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Volumn 58, Issue 1, 2008, Pages 53-60

Yersinia pestis YopD 150-287 fragment is partially unfolded in the native state

Author keywords

Molten globule; SycD; Translocator; Yersinia pestis; YopD

Indexed keywords

BACTERIAL PROTEIN; CHAPERONE; OUTER MEMBRANE PROTEIN; PEPTIDE FRAGMENT; UNCLASSIFIED DRUG; VIRULENCE FACTOR; YOPB PROTEIN, YERSINIA; YOPD PROTEIN, YERSINIA;

EID: 38349084653     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2007.11.001     Document Type: Article
Times cited : (7)

References (39)
  • 1
    • 0031614870 scopus 로고    scopus 로고
    • The Yersinia Yop virulon a bacterial system to subvert cells of the primary host defense
    • Cornelis G.R. The Yersinia Yop virulon a bacterial system to subvert cells of the primary host defense. Folia Microbiol. (Praha) 43 (1998) 253-261
    • (1998) Folia Microbiol. (Praha) , vol.43 , pp. 253-261
    • Cornelis, G.R.1
  • 2
    • 0036532450 scopus 로고    scopus 로고
    • Port of entry-the type III secretion translocon
    • Buttner D., and Bonas U. Port of entry-the type III secretion translocon. Trends Microbiol. 10 (2002) 186-192
    • (2002) Trends Microbiol. , vol.10 , pp. 186-192
    • Buttner, D.1    Bonas, U.2
  • 3
    • 14644430389 scopus 로고    scopus 로고
    • Insertion of the bacterial type III translocon: not your average needle stick
    • Coombes B.K., and Finlay B.B. Insertion of the bacterial type III translocon: not your average needle stick. Trends Microbiol. 13 (2005) 92-95
    • (2005) Trends Microbiol. , vol.13 , pp. 92-95
    • Coombes, B.K.1    Finlay, B.B.2
  • 4
    • 0031928329 scopus 로고    scopus 로고
    • YopD of Yersinia pseudotuberculosis is translocated into the cytosol of HeLa epithelial cells: evidence of a structural domain necessary for translocation
    • Francis M.S., and Wolf-Watz H. YopD of Yersinia pseudotuberculosis is translocated into the cytosol of HeLa epithelial cells: evidence of a structural domain necessary for translocation. Mol. Microbiol. 29 (1998) 799-813
    • (1998) Mol. Microbiol. , vol.29 , pp. 799-813
    • Francis, M.S.1    Wolf-Watz, H.2
  • 6
    • 3343006984 scopus 로고    scopus 로고
    • The V antigen of Pseudomonas aeruginosa is required for assembly of the functional PopB/PopD translocation pore in host cell membranes
    • Goure J., Pastor A., Faudry E., Chabert J., Dessen A., and Attree I. The V antigen of Pseudomonas aeruginosa is required for assembly of the functional PopB/PopD translocation pore in host cell membranes. Infect. Immun. 72 (2004) 4741-4750
    • (2004) Infect. Immun. , vol.72 , pp. 4741-4750
    • Goure, J.1    Pastor, A.2    Faudry, E.3    Chabert, J.4    Dessen, A.5    Attree, I.6
  • 7
    • 0035836714 scopus 로고    scopus 로고
    • Polymerization of a single protein of the pathogen Yersinia enterocolitica into needles punctures eukaryotic cells
    • Hoiczyk E., and Blobel G. Polymerization of a single protein of the pathogen Yersinia enterocolitica into needles punctures eukaryotic cells. Proc. Natl. Acad. Sci. USA 98 (2001) 4669-4674
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 4669-4674
    • Hoiczyk, E.1    Blobel, G.2
  • 11
    • 0035499438 scopus 로고    scopus 로고
    • Maintenance of an unfolded polypeptide by a cognate chaperone in bacterial type III secretion
    • Stebbins C.E., and Galan J.E. Maintenance of an unfolded polypeptide by a cognate chaperone in bacterial type III secretion. Nature 414 (2001) 77-81
    • (2001) Nature , vol.414 , pp. 77-81
    • Stebbins, C.E.1    Galan, J.E.2
  • 12
    • 0037321471 scopus 로고    scopus 로고
    • Structure of the Yersinia enterocolitica molecular-chaperone protein SycE
    • Trame C.B., and McKay D.B. Structure of the Yersinia enterocolitica molecular-chaperone protein SycE. Acta Crystallogr. D Biol. Crystallogr. 59 (2003) 389-392
    • (2003) Acta Crystallogr. D Biol. Crystallogr. , vol.59 , pp. 389-392
    • Trame, C.B.1    McKay, D.B.2
  • 13
    • 0036283512 scopus 로고    scopus 로고
    • Three-dimensional secretion signals in chaperone-effector complexes of bacterial pathogens
    • Birtalan S.C., Phillips R.M., and Ghosh P. Three-dimensional secretion signals in chaperone-effector complexes of bacterial pathogens. Mol. Cell 9 (2002) 971-980
    • (2002) Mol. Cell , vol.9 , pp. 971-980
    • Birtalan, S.C.1    Phillips, R.M.2    Ghosh, P.3
  • 14
    • 33344459126 scopus 로고    scopus 로고
    • A common structural motif in the binding of virulence factors to bacterial secretion chaperones
    • Lilic M., Vujanac M., and Stebbins C.E. A common structural motif in the binding of virulence factors to bacterial secretion chaperones. Mol. Cell 21 (2006) 653-664
    • (2006) Mol. Cell , vol.21 , pp. 653-664
    • Lilic, M.1    Vujanac, M.2    Stebbins, C.E.3
  • 15
    • 13444303937 scopus 로고    scopus 로고
    • Three-dimensional structure of a macromolecular assembly that regulates type III secretion in Yersinia pestis
    • Schubot F.D., Jackson M.W., Penrose K.J., Cherry S., Tropea J.E., Plano J.V., and Waugh D.S. Three-dimensional structure of a macromolecular assembly that regulates type III secretion in Yersinia pestis. J. Mol. Biol. 346 (2005) 1147-1161
    • (2005) J. Mol. Biol. , vol.346 , pp. 1147-1161
    • Schubot, F.D.1    Jackson, M.W.2    Penrose, K.J.3    Cherry, S.4    Tropea, J.E.5    Plano, J.V.6    Waugh, D.S.7
  • 16
    • 0032947515 scopus 로고    scopus 로고
    • Role of SycD, the chaperone of the Yersinia Yop translocators YopB and YopD
    • Neyt C., and Cornelis G.R. Role of SycD, the chaperone of the Yersinia Yop translocators YopB and YopD. Mol. Microbiol. 31 (1999) 143-156
    • (1999) Mol. Microbiol. , vol.31 , pp. 143-156
    • Neyt, C.1    Cornelis, G.R.2
  • 17
    • 0033810428 scopus 로고    scopus 로고
    • A study of the YopD-lcrH interaction from Yersinia pseudotuberculosis reveals a role for hydrophobic residues within the amphipathic domain of YopD
    • Francis M.S., Aili M., Wiklund M.L., and Wolf-Watz H. A study of the YopD-lcrH interaction from Yersinia pseudotuberculosis reveals a role for hydrophobic residues within the amphipathic domain of YopD. Mol. Microbiol. 38 (2000) 85-102
    • (2000) Mol. Microbiol. , vol.38 , pp. 85-102
    • Francis, M.S.1    Aili, M.2    Wiklund, M.L.3    Wolf-Watz, H.4
  • 18
    • 0036371182 scopus 로고    scopus 로고
    • Conformational analysis by CD and NMR spectroscopy of a peptide encompassing the amphipathic domain of YopD from Yersinia
    • Tengel T., Sethson I., and Francis M.S. Conformational analysis by CD and NMR spectroscopy of a peptide encompassing the amphipathic domain of YopD from Yersinia. Eur. J. Biochem. 269 (2002) 3659-3668
    • (2002) Eur. J. Biochem. , vol.269 , pp. 3659-3668
    • Tengel, T.1    Sethson, I.2    Francis, M.S.3
  • 19
    • 33645093201 scopus 로고    scopus 로고
    • Tetratricopeptide repeats in the type III secretion chaperone, LcrH: their role in substrate binding and secretion
    • Edqvist P.J., Broms J.E., Betts H.J., Forsberg A., Pallen M.J., and Francis M.S. Tetratricopeptide repeats in the type III secretion chaperone, LcrH: their role in substrate binding and secretion. Mol. Microbiol. 59 (2006) 31-44
    • (2006) Mol. Microbiol. , vol.59 , pp. 31-44
    • Edqvist, P.J.1    Broms, J.E.2    Betts, H.J.3    Forsberg, A.4    Pallen, M.J.5    Francis, M.S.6
  • 20
    • 0037418190 scopus 로고    scopus 로고
    • Disorder in the nuclear pore complex: the FG repeat regions of nucleoporins are natively unfolded
    • Denning D.P., Patel S.S., Uversky V., Fink A.L., and Rexach M. Disorder in the nuclear pore complex: the FG repeat regions of nucleoporins are natively unfolded. Proc. Natl. Acad. Sci. USA 100 (2003) 2450-2455
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 2450-2455
    • Denning, D.P.1    Patel, S.S.2    Uversky, V.3    Fink, A.L.4    Rexach, M.5
  • 22
    • 33645778262 scopus 로고    scopus 로고
    • Conservation of intrinsic disorder in protein domains and families: I. A database of conserved predicted disordered regions
    • Chen J.W., Romero P., Uversky V.N., and Dunker A.K. Conservation of intrinsic disorder in protein domains and families: I. A database of conserved predicted disordered regions. J. Proteome Res. 5 (2006) 879-887
    • (2006) J. Proteome Res. , vol.5 , pp. 879-887
    • Chen, J.W.1    Romero, P.2    Uversky, V.N.3    Dunker, A.K.4
  • 23
    • 0038237346 scopus 로고    scopus 로고
    • Zinc binding and dimerization of Streptococcus pyogenes pyrogenic exotoxin C are not essential for T-cell stimulation
    • Swietnicki W., Barnie A.M., Dyas B.K., and Ulrich R.G. Zinc binding and dimerization of Streptococcus pyogenes pyrogenic exotoxin C are not essential for T-cell stimulation. J. Biol. Chem. 278 (2003) 9885-9895
    • (2003) J. Biol. Chem. , vol.278 , pp. 9885-9895
    • Swietnicki, W.1    Barnie, A.M.2    Dyas, B.K.3    Ulrich, R.G.4
  • 24
    • 0001040367 scopus 로고
    • An algorithm for protein secondary structure prediction based on class prediction
    • Deleage G., and Roux B. An algorithm for protein secondary structure prediction based on class prediction. Protein Eng. 1 (1987) 289-294
    • (1987) Protein Eng. , vol.1 , pp. 289-294
    • Deleage, G.1    Roux, B.2
  • 25
    • 0029804192 scopus 로고    scopus 로고
    • Identification and application of the concepts important for accurate and reliable protein secondary structure prediction
    • King R.D., and Sternberg M.J. Identification and application of the concepts important for accurate and reliable protein secondary structure prediction. Protein Sci. 5 (1996) 2298-2310
    • (1996) Protein Sci. , vol.5 , pp. 2298-2310
    • King, R.D.1    Sternberg, M.J.2
  • 26
    • 0029884694 scopus 로고    scopus 로고
    • GOR method for predicting protein secondary structure from amino acid sequence
    • Garnier J., Gibrat J.F., and Robson B. GOR method for predicting protein secondary structure from amino acid sequence. Methods Enzymol. 266 (1996) 540-553
    • (1996) Methods Enzymol. , vol.266 , pp. 540-553
    • Garnier, J.1    Gibrat, J.F.2    Robson, B.3
  • 27
    • 38349178455 scopus 로고    scopus 로고
    • Guermer, Y. Ph.D. Thesis.
  • 28
    • 0027291015 scopus 로고
    • Prediction of protein secondary structure at better than 70% accuracy
    • Rost B., and Sander C. Prediction of protein secondary structure at better than 70% accuracy. J. Mol. Biol. 232 (1993) 584-599
    • (1993) J. Mol. Biol. , vol.232 , pp. 584-599
    • Rost, B.1    Sander, C.2
  • 29
    • 0029996162 scopus 로고    scopus 로고
    • Incorporation of non-local interactions in protein secondary structure prediction from the amino acid sequence
    • Frishman D., and Argos P. Incorporation of non-local interactions in protein secondary structure prediction from the amino acid sequence. Protein Eng. 9 (1996) 133-142
    • (1996) Protein Eng. , vol.9 , pp. 133-142
    • Frishman, D.1    Argos, P.2
  • 30
    • 0023050277 scopus 로고
    • An algorithm for secondary structure determination in proteins based on sequence similarity
    • Levin J.M., Robson B., and Garnier J. An algorithm for secondary structure determination in proteins based on sequence similarity. FEBS Lett. 205 (1986) 303-308
    • (1986) FEBS Lett. , vol.205 , pp. 303-308
    • Levin, J.M.1    Robson, B.2    Garnier, J.3
  • 31
    • 0028009149 scopus 로고
    • SOPM: a self-optimized method for protein secondary structure prediction
    • Geourjon C., and Deleage G. SOPM: a self-optimized method for protein secondary structure prediction. Protein Eng. 7 (1994) 157-164
    • (1994) Protein Eng. , vol.7 , pp. 157-164
    • Geourjon, C.1    Deleage, G.2
  • 32
    • 0000207681 scopus 로고
    • TMbase-a database of membrane spanning protein segments
    • Hoffmann K., and Stoffel W. TMbase-a database of membrane spanning protein segments. Biol. Chem. Hoppe-Seyler 374 (1993) 166-172
    • (1993) Biol. Chem. Hoppe-Seyler , vol.374 , pp. 166-172
    • Hoffmann, K.1    Stoffel, W.2
  • 33
    • 0030022713 scopus 로고    scopus 로고
    • Thermodynamics of denaturation of staphylococcal nuclease mutants: an intermediate state in protein folding
    • Carra J.H., and Privalov P.L. Thermodynamics of denaturation of staphylococcal nuclease mutants: an intermediate state in protein folding. FASEB J. 10 (1996) 67-74
    • (1996) FASEB J. , vol.10 , pp. 67-74
    • Carra, J.H.1    Privalov, P.L.2
  • 34
    • 0025982146 scopus 로고
    • Molten globule intermediates and protein folding
    • Christensen H., and Pain R.H. Molten globule intermediates and protein folding. Eur. Biophys. J. 19 (1991) 221-229
    • (1991) Eur. Biophys. J. , vol.19 , pp. 221-229
    • Christensen, H.1    Pain, R.H.2
  • 35
    • 0034581327 scopus 로고    scopus 로고
    • Role of the molten globule state in protein folding
    • Arai M., and Kuwajima K. Role of the molten globule state in protein folding. Adv. Protein Chem. 53 (2000) 209-282
    • (2000) Adv. Protein Chem. , vol.53 , pp. 209-282
    • Arai, M.1    Kuwajima, K.2
  • 36
    • 0028286474 scopus 로고
    • Protein conformational changes induced by 1,1′-bis(4-anilino-5-naphthalenesulfonic acid): preferential binding to the molten globule of DnaK
    • Shi L., Palleros D.R., and Fink A.L. Protein conformational changes induced by 1,1′-bis(4-anilino-5-naphthalenesulfonic acid): preferential binding to the molten globule of DnaK. Biochemistry 33 (1994) 7536-7546
    • (1994) Biochemistry , vol.33 , pp. 7536-7546
    • Shi, L.1    Palleros, D.R.2    Fink, A.L.3
  • 37
    • 33745615443 scopus 로고    scopus 로고
    • Synergistic pore formation by type III toxin translocators of Pseudomonas aeruginosa
    • Faudry E., Vernier G., Neumann E., Forge V., and Attree I. Synergistic pore formation by type III toxin translocators of Pseudomonas aeruginosa. Biochemistry 45 (2006) 8117-8123
    • (2006) Biochemistry , vol.45 , pp. 8117-8123
    • Faudry, E.1    Vernier, G.2    Neumann, E.3    Forge, V.4    Attree, I.5
  • 38
    • 0141642035 scopus 로고    scopus 로고
    • Oligomerization of type III secretion proteins PopB and PopD precedes pore formation in Pseudomonas
    • Schoehn G., Di Guilmi A.M., Lemaire D., Attree I., Weissenhorn W., and Dessen A. Oligomerization of type III secretion proteins PopB and PopD precedes pore formation in Pseudomonas. EMBO J. 22 (2003) 4957-4967
    • (2003) EMBO J. , vol.22 , pp. 4957-4967
    • Schoehn, G.1    Di Guilmi, A.M.2    Lemaire, D.3    Attree, I.4    Weissenhorn, W.5    Dessen, A.6
  • 39
    • 0026608073 scopus 로고
    • Environment affects amino acid preference for secondary structure
    • Zhong L., and Johnson Jr. W.C. Environment affects amino acid preference for secondary structure. Proc. Natl. Acad. Sci. USA 89 (1992) 4462-4465
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 4462-4465
    • Zhong, L.1    Johnson Jr., W.C.2


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