메뉴 건너뛰기




Volumn 345, Issue 1, 2006, Pages 93-98

Localization of the flagellum-specific secretion signal in Salmonella flagellin

Author keywords

Export signal; Flagellin; Flagellum specific export; Salmonella typhimurium; Type III secretion

Indexed keywords

FLAGELLIN; MOLECULAR MOTOR;

EID: 33745804572     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2006.04.055     Document Type: Article
Times cited : (40)

References (19)
  • 1
    • 33747631210 scopus 로고    scopus 로고
    • R.M. Macnab, Flagella and motility, In: Escherichia coli and Salmonella. Cellular and Molecular Biology second ed., American Society for Microbiology Publications, Washington, DC, (1995), pp. 123-145.
  • 2
    • 8844249277 scopus 로고    scopus 로고
    • Type III flagellar protein export and flagellar assembly
    • Macnab R.M. Type III flagellar protein export and flagellar assembly. Biochim. Biophys. Acta 1694 (2004) 207-217
    • (2004) Biochim. Biophys. Acta , vol.1694 , pp. 207-217
    • Macnab, R.M.1
  • 3
    • 2642559479 scopus 로고    scopus 로고
    • Self-assembly and type III protein export of the bacterial flagellum
    • Minamino T., and Namba K. Self-assembly and type III protein export of the bacterial flagellum. J. Mol. Microbiol. Biotechnol. 7 (2004) 5-17
    • (2004) J. Mol. Microbiol. Biotechnol. , vol.7 , pp. 5-17
    • Minamino, T.1    Namba, K.2
  • 4
    • 0037387967 scopus 로고    scopus 로고
    • Substrate specificity classes and the recognition signal for Salmonella type III flagellar export
    • Hirano T., Minamino T., Namba K., and Macnab R.M. Substrate specificity classes and the recognition signal for Salmonella type III flagellar export. J. Bacteriol. 185 (2003) 2485-2492
    • (2003) J. Bacteriol. , vol.185 , pp. 2485-2492
    • Hirano, T.1    Minamino, T.2    Namba, K.3    Macnab, R.M.4
  • 5
    • 0037453098 scopus 로고    scopus 로고
    • Type III secretion systems and bacterial flagella: insights into their function from structural similarities
    • Blocker A., Komoriya K., and Aizawa S.-I. Type III secretion systems and bacterial flagella: insights into their function from structural similarities. Proc. Natl. Acad. Sci. USA 100 (2003) 3021-3030
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 3021-3030
    • Blocker, A.1    Komoriya, K.2    Aizawa, S.-I.3
  • 6
    • 0035151519 scopus 로고    scopus 로고
    • Yersinia YopE is targeted for type III secretion by N-terminal, not mRNA, signals
    • Lloyd S.A., Norman M., Rosqvist R., and Wolf-Watz H. Yersinia YopE is targeted for type III secretion by N-terminal, not mRNA, signals. Mol. Microbiol. 39 (2001) 520-531
    • (2001) Mol. Microbiol. , vol.39 , pp. 520-531
    • Lloyd, S.A.1    Norman, M.2    Rosqvist, R.3    Wolf-Watz, H.4
  • 7
    • 14244263014 scopus 로고    scopus 로고
    • Type III secretion of the Salmonella effector protein SopE is Mediated via an N-terminal amino acid signal and not an mRNA sequence
    • Karavolos M.H., Wilson M., Henderson J., Lee J.J., and Khan C.M.A. Type III secretion of the Salmonella effector protein SopE is Mediated via an N-terminal amino acid signal and not an mRNA sequence. J. Bacteriol. 187 (2005) 1559-1567
    • (2005) J. Bacteriol. , vol.187 , pp. 1559-1567
    • Karavolos, M.H.1    Wilson, M.2    Henderson, J.3    Lee, J.J.4    Khan, C.M.A.5
  • 8
    • 0942279512 scopus 로고    scopus 로고
    • Salmonella type III secretion-associated chaperones confer secretion-pathway specificity
    • Lee S.H., and Galán J.E. Salmonella type III secretion-associated chaperones confer secretion-pathway specificity. Mol. Microbiol. 51 (2004) 483-495
    • (2004) Mol. Microbiol. , vol.51 , pp. 483-495
    • Lee, S.H.1    Galán, J.E.2
  • 10
    • 0027942085 scopus 로고
    • Information essential for cell-cycle-dependent secretion of the 591-residue Caulobacter hook protein is confined to a 21-amino-acid sequence near the N-terminus
    • Kornacker M.G., and Newton A. Information essential for cell-cycle-dependent secretion of the 591-residue Caulobacter hook protein is confined to a 21-amino-acid sequence near the N-terminus. Mol. Microbiol. 14 (1994) 73-85
    • (1994) Mol. Microbiol. , vol.14 , pp. 73-85
    • Kornacker, M.G.1    Newton, A.2
  • 11
    • 0025367437 scopus 로고
    • Flagellar hook and hook-associated proteins of Salmonella typhimurium and their relationship to other axial components of the flagellum
    • Homma M., DeRosier D.J., and Macnab R.M. Flagellar hook and hook-associated proteins of Salmonella typhimurium and their relationship to other axial components of the flagellum. J. Mol. Biol. 213 (1990) 819-832
    • (1990) J. Mol. Biol. , vol.213 , pp. 819-832
    • Homma, M.1    DeRosier, D.J.2    Macnab, R.M.3
  • 12
    • 0024415907 scopus 로고
    • Terminal regions of flagellin are disordered in solution
    • Vonderviszt F., Kanto S., Aizawa S.-I., and Namba K. Terminal regions of flagellin are disordered in solution. J. Mol. Biol. 209 (1989) 127-133
    • (1989) J. Mol. Biol. , vol.209 , pp. 127-133
    • Vonderviszt, F.1    Kanto, S.2    Aizawa, S.-I.3    Namba, K.4
  • 13
    • 0026737755 scopus 로고
    • Terminal disorder: a common structural feature of the axial proteins of the bacterial flagellum?
    • Vonderviszt F., Ishima R., Akasaka K., and Aizawa S.-I. Terminal disorder: a common structural feature of the axial proteins of the bacterial flagellum?. J. Mol. Biol. 226 (1992) 575-579
    • (1992) J. Mol. Biol. , vol.226 , pp. 575-579
    • Vonderviszt, F.1    Ishima, R.2    Akasaka, K.3    Aizawa, S.-I.4
  • 16
    • 0028329280 scopus 로고
    • FlgD is a scaffolding protein needed for flagellar hook assembly in Salmonella typhimurium
    • Ohnishi K., Ohto Y., Aizawa S.-I., Macnab R.M., and Iino T. FlgD is a scaffolding protein needed for flagellar hook assembly in Salmonella typhimurium. J. Bacteriol. 176 (1994) 2272-2281
    • (1994) J. Bacteriol. , vol.176 , pp. 2272-2281
    • Ohnishi, K.1    Ohto, Y.2    Aizawa, S.-I.3    Macnab, R.M.4    Iino, T.5
  • 18
    • 0031791224 scopus 로고    scopus 로고
    • The type III secretion determinants of the flagellar anti-transcription factor, FlgM, extend from the amino-terminus into the anti-sigma28 domain
    • Chilcott G.S., and Hughes K.T. The type III secretion determinants of the flagellar anti-transcription factor, FlgM, extend from the amino-terminus into the anti-sigma28 domain. Mol. Microbiol. 30 (1998) 1029-1040
    • (1998) Mol. Microbiol. , vol.30 , pp. 1029-1040
    • Chilcott, G.S.1    Hughes, K.T.2
  • 19
    • 0027968068 scopus 로고
    • CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., and Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22 (1994) 4673-4680
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.