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{"title"=>"Contact- and Protein Transfer-Dependent Stimulation of Assembly of the Gliding Motility Machinery in Myxococcus xanthus", "type"=>"journal", "authors"=>[{"first_name"=>"Beata", "last_name"=>"Jakobczak", "scopus_author_id"=>"56768188700"}, {"first_name"=>"Daniela", "last_name"=>"Keilberg", "scopus_author_id"=>"46861015500"}, {"first_name"=>"Kristin", "last_name"=>"Wuichet", "scopus_author_id"=>"6505915585"}, {"first_name"=>"Lotte", "last_name"=>"Søgaard-Andersen", "scopus_author_id"=>"7004054962"}], "year"=>2015, "source"=>"PLoS Genetics", "identifiers"=>{"issn"=>"15537404", "pui"=>"605567926", "doi"=>"10.1371/journal.pgen.1005341", "sgr"=>"84938792073", "scopus"=>"2-s2.0-84938792073", "pmid"=>"26132848"}, "id"=>"1c000d9f-67d9-303b-81a5-c4422180dcef", "abstract"=>"Bacteria engage in contact-dependent activities to coordinate cellular activities that aid their survival. Cells of Myxococcus xanthus move over surfaces by means of type IV pili and gliding motility. Upon direct contact, cells physically exchange outer membrane (OM) lipoproteins, and this transfer can rescue motility in mutants lacking lipoproteins required for motility. The mechanism of gliding motility and its stimulation by transferred OM lipoproteins remain poorly characterized. We investigated the function of CglC, GltB, GltA and GltC, all of which are required for gliding. We demonstrate that CglC is an OM lipoprotein, GltB and GltA are integral OM β-barrel proteins, and GltC is a soluble periplasmic protein. GltB and GltA are mutually stabilizing, and both are required to stabilize GltC, whereas CglC accumulate independently of GltB, GltA and GltC. Consistently, purified GltB, GltA and GltC proteins interact in all pair-wise combinations. Using active fluorescently-tagged fusion proteins, we demonstrate that GltB, GltA and GltC are integral components of the gliding motility complex. Incorporation of GltB and GltA into this complex depends on CglC and GltC as well as on the cytoplasmic AglZ protein and the inner membrane protein AglQ, both of which are components of the gliding motility complex. Conversely, incorporation of AglZ and AglQ into the gliding motility complex depends on CglC, GltB, GltA and GltC. Remarkably, physical transfer of the OM lipoprotein CglC to a ΔcglC recipient stimulates assembly of the gliding motility complex in the recipient likely by facilitating the OM integration of GltB and GltA. These data provide evidence that the gliding motility complex in M. xanthus includes OM proteins and suggest that this complex extends from the cytoplasm across the cell envelope to the OM. These data add assembly of gliding motility complexes in M. xanthus to the growing list of contact-dependent activities in bacteria.", "link"=>"http://www.mendeley.com/research/contact-protein-transferdependent-stimulation-assembly-gliding-motility-machinery-myxococcus-xanthus", "reader_count"=>13, "reader_count_by_academic_status"=>{"Researcher"=>2, "Student > Ph. D. Student"=>2, "Student > Master"=>5, "Student > Bachelor"=>1, "Professor"=>2, "Unspecified"=>1}, "reader_count_by_user_role"=>{"Researcher"=>2, "Student > Ph. D. Student"=>2, "Student > Master"=>5, "Student > Bachelor"=>1, "Professor"=>2, "Unspecified"=>1}, "reader_count_by_subject_area"=>{"Biochemistry, Genetics and Molecular Biology"=>5, "Agricultural and Biological Sciences"=>6, "Immunology and Microbiology"=>1, "Unspecified"=>1}, "reader_count_by_subdiscipline"=>{"Immunology and Microbiology"=>{"Immunology and Microbiology"=>1}, "Agricultural and Biological Sciences"=>{"Agricultural and Biological Sciences"=>6}, "Biochemistry, Genetics and Molecular Biology"=>{"Biochemistry, Genetics and Molecular Biology"=>5}, "Unspecified"=>{"Unspecified"=>1}}, "group_count"=>1}

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• http://doi.org/10.1128/JB.00335-20
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• http://doi.org/10.1093/femsre/fux045
• http://doi.org/10.1007/s12268-020-1320-7
• http://doi.org/10.1038/s41564-020-0710-4
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• http://doi.org/10.1111/mmi.13389
• http://doi.org/10.1083/jcb.201412047
• http://doi.org/10.1093/jb/mvw061
• http://doi.org/10.1038/nature20121

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Figshare

• {"files"=>["https://ndownloader.figshare.com/files/2157939", "https://ndownloader.figshare.com/files/2157940", "https://ndownloader.figshare.com/files/2157941", "https://ndownloader.figshare.com/files/2157942", "https://ndownloader.figshare.com/files/2157943", "https://ndownloader.figshare.com/files/2157944", "https://ndownloader.figshare.com/files/2157945"], "description"=>"<div><p>Bacteria engage in contact-dependent activities to coordinate cellular activities that aid their survival. Cells of <i>Myxococcus xanthus</i> move over surfaces by means of type IV pili and gliding motility. Upon direct contact, cells physically exchange outer membrane (OM) lipoproteins, and this transfer can rescue motility in mutants lacking lipoproteins required for motility. The mechanism of gliding motility and its stimulation by transferred OM lipoproteins remain poorly characterized. We investigated the function of CglC, GltB, GltA and GltC, all of which are required for gliding. We demonstrate that CglC is an OM lipoprotein, GltB and GltA are integral OM β-barrel proteins, and GltC is a soluble periplasmic protein. GltB and GltA are mutually stabilizing, and both are required to stabilize GltC, whereas CglC accumulate independently of GltB, GltA and GltC. Consistently, purified GltB, GltA and GltC proteins interact in all pair-wise combinations. Using active fluorescently-tagged fusion proteins, we demonstrate that GltB, GltA and GltC are integral components of the gliding motility complex. Incorporation of GltB and GltA into this complex depends on CglC and GltC as well as on the cytoplasmic AglZ protein and the inner membrane protein AglQ, both of which are components of the gliding motility complex. Conversely, incorporation of AglZ and AglQ into the gliding motility complex depends on CglC, GltB, GltA and GltC. Remarkably, physical transfer of the OM lipoprotein CglC to a Δ<i>cglC</i> recipient stimulates assembly of the gliding motility complex in the recipient likely by facilitating the OM integration of GltB and GltA. These data provide evidence that the gliding motility complex in <i>M</i>. <i>xanthus</i> includes OM proteins and suggest that this complex extends from the cytoplasm across the cell envelope to the OM. These data add assembly of gliding motility complexes in <i>M</i>. <i>xanthus</i> to the growing list of contact-dependent activities in bacteria.</p></div>", "links"=>[], "tags"=>["OM integration", "OM lipoprotein", "cytoplasmic AglZ protein", "GltC proteins", "OM lipoproteins", "OM lipoprotein CglC", "membrane protein AglQ", "Gliding Motility Machinery", "GltA", "GltB", "Myxococcus xanthus Bacteria", "periplasmic protein", "OM proteins", "integral components", "cell envelope", "motility complexes", "Myxococcus xanthus move", "type iv pili", "Δ cglC"], "article_id"=>1470272, "categories"=>["Uncategorised"], "users"=>["Beata Jakobczak", "Daniela Keilberg", "Kristin Wuichet", "Lotte Søgaard-Andersen"], "doi"=>["https://dx.doi.org/10.1371/journal.pgen.1005341.s001", "https://dx.doi.org/10.1371/journal.pgen.1005341.s002", "https://dx.doi.org/10.1371/journal.pgen.1005341.s003", "https://dx.doi.org/10.1371/journal.pgen.1005341.s004", "https://dx.doi.org/10.1371/journal.pgen.1005341.s005", "https://dx.doi.org/10.1371/journal.pgen.1005341.s006", "https://dx.doi.org/10.1371/journal.pgen.1005341.s007"], "stats"=>{"downloads"=>29, "page_views"=>14, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/Contact_and_Protein_Transfer_Dependent_Stimulation_of_Assembly_of_the_Gliding_Motility_Machinery_in_Myxococcus_xanthus_/1470272", "title"=>"Contact- and Protein Transfer-Dependent Stimulation of Assembly of the Gliding Motility Machinery in <i>Myxococcus xanthus</i>", "pos_in_sequence"=>0, "defined_type"=>4, "published_date"=>"2015-07-01 02:57:37"}
• {"files"=>["https://ndownloader.figshare.com/files/2157908"], "description"=>"<p>Synonyms for proteins required for gliding motility are indicated on the left. Proteins shown on a grey, brown or purple background in the left panel and in grey, brown or purple in the right panel are encoded together in the genome [<a href=\"http://www.plosgenetics.org/article/info:doi/10.1371/journal.pgen.1005341#pgen.1005341.ref017\" target=\"_blank\">17</a>]; proteins in white are not encoded near other proteins shown here. Proteins outlined in red have been shown by fluorescence microscopy to localize in clusters along the cell body [here; [<a href=\"http://www.plosgenetics.org/article/info:doi/10.1371/journal.pgen.1005341#pgen.1005341.ref015\" target=\"_blank\">15</a>–<a href=\"http://www.plosgenetics.org/article/info:doi/10.1371/journal.pgen.1005341#pgen.1005341.ref018\" target=\"_blank\">18</a>]]; proteins that interact based on pull down experiments using <i>M</i>. <i>xanthus</i> cell extracts are indicated in italics [<a href=\"http://www.plosgenetics.org/article/info:doi/10.1371/journal.pgen.1005341#pgen.1005341.ref015\" target=\"_blank\">15</a>]. CglB is an OM lipoprotein [<a href=\"http://www.plosgenetics.org/article/info:doi/10.1371/journal.pgen.1005341#pgen.1005341.ref029\" target=\"_blank\">29</a>] and CglD is predicted to be an OM lipoprotein [<a href=\"http://www.plosgenetics.org/article/info:doi/10.1371/journal.pgen.1005341#pgen.1005341.ref020\" target=\"_blank\">20</a>]. It is not known if they face towards the periplasm or are exposed on the cell surface. They are shown on the cell surface because they contain a von Willebrand domain (VWA_2), which is often involved in cell adhesion [<a href=\"http://www.plosgenetics.org/article/info:doi/10.1371/journal.pgen.1005341#pgen.1005341.ref030\" target=\"_blank\">30</a>].</p>", "links"=>[], "tags"=>["OM integration", "OM lipoprotein", "cytoplasmic AglZ protein", "GltC proteins", "OM lipoproteins", "OM lipoprotein CglC", "membrane protein AglQ", "Gliding Motility Machinery", "GltA", "GltB", "Myxococcus xanthus Bacteria", "periplasmic protein", "OM proteins", "integral components", "cell envelope", "motility complexes", "Myxococcus xanthus move", "type iv pili", "Δ cglC"], "article_id"=>1470256, "categories"=>["Uncategorised"], "users"=>["Beata Jakobczak", "Daniela Keilberg", "Kristin Wuichet", "Lotte Søgaard-Andersen"], "doi"=>"https://dx.doi.org/10.1371/journal.pgen.1005341.g001", "stats"=>{"downloads"=>0, "page_views"=>11, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Subcellular_localization_of_proteins_required_for_gliding_motility_/1470256", "title"=>"Subcellular localization of proteins required for gliding motility.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2015-07-01 02:57:37"}
• {"files"=>["https://ndownloader.figshare.com/files/2157910"], "description"=>"<p>(A) Genetic organization of <i>cglC</i>, <i>gltB</i>, <i>gltA</i> and <i>gltC</i> region. Numbers below diagram indicates distances between start and stop codons of flanking genes. Orange box indicates the intergenic region containing the divergent <i>cglC</i> and <i>gltBAC</i> promoters. The four complementation constructs with the native promoter (orange) are indicated below. (B, C) Motility phenotypes of the indicated mutants (B) and complementation strains (C). Cells were incubated at 32°C for 24 h on 0.5% and 1.5% agar to score for type IV pili-dependent and gliding motility, respectively. In-frame deletion mutants are shown in (B) and the corresponding complementation strains are shown in (C). In the rows labeled P_<i>nat</i> and P_<i>pilA</i>, the complementing genes were expressed from the native promoter (marked orange in panel A) and the <i>pilA</i> promoter, respectively. Scale bar, 50μm on 1.5% agar and 2 mm on 0.5% agar. (D) Accumulation of CglC, GltB, GltA and GltC. Total cell lysates from exponentially growing cultures were separated by SDS-PAGE (proteins from 7×10⁷ cells loaded per lane) and analyzed by immunoblotting using specific antibodies as indicated. In the left and right panels, the complementation strains express the relevant gene from the native and the <i>pilA</i> promoter, respectively. Arrowheads indicate the relevant protein with the calculated molecular mass without signal peptides in brackets. Molecular mass markers are indicated in the leftmost lane of the two panels. Note that GltC has a calculated molecular mass of 73.3 kDa but is consistently observed to run as a higher molecular mass protein by SDS-PAGE. (E) Domain structure of CglC, GltB, GltA and GltC.</p>", "links"=>[], "tags"=>["OM integration", "OM lipoprotein", "cytoplasmic AglZ protein", "GltC proteins", "OM lipoproteins", "OM lipoprotein CglC", "membrane protein AglQ", "Gliding Motility Machinery", "GltA", "GltB", "Myxococcus xanthus Bacteria", "periplasmic protein", "OM proteins", "integral components", "cell envelope", "motility complexes", "Myxococcus xanthus move", "type iv pili", "Δ cglC"], "article_id"=>1470258, "categories"=>["Uncategorised"], "users"=>["Beata Jakobczak", "Daniela Keilberg", "Kristin Wuichet", "Lotte Søgaard-Andersen"], "doi"=>"https://dx.doi.org/10.1371/journal.pgen.1005341.g002", "stats"=>{"downloads"=>1, "page_views"=>26, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_CglC_GltB_GltA_and_GltC_are_required_for_gliding_motility_/1470258", "title"=>"CglC, GltB, GltA and GltC are required for gliding motility.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2015-07-01 02:57:37"}
• {"files"=>["https://ndownloader.figshare.com/files/2157912"], "description"=>"<p>(A) GltB, GltA and GltC localize to the OM and GltC is a soluble protein. Total WT cell extracts were separated into soluble and membrane fractions. Outer membrane vesicles (OMVs) were isolated from the cell free supernatant. Fractions were analyzed by immunoblotting using the indicated antibodies. Molecular mass markers are indicated to the left. The relevant proteins are indicated. (B) CglC is facing towards the periplasm. WT cells were treated with Proteinase K (PK) at the indicated concentrations for 10 min, followed by SDS-PAGE and immunoblotting. Lanes labeled Δ contain total cell extracts from the relevant in-frame deletion mutant. (C) CglC is important for OM incorporation of GltB and GltA. Left panel, total cell extracts from Δ<i>cglC</i> cells were separated into soluble and membrane fractions. Right panel, OMVs were isolated as in (A) from the indicated strains. All fraction were analyzed by immunoblotting using the indicated antibodies. Lanes labeled Δ contain total cell extracts from the relevant in-frame deletion mutants.</p>", "links"=>[], "tags"=>["OM integration", "OM lipoprotein", "cytoplasmic AglZ protein", "GltC proteins", "OM lipoproteins", "OM lipoprotein CglC", "membrane protein AglQ", "Gliding Motility Machinery", "GltA", "GltB", "Myxococcus xanthus Bacteria", "periplasmic protein", "OM proteins", "integral components", "cell envelope", "motility complexes", "Myxococcus xanthus move", "type iv pili", "Δ cglC"], "article_id"=>1470260, "categories"=>["Uncategorised"], "users"=>["Beata Jakobczak", "Daniela Keilberg", "Kristin Wuichet", "Lotte Søgaard-Andersen"], "doi"=>"https://dx.doi.org/10.1371/journal.pgen.1005341.g003", "stats"=>{"downloads"=>2, "page_views"=>16, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Subcellular_localization_of_CglC_GltB_GltA_and_GltC_/1470260", "title"=>"Subcellular localization of CglC, GltB, GltA and GltC.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2015-07-01 02:57:37"}
• {"files"=>["https://ndownloader.figshare.com/files/2157913"], "description"=>"<p>(A) GltB and GltA are mutually stabilizing and stabilize GltC. Total cell extracts from cells grown as described in <a href=\"http://www.plosgenetics.org/article/info:doi/10.1371/journal.pgen.1005341#pgen.1005341.g002\" target=\"_blank\">Fig 2D</a> were isolated from strains of the indicated genotypes and analyzed by immunoblotting using specific antibodies as indicated. Molecular mass markers are indicated to the left. The relevant proteins are indicated. (B) Summary of observed effects on protein stability. Green and red indicate no effect or negative effect, respectively.</p>", "links"=>[], "tags"=>["OM integration", "OM lipoprotein", "cytoplasmic AglZ protein", "GltC proteins", "OM lipoproteins", "OM lipoprotein CglC", "membrane protein AglQ", "Gliding Motility Machinery", "GltA", "GltB", "Myxococcus xanthus Bacteria", "periplasmic protein", "OM proteins", "integral components", "cell envelope", "motility complexes", "Myxococcus xanthus move", "type iv pili", "Δ cglC"], "article_id"=>1470261, "categories"=>["Uncategorised"], "users"=>["Beata Jakobczak", "Daniela Keilberg", "Kristin Wuichet", "Lotte Søgaard-Andersen"], "doi"=>"https://dx.doi.org/10.1371/journal.pgen.1005341.g004", "stats"=>{"downloads"=>1, "page_views"=>19, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_GltB_and_GltA_are_mutually_stabilizing_and_stabilize_GltC_/1470261", "title"=>"GltB and GltA are mutually stabilizing and stabilize GltC.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2015-07-01 02:57:37"}
• {"files"=>["https://ndownloader.figshare.com/files/2157914"], "description"=>"<p>(A) GltC interacts with GltB and GltA. Purified MalE, MalE-CglC^20-172, MalE-GltB^20-275 or MalE-GltA^22-256 were mixed with an equal amount of GltC^25-673-His₆, loaded on an amylose matrix, the matrix was washed and then bound proteins were eluted with 10 mM maltose. Samples before loading (L), from the flow through (FT), the washing step (W) and elution (E) were analyzed by immunoblotting using antibodies against GltC and MalE. In the upper row, arrowheads indicate GltC^25-673-His₆ with its calculated molecular mass and in the lower row, the individual MalE proteins. Molecular mass markers are indicated to the left. (B) GltB interacts with GltA. Purified MalE, MalE-CglC^20-172 or MalE-GltA^22-256 were mixed with an equal amount of GST-GltB^20-275 and analyzed as described in A. Blots are marked as in A. (C) Summary of direct protein interactions. Green lines indicate interaction detected, red lines indicate interactions tested but not detected; grey line indicates interaction not tested.</p>", "links"=>[], "tags"=>["OM integration", "OM lipoprotein", "cytoplasmic AglZ protein", "GltC proteins", "OM lipoproteins", "OM lipoprotein CglC", "membrane protein AglQ", "Gliding Motility Machinery", "GltA", "GltB", "Myxococcus xanthus Bacteria", "periplasmic protein", "OM proteins", "integral components", "cell envelope", "motility complexes", "Myxococcus xanthus move", "type iv pili", "Δ cglC"], "article_id"=>1470262, "categories"=>["Uncategorised"], "users"=>["Beata Jakobczak", "Daniela Keilberg", "Kristin Wuichet", "Lotte Søgaard-Andersen"], "doi"=>"https://dx.doi.org/10.1371/journal.pgen.1005341.g005", "stats"=>{"downloads"=>2, "page_views"=>13, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_GltB_GltA_and_GltC_interact_directly_/1470262", "title"=>"GltB, GltA and GltC interact directly.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2015-07-01 02:57:37"}
• {"files"=>["https://ndownloader.figshare.com/files/2157915"], "description"=>"<p>(A) Localization of GltB-mCherry, GltA-mCherry GltC-mCherry in the indicated genetic backgrounds. Cells were transferred from exponentially growing cultures to a thin agar pad on a microscope slide and imaged by fluorescence microscopy. For the z-sections, the z positions are indicated by a barred circle. The localization patterns observed are indicated in the schematics and numbers represent % of cells with that pattern; n > 100. Scale bar, 2μm. (B) Time-lapse microscopy of cells containing GltB-mCherry, GltA-mCherry or GltC-mCherry. Cells of the indicated genotypes were treated as in (A) and imaged by time-lapse DIC and fluorescence microscopy at 60 s intervals. Same colored arrowheads indicate position of motility complex during cell movement. Left panel, fluorescence microscopy images; right panel, merged DIC and fluorescence microscopy images. (C) Fluorescence microscopy images and line scans of cells expressing GltB-mCherry or GltA-mCherry and AglZ-YFP. In the line scans, red lines refer to GltB/GltA-mCherry while green lines refer to AglZ-YFP. Cells were treated as in A. Scale bar, 2μm. (D) Time-lapse microscopy of cells containing GltB-mCherry or GltA-mCherry and AglZ-YFP. Cells containing the indicated fusions were treated as in (A) and imaged by time-lapse fluorescence microscopy at 60 s intervals. Same colored triangles indicate position of motility complex during cell movement. The corresponding linescans are shown in <a href=\"http://www.plosgenetics.org/article/info:doi/10.1371/journal.pgen.1005341#pgen.1005341.s004\" target=\"_blank\">S4 Fig</a>.</p>", "links"=>[], "tags"=>["OM integration", "OM lipoprotein", "cytoplasmic AglZ protein", "GltC proteins", "OM lipoproteins", "OM lipoprotein CglC", "membrane protein AglQ", "Gliding Motility Machinery", "GltA", "GltB", "Myxococcus xanthus Bacteria", "periplasmic protein", "OM proteins", "integral components", "cell envelope", "motility complexes", "Myxococcus xanthus move", "type iv pili", "Δ cglC"], "article_id"=>1470263, "categories"=>["Uncategorised"], "users"=>["Beata Jakobczak", "Daniela Keilberg", "Kristin Wuichet", "Lotte Søgaard-Andersen"], "doi"=>"https://dx.doi.org/10.1371/journal.pgen.1005341.g006", "stats"=>{"downloads"=>1, "page_views"=>9, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_GltB_and_GltA_are_incorporated_into_gliding_motility_complexes_/1470263", "title"=>"GltB and GltA are incorporated into gliding motility complexes.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2015-07-01 02:57:37"}
• {"files"=>["https://ndownloader.figshare.com/files/2157916"], "description"=>"<p>Cells were treated and analyzed as in <a href=\"http://www.plosgenetics.org/article/info:doi/10.1371/journal.pgen.1005341#pgen.1005341.g006\" target=\"_blank\">Fig 6A</a>. Note that all strains tested for GltB-mCherry and GltA-mCherry localization are <i>gltB</i>⁺ and <i>gltA</i>⁺, respectively. Scale bar, 2μm.</p>", "links"=>[], "tags"=>["OM integration", "OM lipoprotein", "cytoplasmic AglZ protein", "GltC proteins", "OM lipoproteins", "OM lipoprotein CglC", "membrane protein AglQ", "Gliding Motility Machinery", "GltA", "GltB", "Myxococcus xanthus Bacteria", "periplasmic protein", "OM proteins", "integral components", "cell envelope", "motility complexes", "Myxococcus xanthus move", "type iv pili", "Δ cglC"], "article_id"=>1470264, "categories"=>["Uncategorised"], "users"=>["Beata Jakobczak", "Daniela Keilberg", "Kristin Wuichet", "Lotte Søgaard-Andersen"], "doi"=>"https://dx.doi.org/10.1371/journal.pgen.1005341.g007", "stats"=>{"downloads"=>1, "page_views"=>16, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_GltB_and_GltA_incorporation_into_motility_complexes_depends_on_other_gliding_motility_proteins_/1470264", "title"=>"GltB and GltA incorporation into motility complexes depends on other gliding motility proteins.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2015-07-01 02:57:37"}
• {"files"=>["https://ndownloader.figshare.com/files/2157917"], "description"=>"<p>Cells were treated and analyzed as in <a href=\"http://www.plosgenetics.org/article/info:doi/10.1371/journal.pgen.1005341#pgen.1005341.g006\" target=\"_blank\">Fig 6A</a>. Scale bar, 2μm.</p>", "links"=>[], "tags"=>["OM integration", "OM lipoprotein", "cytoplasmic AglZ protein", "GltC proteins", "OM lipoproteins", "OM lipoprotein CglC", "membrane protein AglQ", "Gliding Motility Machinery", "GltA", "GltB", "Myxococcus xanthus Bacteria", "periplasmic protein", "OM proteins", "integral components", "cell envelope", "motility complexes", "Myxococcus xanthus move", "type iv pili", "Δ cglC"], "article_id"=>1470265, "categories"=>["Uncategorised"], "users"=>["Beata Jakobczak", "Daniela Keilberg", "Kristin Wuichet", "Lotte Søgaard-Andersen"], "doi"=>"https://dx.doi.org/10.1371/journal.pgen.1005341.g008", "stats"=>{"downloads"=>0, "page_views"=>16, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_AglZ_YFP_and_AglQ_mCherry_incorporation_into_motility_complexes_depends_on_CglC_GltB_GltA_and_GltC_/1470265", "title"=>"AglZ-YFP and AglQ-mCherry incorporation into motility complexes depends on CglC, GltB, GltA and GltC.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2015-07-01 02:57:37"}
• {"files"=>["https://ndownloader.figshare.com/files/2157920"], "description"=>"<p>(A) Motility and stimulation phenotypes of the indicated strains and strain mixtures. Cells were incubated at 32°C for 48 h on 1.5% agar to score for gliding motility. Scale bar, 50μm. (B) Localization of GltB-mCherry, GltA-mCherry, AglZ-YFP and AglQ-mCherry in the Δ<i>cglC</i> mutant background incubated alone or in the presence of the non-motile CglC donor DK6204. Recipient and donor were mixed in a 1:1 ratio and incubated as described in (A), transferred to a thin agar pad on a microscope slide and imaged by fluorescence microscopy. Scale bar, 2μm.</p>", "links"=>[], "tags"=>["OM integration", "OM lipoprotein", "cytoplasmic AglZ protein", "GltC proteins", "OM lipoproteins", "OM lipoprotein CglC", "membrane protein AglQ", "Gliding Motility Machinery", "GltA", "GltB", "Myxococcus xanthus Bacteria", "periplasmic protein", "OM proteins", "integral components", "cell envelope", "motility complexes", "Myxococcus xanthus move", "type iv pili", "Δ cglC"], "article_id"=>1470267, "categories"=>["Uncategorised"], "users"=>["Beata Jakobczak", "Daniela Keilberg", "Kristin Wuichet", "Lotte Søgaard-Andersen"], "doi"=>"https://dx.doi.org/10.1371/journal.pgen.1005341.g009", "stats"=>{"downloads"=>0, "page_views"=>10, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_CglC_stimulates_formation_of_motility_complexes_after_transfer_/1470267", "title"=>"CglC stimulates formation of motility complexes after transfer.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2015-07-01 02:57:37"}
• {"files"=>["https://ndownloader.figshare.com/files/2157925"], "description"=>"<p>¹ Plasmids mentioned in parentheses were integrated at the chromosomal Mx8 <i>attB</i> site with the exception of those marked with an asterisk (*), which were integrated at the native site by a single homologous recombination event. Constructs were transcribed from the native promoter (P<i>nat</i>) or the <i>pilA</i> promoter (P<i>pilA</i>) as indicated.</p><p><i>M</i>. <i>xanthus</i> strains used in this work<a href=\"http://www.plosgenetics.org/article/info:doi/10.1371/journal.pgen.1005341#t001fn001\" target=\"_blank\">¹</a>.</p>", "links"=>[], "tags"=>["OM integration", "OM lipoprotein", "cytoplasmic AglZ protein", "GltC proteins", "OM lipoproteins", "OM lipoprotein CglC", "membrane protein AglQ", "Gliding Motility Machinery", "GltA", "GltB", "Myxococcus xanthus Bacteria", "periplasmic protein", "OM proteins", "integral components", "cell envelope", "motility complexes", "Myxococcus xanthus move", "type iv pili", "Δ cglC"], "article_id"=>1470268, "categories"=>["Uncategorised"], "users"=>["Beata Jakobczak", "Daniela Keilberg", "Kristin Wuichet", "Lotte Søgaard-Andersen"], "doi"=>"https://dx.doi.org/10.1371/journal.pgen.1005341.t001", "stats"=>{"downloads"=>6, "page_views"=>6, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_M_xanthus_strains_used_in_this_work_1_/1470268", "title"=>"<i>M</i>. <i>xanthus</i> strains used in this work¹.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2015-07-01 02:57:37"}

PMC Usage Stats | Further Information

• {"unique-ip"=>"14", "full-text"=>"15", "pdf"=>"4", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"6", "supp-data"=>"1", "cited-by"=>"0", "year"=>"2015", "month"=>"7"}
• {"unique-ip"=>"17", "full-text"=>"15", "pdf"=>"9", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2015", "month"=>"8"}
• {"unique-ip"=>"24", "full-text"=>"24", "pdf"=>"10", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"2", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2015", "month"=>"9"}
• {"unique-ip"=>"25", "full-text"=>"31", "pdf"=>"8", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"5", "supp-data"=>"1", "cited-by"=>"0", "year"=>"2015", "month"=>"10"}
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Relative Metric

{"start_date"=>"2015-01-01T00:00:00Z", "end_date"=>"2015-12-31T00:00:00Z", "subject_areas"=>[]}

F1000Prime