메뉴 건너뛰기




Volumn 70, Issue 5, 2008, Pages 1210-1222

Yersinia enterocolitica type III secretion of YopR requires a structure in its mRNA

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; MESSENGER RNA; PROTEIN YOPS; UNCLASSIFIED DRUG;

EID: 55349145620     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2008.06474.x     Document Type: Article
Times cited : (17)

References (64)
  • 1
    • 23844543359 scopus 로고    scopus 로고
    • 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
    • Agrain, C., Sorg, I., Paroz, C. Cornelis, G.R. (2005a) 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. Mol Microbiol 57 : 1415 1427.
    • (2005) Mol Microbiol , vol.57 , pp. 1415-1427
    • Agrain, C.1    Sorg, I.2    Paroz, C.3    Cornelis, G.R.4
  • 2
    • 16244407371 scopus 로고    scopus 로고
    • Characterization of a type III secretion substrate specificity switch (T3S4) domain in YscP from Yersinia enterocolitica
    • Agrain, C., Callebaut, I., Journet, L., Sorg, I., Paroz, C., Mota, L.J. Cornelis, G.R. (2005b) Characterization of a type III secretion substrate specificity switch (T3S4) domain in YscP from Yersinia enterocolitica. Mol Microbiol 56 : 54 67.
    • (2005) Mol Microbiol , vol.56 , pp. 54-67
    • Agrain, C.1    Callebaut, I.2    Journet, L.3    Sorg, I.4    Paroz, C.5    Mota, L.J.6    Cornelis, G.R.7
  • 3
    • 33744991096 scopus 로고    scopus 로고
    • Transcriptional and translational control of the Salmonella fliC gene
    • Aldridge, P., Gnerer, J., Karlinsey, J.E. Hughes, K.T. (2006) Transcriptional and translational control of the Salmonella fliC gene. J Bacteriol 188 : 4487 4496.
    • (2006) J Bacteriol , vol.188 , pp. 4487-4496
    • Aldridge, P.1    Gnerer, J.2    Karlinsey, J.E.3    Hughes, K.T.4
  • 4
    • 0028883418 scopus 로고
    • Mutational analysis of the Yersinia enterocolitica virC operon: Characterization of yscE, F, G, I, J, K required for Yop secretion and yscH encoding YopR
    • Allaoui, A., Schulte, R. Cornelis, G.R. (1995) Mutational analysis of the Yersinia enterocolitica virC operon: characterization of yscE, F, G, I, J, K required for Yop secretion and yscH encoding YopR. Mol Microbiol 18 : 343 355.
    • (1995) Mol Microbiol , vol.18 , pp. 343-355
    • Allaoui, A.1    Schulte, R.2    Cornelis, G.R.3
  • 5
    • 1842413699 scopus 로고    scopus 로고
    • A mRNA signal for the type III secretion of Yop proteins by Yersinia enterocolitica
    • Anderson, D.M. Schneewind, O. (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
  • 6
    • 0033003131 scopus 로고    scopus 로고
    • Yersinia enterocolitica type III secretion: An mRNA signal that couples translation and secretion of YopQ
    • Anderson, D.M. Schneewind, O. (1999) Yersinia enterocolitica type III secretion: an mRNA signal that couples translation and secretion of YopQ. Mol Microbiol 31 : 1139 1148.
    • (1999) Mol Microbiol , vol.31 , pp. 1139-1148
    • Anderson, D.M.1    Schneewind, O.2
  • 7
    • 0018365094 scopus 로고
    • Use of gene fusion to study secretion of maltose-binding protein into Escherichia coli periplasm
    • Jr.
    • Bassford, P.J. Jr., Silhavy, T.J. Beckwith, J. (1979) Use of gene fusion to study secretion of maltose-binding protein into Escherichia coli periplasm. J Bacteriol 139 : 19 31.
    • (1979) J Bacteriol , vol.139 , pp. 19-31
    • Bassford, P.J.1    Silhavy, T.J.2    Beckwith, J.3
  • 8
    • 0025374532 scopus 로고
    • PrlA (SecY) and PrlG (SecE) interact directly and function sequentially during protein translocation in E. coli
    • Bieker, K.L. Silhavy, T.J. (1990) PrlA (SecY) and PrlG (SecE) interact directly and function sequentially during protein translocation in E. coli. Cell 61 : 833 842.
    • (1990) Cell , vol.61 , pp. 833-842
    • Bieker, K.L.1    Silhavy, T.J.2
  • 9
    • 0036283512 scopus 로고    scopus 로고
    • Three-dimensional secretion signals in chaperone-effector complexes of bacterial pathogens
    • Birtalan, S.C., Phillips, R.M. Ghosh, P. (2002) Three-dimensional secretion signals in chaperone-effector complexes of bacterial pathogens. Mol Cell 9 : 971 980.
    • (2002) Mol Cell , vol.9 , pp. 971-980
    • Birtalan, S.C.1    Phillips, R.M.2    Ghosh, P.3
  • 10
    • 0037453098 scopus 로고    scopus 로고
    • Type III secretion systems and bacterial flagella: Insights into their function from structural similarities
    • Blocker, A., Komoriya, K. Aizawa, S. (2003) Type III secretion systems and bacterial flagella: insights into their function from structural similarities. Proc Natl Acad Sci USA 100 : 3027 3030.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 3027-3030
    • Blocker, A.1    Komoriya, K.2    Aizawa, S.3
  • 11
    • 0029814613 scopus 로고    scopus 로고
    • Status of YopM and YopN in the Yersinia yop virulon: YopM of Y. enterocolitica is internalized inside the cytosol of PU5-1.8 macrophages by the YopB, D, N delivery apparatus
    • Boland, A., Sory, M.-P., Iriarte, M., Kerbourch, C., Wattiau, P. Cornelis, G.R. (1996) Status of YopM and YopN in the Yersinia yop virulon: YopM of Y. enterocolitica is internalized inside the cytosol of PU5-1.8 macrophages by the YopB, D, N delivery apparatus. EMBO J 15 : 5191 5201.
    • (1996) EMBO J , vol.15 , pp. 5191-5201
    • Boland, A.1    Sory, M.-P.2    Iriarte, M.3    Kerbourch, C.4    Wattiau, P.5    Cornelis, G.R.6
  • 12
    • 36749036576 scopus 로고    scopus 로고
    • Diminished LcrV secretion attenuates Yersinia pseudotuberculosis virulence
    • Bröms, J.E., Francis, M.S. Forsberg, A. (2007) Diminished LcrV secretion attenuates Yersinia pseudotuberculosis virulence. J Bacteriol 189 : 8417 8429.
    • (2007) J Bacteriol , vol.189 , pp. 8417-8429
    • Bröms, J.E.1    Francis, M.S.2    Forsberg, A.3
  • 13
    • 0033618257 scopus 로고    scopus 로고
    • Yersinia enterocolitica type III secretion: On the role of SycE in targeting YopE into HeLa cells
    • Cheng, L.W. Schneewind, O. (1999) Yersinia enterocolitica type III secretion: on the role of SycE in targeting YopE into HeLa cells. J Biol Chem 274 : 22102 22108.
    • (1999) J Biol Chem , vol.274 , pp. 22102-22108
    • Cheng, L.W.1    Schneewind, O.2
  • 14
    • 0030967331 scopus 로고    scopus 로고
    • Two independent type III secretion mechanisms for YopE in Yersinia enterocolitica
    • Cheng, L.W., Anderson, D.M. Schneewind, O. (1997) Two independent type III secretion mechanisms for YopE in Yersinia enterocolitica. Mol Microbiol 24 : 757 765.
    • (1997) Mol Microbiol , vol.24 , pp. 757-765
    • Cheng, L.W.1    Anderson, D.M.2    Schneewind, O.3
  • 15
    • 0345257863 scopus 로고    scopus 로고
    • How Yop proteins find their way out of Yersinia
    • Cornelis, G.R. (2003) How Yop proteins find their way out of Yersinia. Mol Microbiol 50 : 1091 1094.
    • (2003) Mol Microbiol , vol.50 , pp. 1091-1094
    • Cornelis, G.R.1
  • 16
    • 33750110911 scopus 로고    scopus 로고
    • The type III injectisome
    • Cornelis, G.R. (2006) The type III injectisome. Nat Rev Microbiol 4 : 811 825.
    • (2006) Nat Rev Microbiol , vol.4 , pp. 811-825
    • Cornelis, G.R.1
  • 17
    • 0016637595 scopus 로고
    • Restriction of DNA in Yersinia enterocolitica detected by the recipient ability for a derepressed R factor from Escherichia coli
    • Cornelis, G.R. Colson, C. (1975) Restriction of DNA in Yersinia enterocolitica detected by the recipient ability for a derepressed R factor from Escherichia coli. J Gen Microbiol 87 : 285 291.
    • (1975) J Gen Microbiol , vol.87 , pp. 285-291
    • Cornelis, G.R.1    Colson, C.2
  • 19
    • 33845249292 scopus 로고    scopus 로고
    • Protein delivery into eukaryotic cells by type III secretion machines
    • Galán, J.E. Wolf-Watz, H. (2006) Protein delivery into eukaryotic cells by type III secretion machines. Nature 444 : 567 573.
    • (2006) Nature , vol.444 , pp. 567-573
    • Galán, J.E.1    Wolf-Watz, H.2
  • 20
    • 0021710132 scopus 로고
    • Genetic analysis of the low calcium response in Yersinia pestis Mud1 (Ap lac) insertion mutants
    • Goguen, J.D., Yother, J. Straley, S.C. (1984) Genetic analysis of the low calcium response in Yersinia pestis Mud1 (Ap lac) insertion mutants. J Bacteriol 160 : 842 848.
    • (1984) J Bacteriol , vol.160 , pp. 842-848
    • Goguen, J.D.1    Yother, J.2    Straley, S.C.3
  • 21
    • 0142030034 scopus 로고    scopus 로고
    • Pseudaminic acid, the major modification on Campylobacter flagellin, is synthesized via the Cj1293 gene
    • Goon, S., Kelly, J.F., Logan, S.M., Ewing, C.P. Guerry, P. (2003) Pseudaminic acid, the major modification on Campylobacter flagellin, is synthesized via the Cj1293 gene. Mol Microbiol 50 : 659 671.
    • (2003) Mol Microbiol , vol.50 , pp. 659-671
    • Goon, S.1    Kelly, J.F.2    Logan, S.M.3    Ewing, C.P.4    Guerry, P.5
  • 23
    • 0029908022 scopus 로고    scopus 로고
    • The YopB protein of Yersinia pseudotuberculosis is essential for the translocation of Yop effector proteins across the target cell plasma membrane and displays a contact-dependent membrane disrupting activity
    • Håkansson, S., Schesser, K., Persson, C., Galyov, E.E., Rosqvist, R., Homble, F. Wolf-Watz, H. (1996) The YopB protein of Yersinia pseudotuberculosis is essential for the translocation of Yop effector proteins across the target cell plasma membrane and displays a contact-dependent membrane disrupting activity. EMBO J 15 : 5812 5823.
    • (1996) EMBO J , vol.15 , pp. 5812-5823
    • Håkansson, S.1    Schesser, K.2    Persson, C.3    Galyov, E.E.4    Rosqvist, R.5    Homble, F.6    Wolf-Watz, H.7
  • 24
    • 0031864184 scopus 로고    scopus 로고
    • Type III protein secretion in bacterial pathogens of animals and plants
    • Hueck, C.J. (1998) Type III protein secretion in bacterial pathogens of animals and plants. Microbiol Mol Biol Rev 62 : 379 433.
    • (1998) Microbiol Mol Biol Rev , vol.62 , pp. 379-433
    • Hueck, C.J.1
  • 25
    • 0345600239 scopus 로고    scopus 로고
    • The needle length of bacterial injectisomes is determined by a molecular ruler
    • Journet, L., Agrain, C., Broz, P. Cornelis, G.R. (2003) The needle length of bacterial injectisomes is determined by a molecular ruler. Science 302 : 1757 1760.
    • (2003) Science , vol.302 , pp. 1757-1760
    • Journet, L.1    Agrain, C.2    Broz, P.3    Cornelis, G.R.4
  • 26
    • 0020689671 scopus 로고
    • Sequence of the lacZ gene of Escherichia coli
    • Kalnins, A., Otto, K., Ruether, U. Mueller-Hill, B. (1983) Sequence of the lacZ gene of Escherichia coli. EMBO J 2 : 593 597.
    • (1983) EMBO J , vol.2 , pp. 593-597
    • Kalnins, A.1    Otto, K.2    Ruether, U.3    Mueller-Hill, B.4
  • 27
    • 0004236851 scopus 로고
    • Role of calcium ions in the stimulation of growth of virulent strains of Pasteurella pestis
    • Kupferberg, L.L. Higuchi, K. (1958) Role of calcium ions in the stimulation of growth of virulent strains of Pasteurella pestis. J Bacteriol 76 : 120 121.
    • (1958) J Bacteriol , vol.76 , pp. 120-121
    • Kupferberg, L.L.1    Higuchi, K.2
  • 28
    • 0033028599 scopus 로고    scopus 로고
    • Type III machines of pathogenic yersiniae secrete virulence factors into the extracellular milieu
    • Lee, V.T. Schneewind, O. (1999) Type III machines of pathogenic yersiniae secrete virulence factors into the extracellular milieu. Mol Microbiol 31 : 1619 1629.
    • (1999) Mol Microbiol , vol.31 , pp. 1619-1629
    • Lee, V.T.1    Schneewind, O.2
  • 29
    • 0035878128 scopus 로고    scopus 로고
    • Protein secretion and the pathogenesis of bacterial infections
    • Lee, V.T. Schneewind, O. (2001) Protein secretion and the pathogenesis of bacterial infections. Genes Dev 15 : 1725 1752.
    • (2001) Genes Dev , vol.15 , pp. 1725-1752
    • Lee, V.T.1    Schneewind, O.2
  • 30
    • 0036283447 scopus 로고    scopus 로고
    • Yop fusions to tightly folded protein domains and their effects on Yersinia enterocolitica type III secretion
    • Lee, V.T. Schneewind, O. (2002) Yop fusions to tightly folded protein domains and their effects on Yersinia enterocolitica type III secretion. J Bacteriol 184 : 3740 3745.
    • (2002) J Bacteriol , vol.184 , pp. 3740-3745
    • Lee, V.T.1    Schneewind, O.2
  • 31
    • 0031970595 scopus 로고    scopus 로고
    • Targeting of Yersinia Yop proteins into the cytosol of HeLa cells: One-step translocation of YopE across bacterial and eukaryotic membranes is dependent on SycE chaperone
    • Lee, V.T., Anderson, D.M. Schneewind, O. (1998) Targeting of Yersinia Yop proteins into the cytosol of HeLa cells: one-step translocation of YopE across bacterial and eukaryotic membranes is dependent on SycE chaperone. Mol Microbiol 28 : 593 601.
    • (1998) Mol Microbiol , vol.28 , pp. 593-601
    • Lee, V.T.1    Anderson, D.M.2    Schneewind, O.3
  • 32
    • 0034889276 scopus 로고    scopus 로고
    • A program of Yersinia enterocolitica type III secretion reactions is triggered by specific host signals
    • Lee, V.T., Mazmanian, S.K. Schneewind, O. (2001) A program of Yersinia enterocolitica type III secretion reactions is triggered by specific host signals. J Bacteriol 183 : 4970 4978.
    • (2001) J Bacteriol , vol.183 , pp. 4970-4978
    • Lee, V.T.1    Mazmanian, S.K.2    Schneewind, O.3
  • 33
    • 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. Wolf-Watz, H. (2001) Yersinia YopE is targeted for type III secretion by N-terminal, not mRNA, signals. Mol Microbiol 39 : 520 531.
    • (2001) Mol Microbiol , vol.39 , pp. 520-531
    • Lloyd, S.A.1    Norman, M.2    Rosqvist, R.3    Wolf-Watz, H.4
  • 34
    • 0036197569 scopus 로고    scopus 로고
    • Molecular characterization of the type III secretion signals via analysis of synthetic N-terminal amino acid sequences
    • Lloyd, S.A., Sjöström, M., Andersson, S. Wolf-Watz, H. (2002) Molecular characterization of the type III secretion signals via analysis of synthetic N-terminal amino acid sequences. Mol Microbiol 43 : 51 59.
    • (2002) Mol Microbiol , vol.43 , pp. 51-59
    • Lloyd, S.A.1    Sjöström, M.2    Andersson, S.3    Wolf-Watz, H.4
  • 36
    • 0033591465 scopus 로고    scopus 로고
    • Expanded sequence dependence of thermodynamic parameters improves prediction of RNA secondary structure
    • Mathews, D.H., Sabina, J., Zuker, M. Turner, D.H. (1999) Expanded sequence dependence of thermodynamic parameters improves prediction of RNA secondary structure. J Mol Biol 288 : 911 940.
    • (1999) J Mol Biol , vol.288 , pp. 911-940
    • Mathews, D.H.1    Sabina, J.2    Zuker, M.3    Turner, D.H.4
  • 37
    • 0026065361 scopus 로고
    • Secretion of hybrid proteins by the Yersinia Yop export system
    • Michiels, T. Cornelis, G.R. (1991) Secretion of hybrid proteins by the Yersinia Yop export system. J Bacteriol 173 : 1677 1685.
    • (1991) J Bacteriol , vol.173 , pp. 1677-1685
    • Michiels, T.1    Cornelis, G.R.2
  • 40
    • 27344457144 scopus 로고    scopus 로고
    • The V-antigen of Yersinia forms a distinct structure at the tip of injectisome needles
    • Mueller, C.A., Broz, P., Muller, S.A., Ringler, P., Erne-Brand, F., Sorg, I., et al. (2005) The V-antigen of Yersinia forms a distinct structure at the tip of injectisome needles. Science 310 : 674 676.
    • (2005) Science , vol.310 , pp. 674-676
    • Mueller, C.A.1    Broz, P.2    Muller, S.A.3    Ringler, P.4    Erne-Brand, F.5    Sorg, I.6
  • 41
    • 0037040411 scopus 로고    scopus 로고
    • The ribosomal exit tunnel functions as a discriminating gate
    • Nakatogawa, H. Ito, K. (2002) The ribosomal exit tunnel functions as a discriminating gate. Cell 108 : 629 636.
    • (2002) Cell , vol.108 , pp. 629-636
    • Nakatogawa, H.1    Ito, K.2
  • 42
    • 0019413905 scopus 로고
    • E. coli mutant pleiotropically defective in the export of secreted proteins
    • Oliver, D.B. Beckwith, J. (1981) E. coli mutant pleiotropically defective in the export of secreted proteins. Cell 25 : 765 772.
    • (1981) Cell , vol.25 , pp. 765-772
    • Oliver, D.B.1    Beckwith, J.2
  • 43
    • 0032947339 scopus 로고    scopus 로고
    • YscP of Yersinia pestis is a secreted component of the Yop secretion system
    • Payne, P.L. Straley, S.C. (1999) YscP of Yersinia pestis is a secreted component of the Yop secretion system. J Bacteriol 181 : 2852 2862.
    • (1999) J Bacteriol , vol.181 , pp. 2852-2862
    • Payne, P.L.1    Straley, S.C.2
  • 45
    • 0344826589 scopus 로고    scopus 로고
    • Substrate recognition by the Yersinia type III protein secretion machinery
    • Ramamurthi, K.S. Schneewind, O. (2003) Substrate recognition by the Yersinia type III protein secretion machinery. Mol Microbiol 50 : 1095 1102.
    • (2003) Mol Microbiol , vol.50 , pp. 1095-1102
    • Ramamurthi, K.S.1    Schneewind, O.2
  • 46
    • 11844279779 scopus 로고    scopus 로고
    • A synonymous mutation in Yersinia enterocolitica yopE affects the function of the YopE type III secretion signal
    • Ramamurthi, K.S. Schneewind, O. (2005) A synonymous mutation in Yersinia enterocolitica yopE affects the function of the YopE type III secretion signal. J Bacteriol 187 : 707 715.
    • (2005) J Bacteriol , vol.187 , pp. 707-715
    • Ramamurthi, K.S.1    Schneewind, O.2
  • 47
    • 51549104666 scopus 로고    scopus 로고
    • Impassable YscP substrates and their impact on the Yersinia enterocolitica type III secretion pathway
    • Riordan, K.E., Sorg, J.A., Berube, B.J. Schneewind, O. (2008) Impassable YscP substrates and their impact on the Yersinia enterocolitica type III secretion pathway. J Bacteriol 190 : 6204 6216.
    • (2008) J Bacteriol , vol.190 , pp. 6204-6216
    • Riordan, K.E.1    Sorg, J.A.2    Berube, B.J.3    Schneewind, O.4
  • 48
    • 0027982852 scopus 로고
    • Target cell contact triggers expression and polarized transfer of Yersinia YopE cytotoxin into mammalian cells
    • Rosqvist, R., Magnusson, K.-E. Wolf-Watz, H. (1994) Target cell contact triggers expression and polarized transfer of Yersinia YopE cytotoxin into mammalian cells. EMBO J 13 : 964 972.
    • (1994) EMBO J , vol.13 , pp. 964-972
    • Rosqvist, R.1    Magnusson, K.-E.2    Wolf-Watz, H.3
  • 49
    • 0029123567 scopus 로고
    • Functional conservation of the secretion and translocation machinery for virulence proteins of yersinia, salmonellae and shigellae
    • Rosqvist, R., Håkansson, S., Forsberg, A. Wolf-Watz, H. (1995) Functional conservation of the secretion and translocation machinery for virulence proteins of yersinia, salmonellae and shigellae. EMBO J 14 : 4187 4195.
    • (1995) EMBO J , vol.14 , pp. 4187-4195
    • Rosqvist, R.1    Håkansson, S.2    Forsberg, A.3    Wolf-Watz, H.4
  • 50
    • 0030474296 scopus 로고    scopus 로고
    • Delineation and mutational analysis of the Yersinia pseudotuberculosis YopE domains which mediate translocation across bacterial and eukaryotic cellular membranes
    • Schesser, K., Fritzh-Lindsten, E. Wolf-Watz, H. (1996) Delineation and mutational analysis of the Yersinia pseudotuberculosis YopE domains which mediate translocation across bacterial and eukaryotic cellular membranes. J Bacteriol 178 : 7227 7233.
    • (1996) J Bacteriol , vol.178 , pp. 7227-7233
    • Schesser, K.1    Fritzh-Lindsten, E.2    Wolf-Watz, H.3
  • 51
    • 0030707876 scopus 로고    scopus 로고
    • Death by lethal injection
    • Silhavy, T.J. (1997) Death by lethal injection. Science 278 : 1085 1086.
    • (1997) Science , vol.278 , pp. 1085-1086
    • Silhavy, T.J.1
  • 52
    • 23844485234 scopus 로고    scopus 로고
    • Substrate recognition of type III secretion machines - Testing the RNA signal hypothesis
    • Sorg, J.A., Miller, N.C. Schneewind, O. (2005a) Substrate recognition of type III secretion machines - testing the RNA signal hypothesis. Cell Microbiol 7 : 1217 1225.
    • (2005) Cell Microbiol , vol.7 , pp. 1217-1225
    • Sorg, J.A.1    Miller, N.C.2    Schneewind, O.3
  • 53
    • 26444526690 scopus 로고    scopus 로고
    • Rejection of impassable substrates by Yersinia type III secretion machines
    • Sorg, J.A., Miller, N.C., Marketon, M.M. Schneewind, O. (2005b) Rejection of impassable substrates by Yersinia type III secretion machines. J Bacteriol 187 : 7090 7102.
    • (2005) J Bacteriol , vol.187 , pp. 7090-7102
    • Sorg, J.A.1    Miller, N.C.2    Marketon, M.M.3    Schneewind, O.4
  • 54
    • 33750809905 scopus 로고    scopus 로고
    • Secretion signal recognition by YscN, the Yersinia type III secretion ATPase
    • Sorg, J.A., Blaylock, B. Schneewind, O. (2006) Secretion signal recognition by YscN, the Yersinia type III secretion ATPase. Proc Nat Acad Sci USA 103 : 16490 16495.
    • (2006) Proc Nat Acad Sci USA , vol.103 , pp. 16490-16495
    • Sorg, J.A.1    Blaylock, B.2    Schneewind, O.3
  • 55
    • 34250840609 scopus 로고    scopus 로고
    • YscU recognizes translocators as export substrates of the Yersinia injectisome
    • Sorg, I., Wagner, S., Amstutz, M., Muller, S.A., Broz, P., Lussi, Y., et al. (2007) YscU recognizes translocators as export substrates of the Yersinia injectisome. EMBO J 26 : 3015 3024.
    • (2007) EMBO J , vol.26 , pp. 3015-3024
    • Sorg, I.1    Wagner, S.2    Amstutz, M.3    Muller, S.A.4    Broz, P.5    Lussi, Y.6
  • 56
    • 0028105015 scopus 로고
    • Translocation of a hybrid YopE-adenylate cyclase from Yersinia enterocolitica into HeLa cells
    • Sory, M.-P. Cornelis, G.R. (1994) Translocation of a hybrid YopE-adenylate cyclase from Yersinia enterocolitica into HeLa cells. Mol Microbiol 14 : 583 594.
    • (1994) Mol Microbiol , vol.14 , pp. 583-594
    • Sory, M.-P.1    Cornelis, G.R.2
  • 57
    • 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., Boland, A., Lambermont, I. Cornelis, G.R. (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 USA 92 : 11998 12002.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 11998-12002
    • Sory, M.-P.1    Boland, A.2    Lambermont, I.3    Cornelis, G.R.4
  • 58
    • 0034712727 scopus 로고    scopus 로고
    • A mutant hunt for defects in membrane protein assembly yields mutations affecting the bacterial signal recognition particle and Sec machinery
    • Tian, H., Boyd, D. Beckwith, J. (2000) A mutant hunt for defects in membrane protein assembly yields mutations affecting the bacterial signal recognition particle and Sec machinery. PNAS 97 : 4730 4735.
    • (2000) PNAS , vol.97 , pp. 4730-4735
    • Tian, H.1    Boyd, D.2    Beckwith, J.3
  • 59
    • 25144451293 scopus 로고    scopus 로고
    • The Yersinia pestis type III secretion needle plays a role in the regulation of Yop secretion
    • Torruellas, J., Jackson, M.W., Pennock, J.W. Plano, G.V. (2005) The Yersinia pestis type III secretion needle plays a role in the regulation of Yop secretion. Mol Microbiol 57 : 1719 1733.
    • (2005) Mol Microbiol , vol.57 , pp. 1719-1733
    • Torruellas, J.1    Jackson, M.W.2    Pennock, J.W.3    Plano, G.V.4
  • 60
    • 0027499076 scopus 로고
    • SycE, a chaperone-like protein of Yersinia enterocolitica involved in the secretion of YopE
    • Wattiau, P. Cornelis, G.R. (1993) SycE, a chaperone-like protein of Yersinia enterocolitica involved in the secretion of YopE. Mol Microbiol 8 : 123 131.
    • (1993) Mol Microbiol , vol.8 , pp. 123-131
    • Wattiau, P.1    Cornelis, G.R.2
  • 62
    • 0029886432 scopus 로고    scopus 로고
    • Customized secretion chaperones in pathogenic bacteria
    • Wattiau, P., Woestyn, S. Cornelis, G.R. (1996) Customized secretion chaperones in pathogenic bacteria. Mol Microbiol 20 : 255 262.
    • (1996) Mol Microbiol , vol.20 , pp. 255-262
    • Wattiau, P.1    Woestyn, S.2    Cornelis, G.R.3
  • 63
    • 0031936516 scopus 로고    scopus 로고
    • YopD of Yersinia pestis plays a role in negative regulation of the low-calcium response in addition to its role in translocation of Yops
    • Williams, A.W. Straley, S.C. (1998) YopD of Yersinia pestis plays a role in negative regulation of the low-calcium response in addition to its role in translocation of Yops. J Bacteriol 180 : 350 358.
    • (1998) J Bacteriol , vol.180 , pp. 350-358
    • Williams, A.W.1    Straley, S.C.2
  • 64
    • 0042121256 scopus 로고    scopus 로고
    • Mfold web server for nucleic acid folding and hybridization prediction
    • Zuker, M. (2003) Mfold web server for nucleic acid folding and hybridization prediction. Nucleic Acids Res 31 : 3406 3415.
    • (2003) Nucleic Acids Res , vol.31 , pp. 3406-3415
    • Zuker, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.