adjacent"], "article_id"=>726665, "categories"=>["Medicine", "Biological Sciences"], "users"=>["Brandon L. Jutras", "Alicia M. Chenail", "Christi L. Rowland", "Dustin Carroll", "M. Clarke Miller", "Tomasz Bykowski", "Brian Stevenson"], "doi"=>["https://dx.doi.org/10.1371/journal.pone.0066683.g006"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_SpoVG_Sa_interacts_specifically_with_a_28_bp_region_adjacent_to_the_cap5_promoter_/726665", "title"=>"SpoVG<i><sub>Sa</sub></i> interacts specifically with a 28 bp region adjacent to the <i>cap5</i> promoter.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-06-20 01:51:05"}
  • {"files"=>["https://ndownloader.figshare.com/files/1095003"], "description"=>"<p>(<b>A</b>) The conserved sequence, 5′ to 3′, identified by multiple motif analysis of promoters bound to and influenced by SpoVG<i><sub>Sa</sub></i>. (<b>B</b>) EMSA with a labeled probe cap41, derived from <i>cap5</i> sequence, and two different 28 bp cold competitors. All lanes contain 5 nM labeled cap41 DNA. Lanes 2–6 also include 0.9 µg of SpoVG<i><sub>Sa</sub></i>. Lanes 3 and 4∶25 fold molar excess competitor A or mutant competitor A, respectively. Lanes 5 and 6∶50 fold molar excess of competitor A and mutant competitor A, respectively. (<b>C</b>) Sequences of probe <i>cap41</i> and competitors. The differences between the wild type and mutant competitors are indicated by boldface italics.</p>", "links"=>[], "tags"=>["Biochemistry", "proteins", "DNA-binding proteins", "protein structure", "microbiology", "bacteriology", "Bacterial biochemistry", "Bacterial physiology", "Microbial physiology", "Infectious diseases", "Bacterial diseases", "palindromic", "motif"], "article_id"=>726667, "categories"=>["Medicine", "Biological Sciences"], "users"=>["Brandon L. Jutras", "Alicia M. Chenail", "Christi L. Rowland", "Dustin Carroll", "M. Clarke Miller", "Tomasz Bykowski", "Brian Stevenson"], "doi"=>["https://dx.doi.org/10.1371/journal.pone.0066683.g007"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_The_palindromic_motif_5_ATTAA_T_A_3_8242_is_required_for_SpoVG_Sa_binding_/726667", "title"=>"The palindromic motif 5′-ATTAA<sup>T</sup>/<sub>A</sub>-3′ is required for SpoVG<b><i><sub>Sa</sub></i></b> binding.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-06-20 01:51:07"}
  • {"files"=>["https://ndownloader.figshare.com/files/1095006"], "description"=>"<p><i>B. burgdorferi</i> SpoVG<i><sub>Bb</sub></i> residues QDFRKA were mutated to the analogous residues of <i>S. aureus</i> to produce SpoVG<i><sub>Bb-Sa</sub></i>. Similarly, SpoVG<i><sub>Sa</sub></i> residues SDMRQE were changed to the corresponding <i>B. burgdorferi</i> SpoVG<i><sub>Bb</sub></i> residues to create SpoVG<i><sub>Sa-Bb.</sub></i> These chimeric proteins were queried for their respective abilities to bind <i>vlsE</i> and <i>cap5</i> probes. (<b>A</b>) SpoVG<i><sub>Bb-Sa</sub></i> domain swap. Lanes 1, 2, 5, and 6 contain labeled <i>vlsE</i> probe. Lanes 3, 4, 7, and 8 contain labeled <i>cap5</i> probe. Lane 2 and 4, 200 nM wild-type SpoVG<i><sub>Bb</sub>.</i> Lane 4 and 8, 200 nM SpoVG<i><sub>Bb-Sa</sub></i>. (<b>B</b>) SpoVG<i><sub>Sa-Bb</sub></i> domain swap. Lanes 1, 2, 5, and 6 contain 5 nM of labeled <i>vlsE</i> probe. Lanes 3, 4, 7, and 8 contain labeled <i>cap5</i> DNA. Lane 2 and 4, 200 nM wild-type SpoVG<i><sub>Sa</sub>.</i> Lane 4 and 8, 200 nM SpoVG<i><sub>Sa-Bb</sub></i>. (<b>C</b>) <i>Listeria monocytogenes</i> SpoVG binds <i>cap5</i> DNA. Lanes 1 and 2 include 5 nM <i>vlsE</i> probe DNA, Lanes 3 and 4 contain 5 nM <i>cap5</i> probe DNA, and Lanes 2 and 4 contain 200 nM SpoVG<i><sub>Lm</sub></i> protein.</p>", "links"=>[], "tags"=>["Biochemistry", "proteins", "DNA-binding proteins", "protein structure", "microbiology", "bacteriology", "Bacterial biochemistry", "Bacterial physiology", "Microbial physiology", "Infectious diseases", "Bacterial diseases", "swapping", "experiments", "defined", "spovg", "nucleotide-binding"], "article_id"=>726670, "categories"=>["Medicine", "Biological Sciences"], "users"=>["Brandon L. Jutras", "Alicia M. Chenail", "Christi L. Rowland", "Dustin Carroll", "M. Clarke Miller", "Tomasz Bykowski", "Brian Stevenson"], "doi"=>["https://dx.doi.org/10.1371/journal.pone.0066683.g008"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Domain_swapping_experiments_defined_a_region_of_SpoVG_required_for_nucleotide_binding_specificity_/726670", "title"=>"Domain swapping experiments defined a region of SpoVG required for nucleotide-binding specificity.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-06-20 01:51:10"}
  • {"files"=>["https://ndownloader.figshare.com/files/1095008"], "description"=>"<p>Lanes 1, 2, 5 and 6 contain 2 nM labeled <i>vlsE</i> probe. Lanes 3,4, and 7–12 contain 2 nM labeled <i>cap41</i> probe. Additional ingredients of each EMSA are: Lane 2, 1.5 µM mutant SpoVG<i><sub>Bb</sub></i> R53A-R54A; Lane 4, 1.5 µM mutant SpoVG<i><sub>Sa</sub></i> K50A-R51A; Lane 6, 500 nM wild-type SpoVG<i><sub>Bb</sub></i>; Lane 8, 1.5 µM mutant SpoVG<i><sub>Sa</sub></i> K50A: Lane 10, 1.5 µM mutant SpoVG<i><sub>Sa</sub></i> R51A; Lane 12, 500 µM wild-type SpoVG<i><sub>Sa</sub></i>.</p>", "links"=>[], "tags"=>["Biochemistry", "proteins", "DNA-binding proteins", "protein structure", "microbiology", "bacteriology", "Bacterial biochemistry", "Bacterial physiology", "Microbial physiology", "Infectious diseases", "Bacterial diseases", "mutagenesis", "residues", "binding"], "article_id"=>726672, "categories"=>["Medicine", "Biological Sciences"], "users"=>["Brandon L. Jutras", "Alicia M. Chenail", "Christi L. Rowland", "Dustin Carroll", "M. Clarke Miller", "Tomasz Bykowski", "Brian Stevenson"], "doi"=>["https://dx.doi.org/10.1371/journal.pone.0066683.g009"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Alanine_mutagenesis_determined_residues_required_for_binding_DNA_/726672", "title"=>"Alanine mutagenesis determined residues required for binding DNA.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-06-20 01:51:12"}
  • {"files"=>["https://ndownloader.figshare.com/files/1095010"], "description"=>"<p>Results of panels A through D illustrate HPLC sizing column chromatography of wild type and mutant SpoVG<i><sub>Sa</sub></i> proteins. For some preparations, proteins eluted with a retention time of approximately 7 minutes, which corresponds with a molecular mass >440 kDa and are composed of protein aggregates. (<b>A</b>) Wild-type SpoVG<i><sub>Sa</sub></i>; (<b>B</b>) SpoVG<i><sub>Sa</sub></i> K50A-R51A; (<b>C</b>) SpoVG<i><sub>Sa</sub></i> K50A; (<b>D</b>) SpoVG<i><sub>Sa</sub></i> R51A. Peaks marked with red asterisks indicate retention volumes corresponding with approximately 55–60 kDa. Panels E and F illustrates proteins separated following native of denaturing PAGE, respectively. M, Molecular mass standards; Lane 1, 1.5 µM mutant SpoVG<i><sub>Sa</sub></i> K50A-R51A; Lane 2, 1 µM mutant SpoVG<i><sub>Sa</sub></i> K50A; Lane 3, 1 µM mutant SpoVG<i><sub>Sa</sub></i> R51A; Lane 4, 1 µM wild-type SpoVG<i><sub>Sa</sub></i>.</p>", "links"=>[], "tags"=>["Biochemistry", "proteins", "DNA-binding proteins", "protein structure", "microbiology", "bacteriology", "Bacterial biochemistry", "Bacterial physiology", "Microbial physiology", "Infectious diseases", "Bacterial diseases", "directed", "mutagenesis", "did", "spovg"], "article_id"=>726674, "categories"=>["Medicine", "Biological Sciences"], "users"=>["Brandon L. Jutras", "Alicia M. Chenail", "Christi L. Rowland", "Dustin Carroll", "M. Clarke Miller", "Tomasz Bykowski", "Brian Stevenson"], "doi"=>["https://dx.doi.org/10.1371/journal.pone.0066683.g010"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Site_directed_mutagenesis_did_not_influence_SpoVG_oligomerization_/726674", "title"=>"Site directed mutagenesis did not influence SpoVG oligomerization.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-06-20 01:51:14"}
  • {"files"=>["https://ndownloader.figshare.com/files/1095013"], "description"=>"<p>Residues required for DNA-binding and those involved with sequence specificity are indicated, with different colors reflecting biochemical properties of amino acids: Gray = positively charged, Red = negatively charged, and Green = polar, uncharged. (<b>A</b>) SpoVG<i><sub>Sa</sub></i>. (<b>B</b>) SpoVG<i><sub>Bb</sub></i>.</p>", "links"=>[], "tags"=>["Biochemistry", "proteins", "DNA-binding proteins", "protein structure", "microbiology", "bacteriology", "Bacterial biochemistry", "Bacterial physiology", "Microbial physiology", "Infectious diseases", "Bacterial diseases", "structures", "modeled", "solved", "spovg"], "article_id"=>726677, "categories"=>["Medicine", "Biological Sciences"], "users"=>["Brandon L. Jutras", "Alicia M. Chenail", "Christi L. Rowland", "Dustin Carroll", "M. Clarke Miller", "Tomasz Bykowski", "Brian Stevenson"], "doi"=>["https://dx.doi.org/10.1371/journal.pone.0066683.g011"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Monomeric_structures_of_SpoVG_Sa_and_SpoVG_Bb_modeled_on_the_solved_S_epidermidis_SpoVG_protein_structure_/726677", "title"=>"Monomeric structures of SpoVG<i><sub>Sa</sub></i> and SpoVG<i><sub>Bb,</sub></i> modeled on the solved <i>S. epidermidis</i> SpoVG protein structure.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-06-20 01:51:17"}
  • {"files"=>["https://ndownloader.figshare.com/files/1095015"], "description"=>"<p>Oligonucleotides used in this study.</p>", "links"=>[], "tags"=>["Biochemistry", "proteins", "DNA-binding proteins", "protein structure", "microbiology", "bacteriology", "Bacterial biochemistry", "Bacterial physiology", "Microbial physiology", "Infectious diseases", "Bacterial diseases"], "article_id"=>726679, "categories"=>["Medicine", "Biological Sciences"], "users"=>["Brandon L. Jutras", "Alicia M. Chenail", "Christi L. Rowland", "Dustin Carroll", "M. Clarke Miller", "Tomasz Bykowski", "Brian Stevenson"], "doi"=>["https://dx.doi.org/10.1371/journal.pone.0066683.t002"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Oligonucleotides_used_in_this_study_/726679", "title"=>"Oligonucleotides used in this study.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2013-06-20 01:51:19"}
  • {"files"=>["https://ndownloader.figshare.com/files/1095016"], "description"=>"<p>Plasmids used in this study.</p>", "links"=>[], "tags"=>["Biochemistry", "proteins", "DNA-binding proteins", "protein structure", "microbiology", "bacteriology", "Bacterial biochemistry", "Bacterial physiology", "Microbial physiology", "Infectious diseases", "Bacterial diseases"], "article_id"=>726680, "categories"=>["Medicine", "Biological Sciences"], "users"=>["Brandon L. Jutras", "Alicia M. Chenail", "Christi L. Rowland", "Dustin Carroll", "M. Clarke Miller", "Tomasz Bykowski", "Brian Stevenson"], "doi"=>["https://dx.doi.org/10.1371/journal.pone.0066683.t001"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Plasmids_used_in_this_study_/726680", "title"=>"Plasmids used in this study.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2013-06-20 01:51:20"}

PMC Usage Stats | Further Information

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Relative Metric

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