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Adam Wise - One of the best experts on this subject based on the ideXlab platform.
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characterisation of shigella spa33 and thermotoga flim n reveals a new model for c Ring Assembly in t3ss
Molecular Microbiology, 2016Co-Authors: Melanie A Mcdowell, Julien Marcoux, Gareth Mcvicker, Steven Johnson, Yu Hang Fong, Rebecca Stevens, Lesley A H Bowman, Matteo T Degiacomi, Adam Wise, Miriam E FriedeAbstract:Flagellar type III secretion systems (T3SS) contain an essential cytoplasmic‐Ring (C‐Ring) largely composed of two proteins FliM and FliN, whereas an analogous substructure for the closely related non‐flagellar (NF) T3SS has not been observed in situ. We show that the spa33 gene encoding the putative NF‐T3SS C‐Ring component in S higella flexneri is alternatively translated to produce both full‐length (Spa33‐FL) and a short variant (Spa33‐C), with both required for secretion. They associate in a 1:2 complex (Spa33‐FL/C2) that further oligomerises into elongated arrays in vitro. The structure of Spa33‐C 2 and identification of an unexpected intramolecular pseudodimer in Spa33‐FL reveal a molecular model for their higher order Assembly within NF‐T3SS. Spa33‐FL and Spa33‐C are identified as functional counterparts of a FliM–FliN fusion and free FliN respectively. Furthermore, we show that T hermotoga maritima FliM and FliN form a 1:3 complex structurally equivalent to Spa33‐FL/C2, allowing us to propose a unified model for C‐Ring Assembly by NF‐T3SS and flagellar‐T3SS.
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Characterisation of Shigella Spa33 and Thermotoga FliM/N reveals a new model for C‐Ring Assembly in T3SS
Molecular microbiology, 2015Co-Authors: Melanie A Mcdowell, Julien Marcoux, Gareth Mcvicker, Steven Johnson, Yu Hang Fong, Lesley A H Bowman, Matteo T Degiacomi, Rebecca V Stevens, Jun Yan, Adam WiseAbstract:Flagellar type III secretion systems (T3SS) contain an essential cytoplasmic-Ring (C-Ring) largely composed of two proteins FliM and FliN, whereas an analogous substructure for the closely related non-flagellar (NF) T3SS has not been observed in situ. We show that the spa33 gene encoding the putative NF-T3SS C-Ring component in Shigella flexneri is alternatively translated to produce both full-length (Spa33-FL) and a short variant (Spa33-C), with both required for secretion. They associate in a 1:2 complex (Spa33-FL/C2) that further oligomerises into elongated arrays in vitro. The structure of Spa33-C2 and identification of an unexpected intramolecular pseudodimer in Spa33-FL reveal a molecular model for their higher order Assembly within NF-T3SS. Spa33-FL and Spa33-C are identified as functional counterparts of a FliM-FliN fusion and free FliN respectively. Furthermore, we show that Thermotoga maritima FliM and FliN form a 1:3 complex structurally equivalent to Spa33-FL/C2 , allowing us to propose a unified model for C-Ring Assembly by NF-T3SS and flagellar-T3SS.
Melanie A Mcdowell - One of the best experts on this subject based on the ideXlab platform.
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characterisation of shigella spa33 and thermotoga flim n reveals a new model for c Ring Assembly in t3ss
Molecular Microbiology, 2016Co-Authors: Melanie A Mcdowell, Julien Marcoux, Gareth Mcvicker, Steven Johnson, Yu Hang Fong, Rebecca Stevens, Lesley A H Bowman, Matteo T Degiacomi, Adam Wise, Miriam E FriedeAbstract:Flagellar type III secretion systems (T3SS) contain an essential cytoplasmic‐Ring (C‐Ring) largely composed of two proteins FliM and FliN, whereas an analogous substructure for the closely related non‐flagellar (NF) T3SS has not been observed in situ. We show that the spa33 gene encoding the putative NF‐T3SS C‐Ring component in S higella flexneri is alternatively translated to produce both full‐length (Spa33‐FL) and a short variant (Spa33‐C), with both required for secretion. They associate in a 1:2 complex (Spa33‐FL/C2) that further oligomerises into elongated arrays in vitro. The structure of Spa33‐C 2 and identification of an unexpected intramolecular pseudodimer in Spa33‐FL reveal a molecular model for their higher order Assembly within NF‐T3SS. Spa33‐FL and Spa33‐C are identified as functional counterparts of a FliM–FliN fusion and free FliN respectively. Furthermore, we show that T hermotoga maritima FliM and FliN form a 1:3 complex structurally equivalent to Spa33‐FL/C2, allowing us to propose a unified model for C‐Ring Assembly by NF‐T3SS and flagellar‐T3SS.
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Characterisation of Shigella Spa33 and Thermotoga FliM/N reveals a new model for C‐Ring Assembly in T3SS
Molecular microbiology, 2015Co-Authors: Melanie A Mcdowell, Julien Marcoux, Gareth Mcvicker, Steven Johnson, Yu Hang Fong, Lesley A H Bowman, Matteo T Degiacomi, Rebecca V Stevens, Jun Yan, Adam WiseAbstract:Flagellar type III secretion systems (T3SS) contain an essential cytoplasmic-Ring (C-Ring) largely composed of two proteins FliM and FliN, whereas an analogous substructure for the closely related non-flagellar (NF) T3SS has not been observed in situ. We show that the spa33 gene encoding the putative NF-T3SS C-Ring component in Shigella flexneri is alternatively translated to produce both full-length (Spa33-FL) and a short variant (Spa33-C), with both required for secretion. They associate in a 1:2 complex (Spa33-FL/C2) that further oligomerises into elongated arrays in vitro. The structure of Spa33-C2 and identification of an unexpected intramolecular pseudodimer in Spa33-FL reveal a molecular model for their higher order Assembly within NF-T3SS. Spa33-FL and Spa33-C are identified as functional counterparts of a FliM-FliN fusion and free FliN respectively. Furthermore, we show that Thermotoga maritima FliM and FliN form a 1:3 complex structurally equivalent to Spa33-FL/C2 , allowing us to propose a unified model for C-Ring Assembly by NF-T3SS and flagellar-T3SS.
Miriam E Friede - One of the best experts on this subject based on the ideXlab platform.
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characterisation of shigella spa33 and thermotoga flim n reveals a new model for c Ring Assembly in t3ss
Molecular Microbiology, 2016Co-Authors: Melanie A Mcdowell, Julien Marcoux, Gareth Mcvicker, Steven Johnson, Yu Hang Fong, Rebecca Stevens, Lesley A H Bowman, Matteo T Degiacomi, Adam Wise, Miriam E FriedeAbstract:Flagellar type III secretion systems (T3SS) contain an essential cytoplasmic‐Ring (C‐Ring) largely composed of two proteins FliM and FliN, whereas an analogous substructure for the closely related non‐flagellar (NF) T3SS has not been observed in situ. We show that the spa33 gene encoding the putative NF‐T3SS C‐Ring component in S higella flexneri is alternatively translated to produce both full‐length (Spa33‐FL) and a short variant (Spa33‐C), with both required for secretion. They associate in a 1:2 complex (Spa33‐FL/C2) that further oligomerises into elongated arrays in vitro. The structure of Spa33‐C 2 and identification of an unexpected intramolecular pseudodimer in Spa33‐FL reveal a molecular model for their higher order Assembly within NF‐T3SS. Spa33‐FL and Spa33‐C are identified as functional counterparts of a FliM–FliN fusion and free FliN respectively. Furthermore, we show that T hermotoga maritima FliM and FliN form a 1:3 complex structurally equivalent to Spa33‐FL/C2, allowing us to propose a unified model for C‐Ring Assembly by NF‐T3SS and flagellar‐T3SS.
Hong Ling - One of the best experts on this subject based on the ideXlab platform.
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Structures of monomeric, dimeric and trimeric PCNA: PCNA-Ring Assembly and opening.
Acta Crystallographica Section D Biological Crystallography, 2008Co-Authors: Vladena Hlinkova, Guangxin Xing, Jacob Bauer, Yoon Jung Shin, Isabelle Dionne, Kanagalaghatta R. Rajashankar, Stephen D. Bell, Hong LingAbstract:DNA sliding clamps form an oligomeric Ring encircling DNA and serve as a moving platform for DNA-processing proteins. The opening and closing of a sliding-clamp Ring is essential to load the clamp onto DNA in order to perform its functions. The molecular details of how clamp Rings open and enclose DNA are still not clear. Three PCNA homologues have been found in Sulfolobus solfataricus which form a heterotrimer. Taking advantage of their hetero-oligomeric nature, the structures of the PCNAs in monomeric PCNA3, dimeric PCNA1–PCNA2 and trimeric PCNA1–PCNA2–PCNA3 forms were determined at resolutions of 2.6–1.9 A. The distinct oligomeric structures represent different stages in Ring formation, which were verified in solution by ultracentrifugation analysis. The heterodimer opens in a V-shape of 130°, while the heterotrimers form a Ring with a 120° rotation between monomers. The association of a rigid PCNA3 monomer with an opened PCNA1–PCNA2 heterodimer closes the Ring and introduces a spRing tension in the PCNA1–PCNA2 interface, thus bending the nine-stranded intermolecular β-sheet to fit the 120° rotation. The release of the spRing tension as PCNA3 dissociates from the Ring may facilitate Ring opening. The structural features in different assemblies present a molecular model for clamp Ring Assembly and opening.
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Structures of monomeric, dimeric and trimeric PCNA: PCNA-Ring Assembly and opening.
Acta crystallographica. Section D Biological crystallography, 2008Co-Authors: Vladena Hlinkova, Guangxin Xing, Jacob Bauer, Yoon Jung Shin, Isabelle Dionne, Kanagalaghatta R. Rajashankar, Stephen D. Bell, Hong LingAbstract:DNA sliding clamps form an oligomeric Ring encircling DNA and serve as a moving platform for DNA-processing proteins. The opening and closing of a sliding-clamp Ring is essential to load the clamp onto DNA in order to perform its functions. The molecular details of how clamp Rings open and enclose DNA are still not clear. Three PCNA homologues have been found in Sulfolobus solfataricus which form a heterotrimer. Taking advantage of their hetero-oligomeric nature, the structures of the PCNAs in monomeric PCNA3, dimeric PCNA1-PCNA2 and trimeric PCNA1-PCNA2-PCNA3 forms were determined at resolutions of 2.6-1.9 A. The distinct oligomeric structures represent different stages in Ring formation, which were verified in solution by ultracentrifugation analysis. The heterodimer opens in a V-shape of 130 degrees , while the heterotrimers form a Ring with a 120 degrees rotation between monomers. The association of a rigid PCNA3 monomer with an opened PCNA1-PCNA2 heterodimer closes the Ring and introduces a spRing tension in the PCNA1-PCNA2 interface, thus bending the nine-stranded intermolecular beta-sheet to fit the 120 degrees rotation. The release of the spRing tension as PCNA3 dissociates from the Ring may facilitate Ring opening. The structural features in different assemblies present a molecular model for clamp Ring Assembly and opening.
Yu Hang Fong - One of the best experts on this subject based on the ideXlab platform.
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characterisation of shigella spa33 and thermotoga flim n reveals a new model for c Ring Assembly in t3ss
Molecular Microbiology, 2016Co-Authors: Melanie A Mcdowell, Julien Marcoux, Gareth Mcvicker, Steven Johnson, Yu Hang Fong, Rebecca Stevens, Lesley A H Bowman, Matteo T Degiacomi, Adam Wise, Miriam E FriedeAbstract:Flagellar type III secretion systems (T3SS) contain an essential cytoplasmic‐Ring (C‐Ring) largely composed of two proteins FliM and FliN, whereas an analogous substructure for the closely related non‐flagellar (NF) T3SS has not been observed in situ. We show that the spa33 gene encoding the putative NF‐T3SS C‐Ring component in S higella flexneri is alternatively translated to produce both full‐length (Spa33‐FL) and a short variant (Spa33‐C), with both required for secretion. They associate in a 1:2 complex (Spa33‐FL/C2) that further oligomerises into elongated arrays in vitro. The structure of Spa33‐C 2 and identification of an unexpected intramolecular pseudodimer in Spa33‐FL reveal a molecular model for their higher order Assembly within NF‐T3SS. Spa33‐FL and Spa33‐C are identified as functional counterparts of a FliM–FliN fusion and free FliN respectively. Furthermore, we show that T hermotoga maritima FliM and FliN form a 1:3 complex structurally equivalent to Spa33‐FL/C2, allowing us to propose a unified model for C‐Ring Assembly by NF‐T3SS and flagellar‐T3SS.
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Characterisation of Shigella Spa33 and Thermotoga FliM/N reveals a new model for C‐Ring Assembly in T3SS
Molecular microbiology, 2015Co-Authors: Melanie A Mcdowell, Julien Marcoux, Gareth Mcvicker, Steven Johnson, Yu Hang Fong, Lesley A H Bowman, Matteo T Degiacomi, Rebecca V Stevens, Jun Yan, Adam WiseAbstract:Flagellar type III secretion systems (T3SS) contain an essential cytoplasmic-Ring (C-Ring) largely composed of two proteins FliM and FliN, whereas an analogous substructure for the closely related non-flagellar (NF) T3SS has not been observed in situ. We show that the spa33 gene encoding the putative NF-T3SS C-Ring component in Shigella flexneri is alternatively translated to produce both full-length (Spa33-FL) and a short variant (Spa33-C), with both required for secretion. They associate in a 1:2 complex (Spa33-FL/C2) that further oligomerises into elongated arrays in vitro. The structure of Spa33-C2 and identification of an unexpected intramolecular pseudodimer in Spa33-FL reveal a molecular model for their higher order Assembly within NF-T3SS. Spa33-FL and Spa33-C are identified as functional counterparts of a FliM-FliN fusion and free FliN respectively. Furthermore, we show that Thermotoga maritima FliM and FliN form a 1:3 complex structurally equivalent to Spa33-FL/C2 , allowing us to propose a unified model for C-Ring Assembly by NF-T3SS and flagellar-T3SS.
