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Volumn 192, Issue 15, 2010, Pages 3847-3849

Secretion signal and protein targeting in Bacteria: A biological puzzle

Author keywords

[No Author keywords available]

Indexed keywords

AMINO TERMINAL SEQUENCE; BARTONELLA; CELL MEMBRANE; ENDOPLASMIC RETICULUM; ESCHERICHIA COLI; HELICOBACTER PYLORI; KLEBSIELLA OXYTOCA; NONHUMAN; NOTE; PRIORITY JOURNAL; PROTEIN SECRETION; PROTEIN STRUCTURE; PROTEIN TARGETING; PSEUDOMONAS AERUGINOSA; SERRATIA MARCESCENS; GRAM NEGATIVE BACTERIUM; METABOLISM; PHYSIOLOGY; PROTEIN MOTIF; PROTEIN TRANSPORT; SECRETORY PATHWAY; SIGNAL TRANSDUCTION;

EID: 77955296751     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.00565-10     Document Type: Note
Times cited : (29)

References (27)
  • 1
    • 1842413699 scopus 로고    scopus 로고
    • A mRNA signal for the type III secretion of Yop proteins by Yersinia enterocolitica
    • Anderson, D. M., and O. Schneewind. 1997. A mRNA signal for the type III secretion of Yop proteins by Yersinia enterocolitica. Science 278:1140-1143.
    • (1997) Science , vol.278 , pp. 1140-1143
    • Anderson, D.M.1    Schneewind, O.2
  • 3
    • 0344405700 scopus 로고    scopus 로고
    • A specific interaction between the NBD of the ABC-transporter HlyB and a C-terminal fragment of its transport substrate haemolysin a
    • Benabdelhak, H., S. Kiontke, C. Horn, R. Ernst, M. A. Blight, I. B. Holland, and L. Schmitt. 2003. A specific interaction between the NBD of the ABC-transporter HlyB and a C-terminal fragment of its transport substrate haemolysin A. J. Mol. Biol. 327:1169-1179.
    • (2003) J. Mol. Biol. , vol.327 , pp. 1169-1179
    • Benabdelhak, H.1    Kiontke, S.2    Horn, C.3    Ernst, R.4    Blight, M.A.5    Holland, I.B.6    Schmitt, L.7
  • 5
    • 0242478028 scopus 로고    scopus 로고
    • Protein secretion by Gram-negative bacterial ABC exporters - A review
    • DOI 10.1016/S0378-1119(96)00829-3, PII S0378111996008293
    • Binet, R., S. Létoffé, J. M. Ghigo, P. Delepelaire, and C. Wandersman. 1997. Protein secretion by Gram-negative bacterial ABC exporters - a review. Gene 192:7-11. (Pubitemid 27267473)
    • (1997) Gene , vol.192 , Issue.1 , pp. 7-11
    • Binet, R.1    Letoffe, S.2    Ghigo, J.M.3    Delepelaire, P.4    Wandersman, C.5
  • 6
    • 33947422975 scopus 로고    scopus 로고
    • Probing the in vivo dynamics of type I protein secretion complex association through sensitivity to detergents
    • DOI 10.1128/JB.01480-06
    • Cescau, S., L. Debarbieux, and C. Wandersman. 2007. Probing the in vivo dynamics of type I protein secretion complex association through sensitivity to detergents. J. Bacteriol. 189:1496-1504. (Pubitemid 46446110)
    • (2007) Journal of Bacteriology , vol.189 , Issue.5 , pp. 1496-1504
    • Cescau, S.1    Debarbieux, L.2    Wandersman, C.3
  • 7
    • 0035958760 scopus 로고    scopus 로고
    • Type II protein secretion in gram-negative pathogenic bacteria: The study of the structure/secretion relationships of the cellulase Cel5 (formerly EGZ) from Erwinia chrysanthemi
    • DOI 10.1006/jmbi.2001.4787
    • Chapon, V., M. Czjzek, M. El Hassouni, B. Py, M. Juy, and F. Barras. 2001. Type II protein secretion in gram-negative pathogenic bacteria: the study of the structure/secretion relationships of the cellulase Cel5 (formerly EGZ) from Erwinia chrysanthemi. J. Mol. Biol. 310:1055-1066. (Pubitemid 32738377)
    • (2001) Journal of Molecular Biology , vol.310 , Issue.5 , pp. 1055-1066
    • Chapon, V.1    Czjzek, M.2    El Hassouni, M.3    Py, B.4    Juy, M.5    Barras, F.6
  • 9
    • 34548128883 scopus 로고    scopus 로고
    • Structure of the membrane protein FhaC: A member of the Omp85-TpsB transporter superfamily
    • DOI 10.1126/science.1143860
    • Clantin, B., A. S. Delattre, P. Rucktooa, N. Saint, A. C. Méli, C. Locht, F. Jacob-Dubuisson, and V. Villeret. 2007. Structure of the membrane protein FhaC: a member of the Omp85-TpsB transporter superfamily. Science 317:957-961. (Pubitemid 47301325)
    • (2007) Science , vol.317 , Issue.5840 , pp. 957-961
    • Clantin, B.1    Delattre, A.-S.2    Rucktooa, P.3    Saint, N.4    Meli, A.C.5    Locht, C.6    Jacob-Dubuisson, F.7    Villeret, V.8
  • 10
    • 33750110911 scopus 로고    scopus 로고
    • The type III secretion injectisome
    • Cornelis, G. R. 2006. The type III secretion injectisome. Nat. Rev. Microbiol. 4:811-825.
    • (2006) Nat. Rev. Microbiol. , vol.4 , pp. 811-825
    • Cornelis, G.R.1
  • 11
    • 0029815310 scopus 로고    scopus 로고
    • Protein secretion by heterologous bacterial ABC-transporters: The C-terminus secretion signal of the secreted protein confers high recognition specificity
    • Duong, F., A. Lazdunski, and M. Murgier. 1996. Protein secretion by heterologous bacterial ABC-transporters: the C-terminus secretion signal of the secreted protein confers high recognition specificity. Mol. Microbiol. 21:459-470.
    • (1996) Mol. Microbiol. , vol.21 , pp. 459-470
    • Duong, F.1    Lazdunski, A.2    Murgier, M.3
  • 12
    • 8844269404 scopus 로고    scopus 로고
    • The underlying mechanisms of type II protein secretion
    • Filloux, A. 2004. The underlying mechanisms of type II protein secretion. Biochim. Biophys. Acta 1694:163-179.
    • (2004) Biochim. Biophys. Acta , vol.1694 , pp. 163-179
    • Filloux, A.1
  • 13
    • 48449086943 scopus 로고    scopus 로고
    • The bacterial type VI secretion machine: Yet another player for protein transport across membranes
    • Filloux, A., A. Hachani, and S. Bleves. 2008. The bacterial type VI secretion machine: yet another player for protein transport across membranes. Microbiology 154:1570-1583.
    • (2008) Microbiology , vol.154 , pp. 1570-1583
    • Filloux, A.1    Hachani, A.2    Bleves, S.3
  • 14
    • 26444506255 scopus 로고    scopus 로고
    • Towards the identification of type II secretion signals in a nonacylated variant of pullulanase from Klebsiella oxytoca
    • Francetić, O., and A. P. Pugsley. 2005. Towards the identification of type II secretion signals in a nonacylated variant of pullulanase from Klebsiella oxytoca. J. Bacteriol. 187:7045-7055.
    • (2005) J. Bacteriol. , vol.187 , pp. 7045-7055
    • Francetić, O.1    Pugsley, A.P.2
  • 15
    • 33645090948 scopus 로고    scopus 로고
    • A C-terminal translocation signal is necessary, but not sufficient for type IV secretion of the Helicobacter pylori CagA protein
    • Hohlfeld, S., I. Pattis, J. Püls, G. V. Plano, R. Haas, and W. Fischer. 2006. A C-terminal translocation signal is necessary, but not sufficient for type IV secretion of the Helicobacter pylori CagA protein. Mol. Microbiol. 59:1624-1637.
    • (2006) Mol. Microbiol. , vol.59 , pp. 1624-1637
    • Hohlfeld, S.1    Pattis, I.2    Püls, J.3    Plano, G.V.4    Haas, R.5    Fischer, W.6
  • 16
    • 8844235655 scopus 로고    scopus 로고
    • Protein secretion through autotransporter and two-partner pathways
    • Jacob-Dubuisson. F, R. Fernadez, and L. Coutte. 2004. Protein secretion through autotransporter and two-partner pathways. Biochim. Biophys. Acta 1694:235-257.
    • (2004) Biochim. Biophys. Acta , vol.1694 , pp. 235-257
    • Jacob-Dubuisson, F.1    Fernadez, R.2    Coutte, L.3
  • 17
    • 0024386073 scopus 로고
    • Isolation and analysis of the C-terminal signal directing export of Escherichia coli hemolysin protein across both bacterial membranes
    • Koronakis, V., E. Koronakis, and C. Hughes. 1989. Isolation and analysis of the C-terminal signal directing export of Escherichia coli hemolysin protein across both bacterial membranes. EMBO J. 8:595-605.
    • (1989) EMBO J , vol.8 , pp. 595-605
    • Koronakis, V.1    Koronakis, E.2    Hughes, C.3
  • 18
    • 77955296461 scopus 로고    scopus 로고
    • Multiple signals direct the assembly and function of a type 1 secretion system
    • Masi, M., and C. Wandersman. 2010. Multiple signals direct the assembly and function of a type 1 secretion system. J. Bacteriol. 192:3861-3869.
    • (2010) J. Bacteriol. , vol.192 , pp. 3861-3869
    • Masi, M.1    Wandersman, C.2
  • 19
    • 34948822413 scopus 로고    scopus 로고
    • The Helicobacter pylori CagF protein is a type IV secretion chaperone-like molecule that binds close to the C-terminal secretion signal of the CagA effector protein
    • Pattis, I., E. Weiss, R. Laugks, R. Haas, and W. Fischer. 2007. The Helicobacter pylori CagF protein is a type IV secretion chaperone-like molecule that binds close to the C-terminal secretion signal of the CagA effector protein. Microbiology 153:2896-2909.
    • (2007) Microbiology , vol.153 , pp. 2896-2909
    • Pattis, I.1    Weiss, E.2    Laugks, R.3    Haas, R.4    Fischer, W.5
  • 20
    • 8844280791 scopus 로고    scopus 로고
    • Tat-dependent protein targeting in prokaryotes and chloroplasts
    • Robinson, C., and A. Bolhuis. 2004. Tat-dependent protein targeting in prokaryotes and chloroplasts. Biochim. Biophys. Acta 1694:135-147.
    • (2004) Biochim. Biophys. Acta , vol.1694 , pp. 135-147
    • Robinson, C.1    Bolhuis, A.2
  • 21
    • 54349103449 scopus 로고    scopus 로고
    • The 'P-usher', a novel protein transporter involved in fimbrial assembly and TpsA secretion
    • Ruer, S., G. Ball, A. Filloux, and S. de Bentzmann. 2008. The 'P-usher', a novel protein transporter involved in fimbrial assembly and TpsA secretion. EMBO J. 27:2669-2680.
    • (2008) EMBO J , vol.27 , pp. 2669-2680
    • Ruer, S.1    Ball, G.2    Filloux, A.3    De Bentzmann, S.4
  • 23
    • 0029608720 scopus 로고
    • Identification of the YopE and YopH domains required for secretion and internalization into the cytosol of macrophages, using the cyaA gene fusion approach
    • Sory, M. P., A. Boland, I. Lambermont, and G. R. Cornelis. 1995. Identification of the YopE and YopH domains required for secretion and internalization into the cytosol of macrophages, using the cyaA gene fusion approach. Proc. Natl. Acad. Sci. U. S. A. 92:11998-12002.
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 11998-12002
    • Sory, M.P.1    Boland, A.2    Lambermont, I.3    Cornelis, G.R.4
  • 24
    • 0025297583 scopus 로고
    • The signal peptide
    • von Heijne, G. 1990. The signal peptide. J. Membr. Biol. 115:195-201.
    • (1990) J. Membr. Biol. , vol.115 , pp. 195-201
    • Von Heijne, G.1
  • 25
    • 0035803406 scopus 로고    scopus 로고
    • Involvement of the twin-arginine translocation system in protein secretion via the type II pathway
    • DOI 10.1093/emboj/20.23.6735
    • Voulhoux, R., G. Ball, B. Ize, M. L. Vasil, A. Lazdunski, L. F. Wu, and A. Filloux. 2001. Involvement of the twin-arginine translocation system in protein secretion via the type II pathway. EMBO J. 20:6735-6741. (Pubitemid 33134203)
    • (2001) EMBO Journal , vol.20 , Issue.23 , pp. 6735-6741
    • Voulhoux, R.1    Ball, G.2    Ize, B.3    Vasil, M.L.4    Lazdunski, A.5    Wu, L.-F.6    Filloux, A.7
  • 26
    • 0033917666 scopus 로고    scopus 로고
    • Influence of deletions within domain II of exotoxin a on its extracellular secretion from Pseudomonas aeruginosa
    • Voulhoux, R., M. P. Taupiac, M. Czjzek, B. Beaumelle, and A. Filloux. 2000. Influence of deletions within domain II of exotoxin A on its extracellular secretion from Pseudomonas aeruginosa. J. Bacteriol. 182:4051-4058.
    • (2000) J. Bacteriol. , vol.182 , pp. 4051-4058
    • Voulhoux, R.1    Taupiac, M.P.2    Czjzek, M.3    Beaumelle, B.4    Filloux, A.5
  • 27
    • 0028936779 scopus 로고
    • Secretion and circular dichroism analysis of the C-terminal signal peptides of HlyA and LktA
    • Zhang, F., Y. Yin, C. H. Arrowsmith, and V. Ling. 1995. Secretion and circular dichroism analysis of the C-terminal signal peptides of HlyA and LktA. Biochemistry 34:4193-4201.
    • (1995) Biochemistry , vol.34 , pp. 4193-4201
    • Zhang, F.1    Yin, Y.2    Arrowsmith, C.H.3    Ling, V.4


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