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Volumn 280, Issue 5363, 1998, Pages 602-605

Supramolecular structure of the salmonella typhimurium type III protein secretion system

Author keywords

[No Author keywords available]

Indexed keywords

ARTICLE; BACTERIAL MEMBRANE; FLAGELLUM; GENE TRANSLOCATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN ISOLATION; PROTEIN PROCESSING; PROTEIN SECRETION; PROTEIN STRUCTURE; SALMONELLA TYPHIMURIUM;

EID: 0032562678     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.280.5363.602     Document Type: Article
Times cited : (730)

References (29)
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    • Salmonella typhimurium strains were derivatives of SJW1103 [S. Yamaguchi, H. Fujita, A. Ishihara, S. Aizawa, R. M. Macnab, J. Bacteriol. 166,187 (1986)] or SL1344 [S. K. Hoiseth and B. A. Stocker, Nature 291, 238 (1981)]. The S. typhimurium flagellar mutants examined were ΔflhC, flgA, flgB, flgC, flgD, flgE, flgF, flgG, flhA, flhB, flhC, fliE, fliF, fliG, fliH, flil, fliJ, fliM, fliN, Δflio-fliR, fliP, ΔfliP-fliR, fliP, and fliQ.
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    • Yamaguchi, S.1    Fujita, H.2    Ishihara, A.3    Aizawa, S.4    Macnab, R.M.5
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    • Salmonella typhimurium strains were derivatives of SJW1103 [S. Yamaguchi, H. Fujita, A. Ishihara, S. Aizawa, R. M. Macnab, J. Bacteriol. 166,187 (1986)] or SL1344 [S. K. Hoiseth and B. A. Stocker, Nature 291, 238 (1981)]. The S. typhimurium flagellar mutants examined were ΔflhC, flgA, flgB, flgC, flgD, flgE, flgF, flgG, flhA, flhB, flhC, fliE, fliF, fliG, fliH, flil, fliJ, fliM, fliN, Δflio-fliR, fliP, ΔfliP-fliR, fliP, and fliQ.
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    • unpublished results
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    • note
    • 4 was added to a final concentration of 10 mM, and samples were centrifuged at 5000g for 20 min. The clarified sample was adjusted to pH 11 with NaOH, incubated for 1 hour at 4°C, and centrifuged at 60,000g for 1 hour. The pellet was resuspended in a solution containing 0.1 M KCl-KOH (pH 11), 0.5 M sucrose, and 0.1% LDAO and centrifuged at 60,000g for 1 hour. The pellet was resuspended in TET buffer [10 mM tris-HCl (pH 8.0), 5 mM EDTA, and 0.1% LDAO] and loaded onto a 30% (w/v) CsCl density gradient. Gradient fractions were centrifuged at 60,1000g for 1 hour, and the pellets were washed with TET buffer.
  • 20
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    • note
    • Polypeptides separated on standard SDS-polyacrytamide gels were electroblotted onto polyvinylidene difluoride membranes, and the bands of interest were applied to a Beckman LF3000 protein sequencer.
  • 21
    • 2642661243 scopus 로고    scopus 로고
    • note
    • The amino acid sequences obtained from the different polypeptide species were as follows: 62 kD, SEKIPVTGSG; 52 kD, METSKEKTI; and 31 kD, CKDKD (19).
  • 23
    • 0030716279 scopus 로고    scopus 로고
    • N. A. Linderoth, M. N. Simon, M. Russel, Science 278, 1635 (1997); M. Koster et al., Mol. Microbiol. 26, 789 (1997).
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    • Koster, M.1
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    • The prgH and prgK genes were cloned from the wild-type strain of S. typhimurium SL1344 by polymerase change reaction, and derivative strains carrying nonpolar mutations in these genes were constructed by allele replacement (8). Salmonella typhimurium strains expressing a functional M45 epitope -tagged PrgH protein were constructed as described elsewhere [C. Collazo and J. E. Galán, Infect. Immun. 64, 3524 (1996)]. The M45 epitope tag consisted of 18 residues from the E4-6/7 protein of adenovirus (MDRSRDRLPPFETETRIL) (79) [S. Obert, R. J. O'Connor, S. Schmid, P. Hearing, Mol. Cell. Biol. 14, 1333 (1994)].
    • (1996) Infect. Immun. , vol.64 , pp. 3524
    • Collazo, C.1    Galán, J.E.2
  • 25
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    • The prgH and prgK genes were cloned from the wild-type strain of S. typhimurium SL1344 by polymerase change reaction, and derivative strains carrying nonpolar mutations in these genes were constructed by allele replacement (8). Salmonella typhimurium strains expressing a functional M45 epitope - tagged PrgH protein were constructed as described elsewhere [C. Collazo and J. E. Galán, Infect. Immun. 64, 3524 (1996)]. The M45 epitope tag consisted of 18 residues from the E4-6/7 protein of adenovirus (MDRSRDRLPPFETETRIL) (79) [S. Obert, R. J. O'Connor, S. Schmid, P. Hearing, Mol. Cell. Biol. 14, 1333 (1994)].
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 1333
    • Obert, S.1    O'Connor, R.J.2    Schmid, S.3    Hearing, P.4
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    • note
    • Single-letter abbreviations for the amino acid residues are as follows: C, Cys; D, Asp; E, Glu; F, Phe; G, Gly; I, IIe; K, Lys; L, Leu; M, Met; P, Pro; R, Arg; S, Ser; T, Thr; and V, Val.
  • 29
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    • note
    • We thank S. Yamaguchi for Salmonella flagellar mutant strains; M. Iwakura for amino acid sequence analysis; S. Makishima, T. Kubo, and N. Kobayashi for assistance in the needle preparation; and J. Bliska, R. Donis, and members of the Galán laboratory for critical reading of this manuscript. Supported by a Grant-in-Aid for Scientific Research from the Ministry of Education, Science, Sports and Culture (S.-I.A.), the American Heart Association, and Public Health Service Grants from the NIH (J.E.G.).


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.