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{"title"=>"Dissection of the TssB-TssC interface during type VI secretion sheath complex formation", "type"=>"journal", "authors"=>[{"first_name"=>"Xiang Y.", "last_name"=>"Zhang", "scopus_author_id"=>"57192504044"}, {"first_name"=>"Yannick R.", "last_name"=>"Brunet", "scopus_author_id"=>"36238714400"}, {"first_name"=>"Laureen", "last_name"=>"Logger", "scopus_author_id"=>"56041864700"}, {"first_name"=>"Badreddine", "last_name"=>"Douzi", "scopus_author_id"=>"35091005400"}, {"first_name"=>"Christian", "last_name"=>"Cambillau", "scopus_author_id"=>"7006765066"}, {"first_name"=>"Laure", "last_name"=>"Journet", "scopus_author_id"=>"55895149400"}, {"first_name"=>"Eric", "last_name"=>"Cascales", "scopus_author_id"=>"6603332760"}], "year"=>2013, "source"=>"PLoS ONE", "identifiers"=>{"pui"=>"372426124", "isbn"=>"1932-6203 (Electronic)\\n1932-6203 (Linking)", "sgr"=>"84894245287", "issn"=>"19326203", "pmid"=>"24282569", "scopus"=>"2-s2.0-84894245287", "doi"=>"10.1371/journal.pone.0081074"}, "id"=>"ea777661-5703-3989-af45-b200a86b27a9", "abstract"=>"The Type VI secretion system (T6SS) is a versatile machine that delivers toxins into either eukaryotic or bacterial cells. At a molecular level, the T6SS is composed of a membrane complex that anchors a long cytoplasmic tubular structure to the cell envelope. This structure is thought to resemble the tail of contractile bacteriophages. It is composed of the Hcp protein that assembles into hexameric rings stacked onto each other to form a tube similar to the phage tail tube. This tube is proposed to be wrapped by a structure called the sheath, composed of two proteins, TssB and TssC. It has been shown using fluorescence microscopy that the TssB and TssC proteins assemble into a tubular structure that cycles between long and short conformations suggesting that, similarly to the bacteriophage sheath, the T6SS sheath undergoes elongation and contraction events. The TssB and TssC proteins have been shown to interact and a specific α-helix of TssB is required for this interaction. Here, we confirm that the TssB and TssC proteins interact in enteroaggregative E. coli. We further show that this interaction requires the N-terminal region of TssC and the conserved α-helix of TssB. Using site-directed mutagenesis coupled to phenotypic analyses, we demonstrate that an hydrophobic motif located in the N-terminal region of this helix is required for interaction with TssC, sheath assembly and T6SS function.", "link"=>"http://www.mendeley.com/research/dissection-tssbtssc-interface-during-type-vi-secretion-sheath-complex-formation", "reader_count"=>33, "reader_count_by_academic_status"=>{"Unspecified"=>2, "Professor > Associate Professor"=>1, "Researcher"=>3, "Student > Ph. D. Student"=>10, "Student > Postgraduate"=>1, "Student > Master"=>7, "Student > Bachelor"=>7, "Lecturer"=>1, "Professor"=>1}, "reader_count_by_user_role"=>{"Unspecified"=>2, "Professor > Associate Professor"=>1, "Researcher"=>3, "Student > Ph. D. Student"=>10, "Student > Postgraduate"=>1, "Student > Master"=>7, "Student > Bachelor"=>7, "Lecturer"=>1, "Professor"=>1}, "reader_count_by_subject_area"=>{"Unspecified"=>2, "Biochemistry, Genetics and Molecular Biology"=>12, "Agricultural and Biological Sciences"=>14, "Business, Management and Accounting"=>2, "Veterinary Science and Veterinary Medicine"=>1, "Physics and Astronomy"=>1, "Immunology and Microbiology"=>1}, "reader_count_by_subdiscipline"=>{"Physics and Astronomy"=>{"Physics and Astronomy"=>1}, "Immunology and Microbiology"=>{"Immunology and Microbiology"=>1}, "Agricultural and Biological Sciences"=>{"Agricultural and Biological Sciences"=>14}, "Business, Management and Accounting"=>{"Business, Management and Accounting"=>2}, "Biochemistry, Genetics and Molecular Biology"=>{"Biochemistry, Genetics and Molecular Biology"=>12}, "Unspecified"=>{"Unspecified"=>2}, "Veterinary Science and Veterinary Medicine"=>{"Veterinary Science and Veterinary Medicine"=>1}}, "group_count"=>1}

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• http://doi.org/10.1016/j.str.2017.12.005
• http://doi.org/10.1371/journal.pone.0110810
• http://doi.org/10.1038/srep34405
• http://doi.org/10.3389/fmicb.2019.01965
• http://doi.org/10.1074/jbc.M114.600510
• http://doi.org/10.1074/jbc.M114.563429
• http://doi.org/10.1016/j.celrep.2014.05.034
• http://doi.org/10.3934/biophy.2015.2.88
• http://doi.org/10.1371/journal.pone.0184797
• http://doi.org/10.1016/j.bbamcr.2014.03.018

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Figshare

• {"files"=>["https://ndownloader.figshare.com/files/1294813"], "description"=>"<p>Amino-acid sequence (A) and helical wheel projection (B) of the TssB1 α-helix (from residue Pro-103 to residue Leu-131). The different motifs described in this study are highlighted in different colours: blue, N-terminal hydrophobic; red, polar/charged; green, leucine-rich. The residues of these motifs mutagenized in this study are underlined (A) or striped (B). Top-view (C) and side-view (D) projections of the TssB1 α-helix. The targeted residues are colored as in panel (A). Top- and side-views have been modelled using PyMOL v0.99. (E) Hcp release assay. Hcp_FLAG release was assessed by separating whole cells (C) and culture supernatant (SN) fractions from 2×10⁹ Δ<i>tssB1</i> cells producing TssB1 (<i>tssB⁺</i>) or TssB1 bearing substitutions within the hydrophobic (<i>tssB^VIL</i>), the polar/charged (<i>tssB^RR</i>) or the leucin-rich (<i>tssB^LL</i>) motif. Proteins were separated by 12.5%-acrylamide SDS-PAGE and Hcp and TolB were immunodetected using anti-FLAG monoclonal (lower panel) and anti-TolB polyclonal (upper panel) antibodies. (F) Bacterial two-hybrid assay. BTH101 reporter cells producing the T25 domain of the <i>Bordetella</i> adenylate cyclase fused to TssC1 (T25-C) and the T18 domain fused to TssB1 (T18-B) or TssB1 variants bearing substitutions within the hydrophobic (T18-B^VIL), the polar/charged (T18-B^RR) or the leucin-rich (T18-B^LL) motif were spotted on X-Gal indicator LB agar plates.</p>", "links"=>[], "tags"=>["hydrophobic", "motif", "tssb1", "t6ss"], "article_id"=>861804, "categories"=>["Biological Sciences"], "users"=>["Xiang Y. Zhang", "Yannick R. Brunet", "Laureen Logger", "Badreddine Douzi", "Christian Cambillau", "Laure Journet", "Eric Cascales"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0081074.g003", "stats"=>{"downloads"=>0, "page_views"=>14, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_The_hydrophobic_motif_of_the_TssB1_945_helix_is_required_for_T6SS_function_and_interaction_with_TssC1_/861804", "title"=>"The hydrophobic motif of the TssB1 α-helix is required for T6SS function and interaction with TssC1.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-11-25 03:33:50"}
• {"files"=>["https://ndownloader.figshare.com/files/1294809"], "description"=>"<p>BTH101 reporter cells carrying pairs of plasmids producing the indicated T6SS proteins or domains (B, TssB1; C, TssC1; C_Nt, N-terminal domain of TssC1; C_Ct, C-terminal domain of TssC1) fused to the T18 or T25 domain of the <i>Bordetella</i> adenylate cyclase were spotted on X-Gal indicator LB agar plates. Controls include T18 and T25 fusions to TolB and Pal, two proteins that interact but unrelated to the T6SS.</p>", "links"=>[], "tags"=>["interacts", "n-terminal"], "article_id"=>861801, "categories"=>["Biological Sciences"], "users"=>["Xiang Y. Zhang", "Yannick R. Brunet", "Laureen Logger", "Badreddine Douzi", "Christian Cambillau", "Laure Journet", "Eric Cascales"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0081074.g001", "stats"=>{"downloads"=>0, "page_views"=>3, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_TssB1_interacts_with_the_N_terminal_domain_of_TssC1_/861801", "title"=>"TssB1 interacts with the N-terminal domain of TssC1.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-11-25 03:33:50"}
• {"files"=>["https://ndownloader.figshare.com/files/1294815"], "description"=>"<p>(A) Hcp release assay. Hcp_FLAG release was assessed by separating whole cells (C) and culture supernatant (SN) fractions from 2×10⁹ Δ<i>tssB1</i> cells producing TssB1 (<i>tssB⁺</i>) or TssB1 bearing double or single substitutions within the hydrophobic motif (<i>tssB^VI</i>, V106W-I110W; <i>tssB^IL</i>, I110W-L117W; <i>tssB^VL</i>, V106W-L117W; <i>tssB^V</i>, V106W; <i>tssB^I</i>, I110W; <i>tssB^L</i>, L117W). Proteins were separated by 12.5%-acrylamide SDS-PAGE and Hcp and TolB were immunodetected using anti-FLAG monoclonal (lower panel) and anti-TolB polyclonal (upper panel) antibodies. (B) Bacterial two-hybrid assay. BTH101 reporter cells producing the T25 domain of the <i>Bordetella</i> adenylate cyclase fused to TssC1 (T25-C) and the T18 domain fused to TssB1 (T18-B) or TssB1 variants bearing substitutions within the hydrophobic motif (T18-B^VI, V106W-I110W; T18-B^IL, I110W-L117W; T18-B^VL, V106W-L117W; T18-B^V, V106W; T18-B^I, I110W; T18-B^L, L117W) were spotted on X-Gal indicator LB agar plates.</p>", "links"=>[], "tags"=>["hydrophobic", "motif", "tssb1"], "article_id"=>861806, "categories"=>["Biological Sciences"], "users"=>["Xiang Y. Zhang", "Yannick R. Brunet", "Laureen Logger", "Badreddine Douzi", "Christian Cambillau", "Laure Journet", "Eric Cascales"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0081074.g004", "stats"=>{"downloads"=>0, "page_views"=>6, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Mutagenesis_study_of_the_hydrophobic_motif_of_the_TssB1_945_helix_/861806", "title"=>"Mutagenesis study of the hydrophobic motif of the TssB1 α-helix.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-11-25 03:33:50"}
• {"files"=>["https://ndownloader.figshare.com/files/1294810"], "description"=>"<p>(A) Hcp release assay. Hcp_FLAG release was assessed by separating whole cells (C) and culture supernatant (SN) fractions from 2×10⁹ wild-type (WT), Δ<i>tssB1</i> (Δ<i>tssB</i>) cells or Δ<i>tssB1</i> cells producing TssB1 (<i>tssB⁺</i>) or TssB1 deleted of the α-helix 104-130 (<i>tssB</i>Δ<i>^hel</i>). Proteins were separated by 12.5%-acrylamide SDS-PAGE and Hcp was immunodetected using anti-FLAG monoclonal antibody (lower panel). The periplasmic TolB protein (immunodetected using an anti-TolB polyclonal antibodies, upper panel) was used as a marker to verify that no lysis occured. (B) Bacterial two-hybrid assay. BTH101 reporter cells carrying pairs of plasmids producing the indicated T6SS proteins (B, TssB1; BΔhel, TssB1 deleted of the α-helix; C1, TssC1) fused to the T18 or T25 domain of the <i>Bordetella</i> adenylate cyclase were spotted on X-Gal indicator LB agar plates.</p>", "links"=>[], "tags"=>["residues", "104", "130", "tssb1", "t6ss"], "article_id"=>861802, "categories"=>["Biological Sciences"], "users"=>["Xiang Y. Zhang", "Yannick R. Brunet", "Laureen Logger", "Badreddine Douzi", "Christian Cambillau", "Laure Journet", "Eric Cascales"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0081074.g002", "stats"=>{"downloads"=>0, "page_views"=>11, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_The_945_helix_located_between_residues_104_and_130_of_TssB1_is_required_for_T6SS_function_and_interaction_with_TssC1_/861802", "title"=>"The α-helix located between residues 104 and 130 of TssB1 is required for T6SS function and interaction with TssC1.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-11-25 03:33:50"}
• {"files"=>["https://ndownloader.figshare.com/files/1294826"], "description"=>"<div><p>The Type VI secretion system (T6SS) is a versatile machine that delivers toxins into either eukaryotic or bacterial cells. At a molecular level, the T6SS is composed of a membrane complex that anchors a long cytoplasmic tubular structure to the cell envelope. This structure is thought to resemble the tail of contractile bacteriophages. It is composed of the Hcp protein that assembles into hexameric rings stacked onto each other to form a tube similar to the phage tail tube. This tube is proposed to be wrapped by a structure called the sheath, composed of two proteins, TssB and TssC. It has been shown using fluorescence microscopy that the TssB and TssC proteins assemble into a tubular structure that cycles between long and short conformations suggesting that, similarly to the bacteriophage sheath, the T6SS sheath undergoes elongation and contraction events. The TssB and TssC proteins have been shown to interact and a specific α-helix of TssB is required for this interaction. Here, we confirm that the TssB and TssC proteins interact in enteroaggregative <i>E. coli</i>. We further show that this interaction requires the N-terminal region of TssC and the conserved α-helix of TssB. Using site-directed mutagenesis coupled to phenotypic analyses, we demonstrate that an hydrophobic motif located in the N-terminal region of this helix is required for interaction with TssC, sheath assembly and T6SS function.</p></div>", "links"=>[], "tags"=>["tssb-tssc", "interface", "vi", "secretion", "sheath"], "article_id"=>861815, "categories"=>["Biological Sciences"], "users"=>["Xiang Y. Zhang", "Yannick R. Brunet", "Laureen Logger", "Badreddine Douzi", "Christian Cambillau", "Laure Journet", "Eric Cascales"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0081074", "stats"=>{"downloads"=>1, "page_views"=>13, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Dissection_of_the_TssB_TssC_Interface_during_Type_VI_Secretion_Sheath_Complex_Formation_/861815", "title"=>"Dissection of the TssB-TssC Interface during Type VI Secretion Sheath Complex Formation", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2013-11-25 03:33:50"}
• {"files"=>["https://ndownloader.figshare.com/files/1294825"], "description"=>"<p>Time-lapse fluorescence microscopy recordings showing sheath dynamics in Δ<i>tssBC1</i> (Δ<i>tssB1</i>-Δ<i>tssC1</i>) or Δ<i>tssB1</i> cells producing TssB1-sfGFP (TssB1) (A) or TssB1-sfGFP bearing the indicated substitutions (B). Individual images were taken every 30 sec. Assembly and contraction events are indicated by the white open triangles. Scale bars are 2 µm.</p>", "links"=>[], "tags"=>["hydrophobic", "motif", "tssb1", "t6ss", "sheath"], "article_id"=>861814, "categories"=>["Biological Sciences"], "users"=>["Xiang Y. Zhang", "Yannick R. Brunet", "Laureen Logger", "Badreddine Douzi", "Christian Cambillau", "Laure Journet", "Eric Cascales"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0081074.g005", "stats"=>{"downloads"=>0, "page_views"=>10, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_The_hydrophobic_motif_of_the_TssB1_945_helix_is_required_for_T6SS_sheath_assembly_/861814", "title"=>"The hydrophobic motif of the TssB1 α-helix is required for T6SS sheath assembly.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-11-25 03:33:50"}

PMC Usage Stats | Further Information

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Relative Metric

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F1000Prime