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Supramolecular structure of the Salmonella typhimurium type III protein secretion system
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4
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0034730179
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Molecular characterization and assembly of the needle complex of the Salmonella typhimurium type III protein secretion system
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Kubori T., Sukhan A., Aizawa S.I., and Galan J.E. Molecular characterization and assembly of the needle complex of the Salmonella typhimurium type III protein secretion system. Proc Natl Acad Sci USA 97 (2000) 10225-10230
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The needle length of bacterial injectisomes is determined by a molecular ruler
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Journet L., Agrain C., Broz P., and Cornelis G.R. The needle length of bacterial injectisomes is determined by a molecular ruler. Science 302 (2003) 1757-1760
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Determination of bacteriophage λ tail length by a protein ruler
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0034715545
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Mutational analysis of two structural genes of the temperate lactococcal bacteriophage TP901-1 involved in tail length determination and baseplate assembly
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Pedersen M., Ostergaard S., Bresciani J., and Vogensen F.K. Mutational analysis of two structural genes of the temperate lactococcal bacteriophage TP901-1 involved in tail length determination and baseplate assembly. Virology 276 (2000) 315-328
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12
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0029989240
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Mutations in fliK and flhB affecting flagellar hook and filament assembly in Salmonella typhimurium
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Williams A.W., Yamaguchi S., Togashi F., Aizawa S.I., Kawagishi I., and Macnab R.M. Mutations in fliK and flhB affecting flagellar hook and filament assembly in Salmonella typhimurium. J Bacteriol 178 (1996) 2960-2970
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Williams, A.W.1
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0028027526
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Isolation and characterization of FliK-independent flagellation mutants from Salmonella typhimurium
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Kutsukake K., Minamino T., and Yokoseki T. Isolation and characterization of FliK-independent flagellation mutants from Salmonella typhimurium. J Bacteriol 176 (1994) 7625-7629
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Kutsukake, K.1
Minamino, T.2
Yokoseki, T.3
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14
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0028093390
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Roles of FliK and FlhB in determination of flagellar hook length in Salmonella typhimurium
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Hirano T., Yamaguchi S., Oosawa K., and Aizawa S. Roles of FliK and FlhB in determination of flagellar hook length in Salmonella typhimurium. J Bacteriol 176 (1994) 5439-5449
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Hirano, T.1
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Aizawa, S.4
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15
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0038016732
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Substrate specificity of type III flagellar protein export in Salmonella is controlled by subdomain interactions in FlhB
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Fraser G.M., Hirano T., Ferris H.U., Devgan L.L., Kihara M., and Macnab R.M. Substrate specificity of type III flagellar protein export in Salmonella is controlled by subdomain interactions in FlhB. Mol Microbiol 48 (2003) 1043-1057
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Fraser, G.M.1
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Ferris, H.U.3
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Macnab, R.M.6
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16
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3343019337
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Domain organization and function of Salmonella FliK, a flagellar hook-length control protein
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This study investigated the structural properties of FliK and showed that FliK has an elongated shape.
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Minamino T., Saijo-Hamano Y., Furukawa Y., Gonzalez-Pedrajo B., Macnab R.M., and Namba K. Domain organization and function of Salmonella FliK, a flagellar hook-length control protein. J Mol Biol 341 (2004) 491-502. This study investigated the structural properties of FliK and showed that FliK has an elongated shape.
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J Mol Biol
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Minamino, T.1
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Macnab, R.M.5
Namba, K.6
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17
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0036282334
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Spa32 regulates a switch in substrate specificity of the type III secreton of Shigella flexneri from needle components to Ipa proteins
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Magdalena J., Hachani A., Chamekh M., Jouihri N., Gounon P., Blocker A., and Allaoui A. Spa32 regulates a switch in substrate specificity of the type III secreton of Shigella flexneri from needle components to Ipa proteins. J Bacteriol 184 (2002) 3433-3441
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Magdalena, J.1
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Gounon, P.5
Blocker, A.6
Allaoui, A.7
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18
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0036178888
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Shigella Spa32 is an essential secretory protein for functional type III secretion machinery and uniformity of its needle length
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Tamano K., Katayama E., Toyotome T., and Sasakawa C. Shigella Spa32 is an essential secretory protein for functional type III secretion machinery and uniformity of its needle length. J Bacteriol 184 (2002) 1244-1252
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Tamano, K.1
Katayama, E.2
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19
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0028124264
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YscU, a Yersinia enterocolitica inner membrane protein involved in Yop secretion
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Allaoui A., Woestyn S., Sluiters C., and Cornelis G.R. YscU, a Yersinia enterocolitica inner membrane protein involved in Yop secretion. J Bacteriol 176 (1994) 4534-4542
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20
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0037379368
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YscP and YscU regulate substrate specificity of the Yersinia type III secretion system
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Edqvist P.J., Olsson J., Lavander M., Sundberg L., Forsberg A., Wolf-Watz H., and Lloyd S.A. YscP and YscU regulate substrate specificity of the Yersinia type III secretion system. J Bacteriol 185 (2003) 2259-2266
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Edqvist, P.J.1
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Lloyd, S.A.7
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21
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0038807558
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Characterisation of the type III secretion protein YscU in Yersinia pseudotuberculosis. YscU cleavage - dispensable for TTSS but essential for survival
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Lavander M., Sundberg L., Edqvist P.J., Lloyd S.A., Wolf-Watz H., and Forsberg A. Characterisation of the type III secretion protein YscU in Yersinia pseudotuberculosis. YscU cleavage - dispensable for TTSS but essential for survival. Adv Exp Med Biol 529 (2003) 109-112
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Lavander, M.1
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Wolf-Watz, H.5
Forsberg, A.6
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22
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16244407371
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Characterization of a type III secretion substrate specificity switch (T3S4) domain in YscP from Yersinia enterocolitica
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This study localized the ∼100 amino acid domain of YscP that is involved in substrate specificity switching (T3S4 domain) and shows that this domain is highly conserved between FliK and several proteins controlling the length of injectisomes. Together with the study by Edqvist et al. [20], this study showed the conservation of the substrate specificity switch between the flagellum and the injectisome.
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Agrain C., Callebaut I., Journet L., Sorg I., Paroz C., Mota L.J., and Cornelis G.R. Characterization of a type III secretion substrate specificity switch (T3S4) domain in YscP from Yersinia enterocolitica. Mol Microbiol 56 (2005) 54-67. This study localized the ∼100 amino acid domain of YscP that is involved in substrate specificity switching (T3S4 domain) and shows that this domain is highly conserved between FliK and several proteins controlling the length of injectisomes. Together with the study by Edqvist et al. [20], this study showed the conservation of the substrate specificity switch between the flagellum and the injectisome.
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(2005)
Mol Microbiol
, vol.56
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Agrain, C.1
Callebaut, I.2
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Sorg, I.4
Paroz, C.5
Mota, L.J.6
Cornelis, G.R.7
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23
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17144424247
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N-terminal signal region of FliK is dispensable for length control of the flagellar hook
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•], and the data should be compared. These data do not reveal as large a discrepancy as the titles of these papers might suggest.
-
•], and the data should be compared. These data do not reveal as large a discrepancy as the titles of these papers might suggest.
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(2005)
Mol Microbiol
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Hirano, T.1
Shibata, S.2
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24
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0032947339
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YscP of Yersinia pestis is a secreted component of the Yop secretion system
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Payne P.L., and Straley S.C. YscP of Yersinia pestis is a secreted component of the Yop secretion system. J Bacteriol 181 (1999) 2852-2862
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Payne, P.L.1
Straley, S.C.2
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25
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0033822550
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2+
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2+. Mol Microbiol 37 (2000) 1005-1018
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Mol Microbiol
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Stainier, I.1
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Cornelis, G.R.9
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26
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0036437055
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Molecular and functional analysis of the type III secretion signal of the Salmonella enterica InvJ protein
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Russmann H., Kubori T., Sauer J., and Galan J.E. Molecular and functional analysis of the type III secretion signal of the Salmonella enterica InvJ protein. Mol Microbiol 46 (2002) 769-779
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Russmann, H.1
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27
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0032827183
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FliK, the protein responsible for flagellar hook length control in Salmonella, is exported during hook assembly
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Minamino T., Gonzalez-Pedrajo B., Yamaguchi K., Aizawa S.I., and Macnab R.M. FliK, the protein responsible for flagellar hook length control in Salmonella, is exported during hook assembly. Mol Microbiol 34 (1999) 295-304
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Macnab, R.M.5
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28
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23844543359
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Secretion of YscP from Yersinia enterocolitica is essential to control the length of the injectisome needle but not to change the type III secretion substrate specificity
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•], which addresses the same topic in the flagellum.
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•], which addresses the same topic in the flagellum.
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Mol Microbiol
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Agrain, C.1
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Isolation, characterization and structure of bacterial flagellar motors containing the switch complex
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Francis, N.R.1
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31
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27344457144
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The V-antigen of Yersinia forms a distinct structure at the tip of injectisome needles
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This study demonstrated that the protective antigen against plague forms a distinct structure at the tip of the needle. It contributes more to the understanding of T3S than to length control. However, it shows that needles deprived of their tip have a normal length and, thus, that LcrV is not an anchor for the ruler.
-
Mueller C.A., Broz P., Muller S.A., Ringler P., Erne-Brand F., Sorg I., Kuhn M., Engel A., and Cornelis G.R. The V-antigen of Yersinia forms a distinct structure at the tip of injectisome needles. Science 310 (2005) 674-676. This study demonstrated that the protective antigen against plague forms a distinct structure at the tip of the needle. It contributes more to the understanding of T3S than to length control. However, it shows that needles deprived of their tip have a normal length and, thus, that LcrV is not an anchor for the ruler.
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(2005)
Science
, vol.310
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Mueller, C.A.1
Broz, P.2
Muller, S.A.3
Ringler, P.4
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Sorg, I.6
Kuhn, M.7
Engel, A.8
Cornelis, G.R.9
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32
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0032503008
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Effect of cellular level of FliK on flagellar hook and filament assembly in Salmonella typhimurium
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Muramoto K., Makishima S., Aizawa S.I., and Macnab R.M. Effect of cellular level of FliK on flagellar hook and filament assembly in Salmonella typhimurium. J Mol Biol 277 (1998) 871-882
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20044379025
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Optimization of virulence functions through glucosylation of Shigella LPS
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West, N.P.1
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