메뉴 건너뛰기




Volumn 4, Issue 2, 2011, Pages 286-299

Extracellular Streptomyces vesicles: Amphorae for survival and defence

Author keywords

[No Author keywords available]

Indexed keywords

ACTINORHODINE; ARGININE; CARBON; IRON; ORGANOPHOSPHATE; SIGNAL PEPTIDE;

EID: 79951821961     PISSN: 17517907     EISSN: 17517915     Source Type: Journal    
DOI: 10.1111/j.1751-7915.2011.00251.x     Document Type: Article
Times cited : (65)

References (51)
  • 2
    • 0037435030 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics
    • Aebersold, R., and Mann, M. (2003) Mass spectrometry-based proteomics. Nature 422: 198-207.
    • (2003) Nature , vol.422 , pp. 198-207
    • Aebersold, R.1    Mann, M.2
  • 3
    • 77953181571 scopus 로고    scopus 로고
    • A heterodimer of EsxA and EsxB is involved in sporulation and is secreted by a type VII secretion system in Streptomyces coelicolor
    • Akpe San Roman, S., Facey, P.D., Fernandez-Martinez, L., Rodriguez, C., Vallin, C., Del Sol, R., and Dyson, P. (2010) A heterodimer of EsxA and EsxB is involved in sporulation and is secreted by a type VII secretion system in Streptomyces coelicolor. Microbiology 156: 1719-1729.
    • (2010) Microbiology , vol.156 , pp. 1719-1729
    • Akpe San Roman, S.1    Facey, P.D.2    Fernandez-Martinez, L.3    Rodriguez, C.4    Vallin, C.5    Del Sol, R.6    Dyson, P.7
  • 4
    • 0028321453 scopus 로고
    • Cloning and analysis of a locus (mcr) involved in mitomycin C resistance in Streptomyces lavendulae
    • August, P.R., Flickinger, M.C., and Sherman, D.H. (1994) Cloning and analysis of a locus (mcr) involved in mitomycin C resistance in Streptomyces lavendulae. J Bacteriol 176: 4448-4454.
    • (1994) J Bacteriol , vol.176 , pp. 4448-4454
    • August, P.R.1    Flickinger, M.C.2    Sherman, D.H.3
  • 5
    • 3042692704 scopus 로고    scopus 로고
    • Feature-based prediction of non-classical and leaderless protein secretion
    • Bendtsen, J.D., Jensen, L.J., Blom ., N., Von Heijne, G., and Brunak, S. (2004) Feature-based prediction of non-classical and leaderless protein secretion. Protein Eng Des Sel 17: 349-356.
    • (2004) Protein Eng Des Sel , vol.17 , pp. 349-356
    • Bendtsen, J.D.1    Jensen, L.J.2    Blom, N.3    Von Heijne, G.4    Brunak, S.5
  • 6
    • 27644500162 scopus 로고    scopus 로고
    • Non-classical protein secretion in bacteria
    • doi:10.1186/1471-2180-5-58.
    • Bendtsen, J.D., Kiemer, L., Fausbøll, A., and Brunak, S. (2005) Non-classical protein secretion in bacteria. BMC Microbiol 5: 58. doi:10.1186/1471-2180-5-58.
    • (2005) BMC Microbiol , vol.5 , pp. 58
    • Bendtsen, J.D.1    Kiemer, L.2    Fausbøll, A.3    Brunak, S.4
  • 7
    • 0009624950 scopus 로고
    • Isolation and biology of a Streptomyces sp. causing potato scab in soils below pH 5.0
    • Bonde, M.R., and McIntyre, G.A. (1968) Isolation and biology of a Streptomyces sp. causing potato scab in soils below pH 5.0. Am J Potato Res 45: 273-278.
    • (1968) Am J Potato Res , vol.45 , pp. 273-278
    • Bonde, M.R.1    McIntyre, G.A.2
  • 8
    • 0029154185 scopus 로고
    • Cloning and characterization of a gene encoding a secreted tripeptidyl aminopeptidase from Streptomyces lividans 66
    • Butler, M.J., Binnie, C., DiZonno, M.A., Krygsman, P., Soltes, G.A., Soostmeyer, G., etal. (1995) Cloning and characterization of a gene encoding a secreted tripeptidyl aminopeptidase from Streptomyces lividans 66. Appl Environ Microbiol 61: 3145-3150.
    • (1995) Appl Environ Microbiol , vol.61 , pp. 3145-3150
    • Butler, M.J.1    Binnie, C.2    DiZonno, M.A.3    Krygsman, P.4    Soltes, G.A.5    Soostmeyer, G.6
  • 11
    • 0038219647 scopus 로고    scopus 로고
    • Ferritins, iron uptake and storage from the bacterioferritin viewpoint
    • Carrondo, M.A. (2003) Ferritins, iron uptake and storage from the bacterioferritin viewpoint. EMBO J 22: 1959-1968.
    • (2003) EMBO J , vol.22 , pp. 1959-1968
    • Carrondo, M.A.1
  • 12
    • 50149097305 scopus 로고    scopus 로고
    • The dihydrolipoamide dehydrogenase of Aeromonas caviae ST exhibits NADH-dependent tellurite reductase activity
    • Castro, M.E., Molina, R., Díaz, W., Pichuantes, S.E., and Vásquez, C.C. (2008) The dihydrolipoamide dehydrogenase of Aeromonas caviae ST exhibits NADH-dependent tellurite reductase activity. Biochem Biophys Res Commun 375: 91-94.
    • (2008) Biochem Biophys Res Commun , vol.375 , pp. 91-94
    • Castro, M.E.1    Molina, R.2    Díaz, W.3    Pichuantes, S.E.4    Vásquez, C.C.5
  • 13
    • 0029612304 scopus 로고
    • Recovery of respiration following the SOS response of Escherichia coli requires RecA-mediated induction of 2-keto-4-hydroxyglutarate aldolase
    • Cayrol, C., Petit, C., Raynaud, B., Capdevielle, J., Guillemot, J.C., and Defais, M. (1995) Recovery of respiration following the SOS response of Escherichia coli requires RecA-mediated induction of 2-keto-4-hydroxyglutarate aldolase. Proc Natl Acad Sci USA 92: 11806-11809.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 11806-11809
    • Cayrol, C.1    Petit, C.2    Raynaud, B.3    Capdevielle, J.4    Guillemot, J.C.5    Defais, M.6
  • 15
    • 79951831567 scopus 로고    scopus 로고
    • NMR solution structure of KP-TerB, a tellurite-resistance protein from Klebsiella pneumoniae
    • Chiang, S.K., Lou, Y.C., and Chen, C. (2008) NMR solution structure of KP-TerB, a tellurite-resistance protein from Klebsiella pneumoniae. Cell Mol Life Sci 67: 179-199.
    • (2008) Cell Mol Life Sci , vol.67 , pp. 179-199
    • Chiang, S.K.1    Lou, Y.C.2    Chen, C.3
  • 16
    • 23844490045 scopus 로고    scopus 로고
    • The high-affinity phosphate-binding protein PstS is accumulated under high fructose concentrations and mutation of the corresponding gene affects differentiation in Streptomyces lividans
    • Díaz, M., Esteban, A., Fernández-Abalos, J.M., and Santamaría, R.I. (2005) The high-affinity phosphate-binding protein PstS is accumulated under high fructose concentrations and mutation of the corresponding gene affects differentiation in Streptomyces lividans. Microbiology 151: 2583-2592.
    • (2005) Microbiology , vol.151 , pp. 2583-2592
    • Díaz, M.1    Esteban, A.2    Fernández-Abalos, J.M.3    Santamaría, R.I.4
  • 17
    • 77955296751 scopus 로고    scopus 로고
    • Secretion signal and protein targeting in bacteria: a biological puzzle
    • Filloux, A. (2010) Secretion signal and protein targeting in bacteria: a biological puzzle. J Bacteriol 192: 3847-3849.
    • (2010) J Bacteriol , vol.192 , pp. 3847-3849
    • Filloux, A.1
  • 19
    • 28944453311 scopus 로고    scopus 로고
    • Peptidyl prolyl cis/trans-isomerases: comparative reactivities of cyclophilins, FK506-binding proteins, and parvulins with fluorinated oligopeptide and protein substrates
    • Golbik, R., Yu, C., Weyher-Stingl, E., Huber, R., Moroder, L., Budisa, N., and Schiene-Fischer, C. (2005) Peptidyl prolyl cis/trans-isomerases: comparative reactivities of cyclophilins, FK506-binding proteins, and parvulins with fluorinated oligopeptide and protein substrates. Biochemistry 44: 16026-16034.
    • (2005) Biochemistry , vol.44 , pp. 16026-16034
    • Golbik, R.1    Yu, C.2    Weyher-Stingl, E.3    Huber, R.4    Moroder, L.5    Budisa, N.6    Schiene-Fischer, C.7
  • 20
    • 1442325440 scopus 로고    scopus 로고
    • Metabolism and function in animal tissues of agmatine, a biogenic amine formed from arginine
    • Grillo, M.A., and Colombatto, S. (2004) Metabolism and function in animal tissues of agmatine, a biogenic amine formed from arginine. Amino Acids 26: 3-8.
    • (2004) Amino Acids , vol.26 , pp. 3-8
    • Grillo, M.A.1    Colombatto, S.2
  • 21
    • 33748777392 scopus 로고    scopus 로고
    • In vivo monitoring of the potassium channel KcsA in Streptomyces lividans hyphae using immuno-electron microscopy and energy-filtering transmission electron microscopy
    • Hegermann, J., Overbeck, J., and Schrempf, H. (2006) In vivo monitoring of the potassium channel KcsA in Streptomyces lividans hyphae using immuno-electron microscopy and energy-filtering transmission electron microscopy. Microbiology 152: 2831-2841.
    • (2006) Microbiology , vol.152 , pp. 2831-2841
    • Hegermann, J.1    Overbeck, J.2    Schrempf, H.3
  • 22
    • 50249150710 scopus 로고    scopus 로고
    • Deletion of xylR gene enhances expression of xylose isomerase in Streptomyces lividans TK24
    • Heo, G.Y., Kim, W.C., Joo, G.J., Kwak, Y.Y., Shin, J.H., Roh, D.H., etal. (2008) Deletion of xylR gene enhances expression of xylose isomerase in Streptomyces lividans TK24. J Microbiol Biotechnol 18: 837-844.
    • (2008) J Microbiol Biotechnol , vol.18 , pp. 837-844
    • Heo, G.Y.1    Kim, W.C.2    Joo, G.J.3    Kwak, Y.Y.4    Shin, J.H.5    Roh, D.H.6
  • 23
    • 41649116701 scopus 로고    scopus 로고
    • Disclosure of the mycobacterial outer membrane: cryo-electron tomography and vitreous sections reveal the lipid bilayer structure
    • Hoffmann, C., Leis, A., Niederweis, M., Plitzko, J.M., and Engelhardt, H. (2008) Disclosure of the mycobacterial outer membrane: cryo-electron tomography and vitreous sections reveal the lipid bilayer structure. Proc Natl Acad Sci USA 105: 3963-3967.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 3963-3967
    • Hoffmann, C.1    Leis, A.2    Niederweis, M.3    Plitzko, J.M.4    Engelhardt, H.5
  • 24
    • 0003728297 scopus 로고
    • Genetic Manipulation of Streptomyces: A Laboratory Manual
    • Norwich, UK: John Innes Foundation.
    • Hopwood, D.A., Bibb, M.J., Chater, K.F., Kieser, T., Bruton, C.J., Kieser, H.M., etal. (1985) Genetic Manipulation of Streptomyces: A Laboratory Manual. Norwich, UK: John Innes Foundation.
    • (1985)
    • Hopwood, D.A.1    Bibb, M.J.2    Chater, K.F.3    Kieser, T.4    Bruton, C.J.5    Kieser, H.M.6
  • 25
    • 50649117912 scopus 로고    scopus 로고
    • Cellular defenses against superoxide and hydrogen peroxide
    • Imlay, J.A. (2008) Cellular defenses against superoxide and hydrogen peroxide. Annu Rev Biochem 77: 755-776.
    • (2008) Annu Rev Biochem , vol.77 , pp. 755-776
    • Imlay, J.A.1
  • 26
    • 84872106345 scopus 로고
    • Production of streptomycin by Streptomyces bikinienis
    • Johnstone, D.B., and Waksman, S.A. (1947) Production of streptomycin by Streptomyces bikinienis. J Series Rutgers Uni 55: 317-236.
    • (1947) J Series Rutgers Uni , vol.55 , pp. 317-236
    • Johnstone, D.B.1    Waksman, S.A.2
  • 27
    • 33644840483 scopus 로고    scopus 로고
    • New insights into the families of PLC enzymes: looking back and going forward
    • Katan, M. (2005) New insights into the families of PLC enzymes: looking back and going forward. Biochem J 391: e7-e9.
    • (2005) Biochem J , vol.391
    • Katan, M.1
  • 28
    • 0031719418 scopus 로고    scopus 로고
    • Uptake and synthesis of compatible solutes as microbial stress responses to high-osmolality environments
    • Kempf, B., and Bremer, E. (1998) Uptake and synthesis of compatible solutes as microbial stress responses to high-osmolality environments. Arch Microbiol 170: 319-330.
    • (1998) Arch Microbiol , vol.170 , pp. 319-330
    • Kempf, B.1    Bremer, E.2
  • 29
    • 77953588476 scopus 로고    scopus 로고
    • A molecular key for building hyphae aggregates: the role of the newly identified Streptomyces protein HyaS
    • Koebsch, I., Overbeck, J., Piepmeyer, S., Meschke, H., and Schrempf, H. (2009) A molecular key for building hyphae aggregates: the role of the newly identified Streptomyces protein HyaS. Microb Biotechnol 2: 343-360.
    • (2009) Microb Biotechnol , vol.2 , pp. 343-360
    • Koebsch, I.1    Overbeck, J.2    Piepmeyer, S.3    Meschke, H.4    Schrempf, H.5
  • 30
    • 27744480818 scopus 로고    scopus 로고
    • Bacterial outer membrane vesicles and the host-pathogen interaction
    • Kuehn, M.J., and Kesty, N.C. (2005) Bacterial outer membrane vesicles and the host-pathogen interaction. Genes Dev 19: 2645-2655.
    • (2005) Genes Dev , vol.19 , pp. 2645-2655
    • Kuehn, M.J.1    Kesty, N.C.2
  • 31
    • 77957959533 scopus 로고    scopus 로고
    • Biological functions and biogenesis of secreted bacterial outer membrane vesicles
    • Kulp, A., and Kuehn, M.J. (2010) Biological functions and biogenesis of secreted bacterial outer membrane vesicles. Annu Rev Microbiol 64: 163-184.
    • (2010) Annu Rev Microbiol , vol.64 , pp. 163-184
    • Kulp, A.1    Kuehn, M.J.2
  • 32
    • 0002567384 scopus 로고
    • The Prokaryotes: A Handbook on Habitats, Isolation and Identification of Bacteria
    • In Starr, M.P., Stolp, H., Trüper, H.G., Balows, A., and Schlegel, H. (eds). Berlin, Germany: Springer-Verlag
    • Kutzner, H.J. (1981) The family Streptomycetaceae. In The Prokaryotes: A Handbook on Habitats, Isolation and Identification of Bacteria. Starr, M.P., Stolp, H., Trüper, H.G., Balows, A., and Schlegel, H. (eds). Berlin, Germany: Springer-Verlag, pp. 2028-2090.
    • (1981) The family Streptomycetaceae , pp. 2028-2090
    • Kutzner, H.J.1
  • 33
    • 73149088617 scopus 로고    scopus 로고
    • Gram-positive bacteria produce membrane vesicles: proteomics-based characterization of Staphylococcus aureus-derived membrane vesicles
    • Lee, E.Y., Choi, D.Y., Kim, D.K., Kim, J.W., Park, J.O., Kim, S., etal. (2009) Gram-positive bacteria produce membrane vesicles: proteomics-based characterization of Staphylococcus aureus-derived membrane vesicles. Proteomics 9: 5425-5436.
    • (2009) Proteomics , vol.9 , pp. 5425-5436
    • Lee, E.Y.1    Choi, D.Y.2    Kim, D.K.3    Kim, J.W.4    Park, J.O.5    Kim, S.6
  • 34
    • 0030002937 scopus 로고    scopus 로고
    • A major autolysin of Pseudomonas aeruginosa: subcellular distribution, potential role in cell growth and division and secretion in surface membrane vesicles
    • Li, Z., Clarke, A.J., and Beveridge, T.J. (1996) A major autolysin of Pseudomonas aeruginosa: subcellular distribution, potential role in cell growth and division and secretion in surface membrane vesicles. J Bacteriol 178: 2479-2488.
    • (1996) J Bacteriol , vol.178 , pp. 2479-2488
    • Li, Z.1    Clarke, A.J.2    Beveridge, T.J.3
  • 35
    • 20444502568 scopus 로고    scopus 로고
    • Secretion systems for secondary metabolites: how producer cells send out messages of intercellular communication
    • Martín, J.F., Casqueiro, J., and Liras, P. (2005) Secretion systems for secondary metabolites: how producer cells send out messages of intercellular communication. Curr Opin Microbiol 8: 282-293.
    • (2005) Curr Opin Microbiol , vol.8 , pp. 282-293
    • Martín, J.F.1    Casqueiro, J.2    Liras, P.3
  • 36
    • 33746561249 scopus 로고    scopus 로고
    • Special delivery: vesicle trafficking in prokaryotes
    • Mashburn-Warren, L.M., and Whiteley, M. (2006) Special delivery: vesicle trafficking in prokaryotes. Mol Microbiol 61: 839-846.
    • (2006) Mol Microbiol , vol.61 , pp. 839-846
    • Mashburn-Warren, L.M.1    Whiteley, M.2
  • 37
    • 77953547778 scopus 로고    scopus 로고
    • Streptomyces lividans inhibits the proliferation of the fungus Verticillium dahliae on seeds and roots of Arabidopsis thaliana
    • Meschke, H., and Schrempf, H. (2010) Streptomyces lividans inhibits the proliferation of the fungus Verticillium dahliae on seeds and roots of Arabidopsis thaliana. Microb Biotechnol 3: 428-433.
    • (2010) Microb Biotechnol , vol.3 , pp. 428-433
    • Meschke, H.1    Schrempf, H.2
  • 38
    • 20444411648 scopus 로고    scopus 로고
    • The moving frontier in nitric oxide-dependent signaling
    • Nathan, C. (2004) The moving frontier in nitric oxide-dependent signaling. Sci STKE 257: pe52.
    • (2004) Sci STKE , vol.257
    • Nathan, C.1
  • 39
    • 13844264476 scopus 로고    scopus 로고
    • TOM software toolbox: acquisition and analysis for electron tomography
    • Nickell, S., Förster, F., Linaroudis, A., Net, W.D., Beck, F., Hegerl, R., etal. (2005) TOM software toolbox: acquisition and analysis for electron tomography. J Struct Biol 149: 227-234.
    • (2005) J Struct Biol , vol.149 , pp. 227-234
    • Nickell, S.1    Förster, F.2    Linaroudis, A.3    Net, W.D.4    Beck, F.5    Hegerl, R.6
  • 41
    • 78751572735 scopus 로고    scopus 로고
    • NMR structure and calcium-binding properties of the tellurite resistance protein TerD from Klebsiella pneumoniae
    • Pan, Y.R., Lou, Y.C., Seven, A.B., Rizo, J., and Chen, C.J. (2011) NMR structure and calcium-binding properties of the tellurite resistance protein TerD from Klebsiella pneumoniae. J Mol Biol 405: 1188-1201.
    • (2011) J Mol Biol , vol.405 , pp. 1188-1201
    • Pan, Y.R.1    Lou, Y.C.2    Seven, A.B.3    Rizo, J.4    Chen, C.J.5
  • 42
    • 0018320319 scopus 로고
    • Genetics of actinorhodin biosynthesis by Streptomyces coelicolor A3(2)
    • Rudd, B.A., and Hopwood, D.A. (1979) Genetics of actinorhodin biosynthesis by Streptomyces coelicolor A3(2). J Gen Microbiol 114: 35-43.
    • (1979) J Gen Microbiol , vol.114 , pp. 35-43
    • Rudd, B.A.1    Hopwood, D.A.2
  • 43
    • 67650741686 scopus 로고    scopus 로고
    • Phosphate and carbon source regulation of two PhoP-dependent glycerophosphodiester phosphodiesterase genes of Streptomyces coelicolor
    • Santos-Beneit, F., Rodríguez-García, A., Apel, A.K., and Martín, J.F. (2009) Phosphate and carbon source regulation of two PhoP-dependent glycerophosphodiester phosphodiesterase genes of Streptomyces coelicolor. Microbiology 155: 1800-1811.
    • (2009) Microbiology , vol.155 , pp. 1800-1811
    • Santos-Beneit, F.1    Rodríguez-García, A.2    Apel, A.K.3    Martín, J.F.4
  • 45
    • 79951821086 scopus 로고    scopus 로고
    • The Prokaryotes
    • Dworkin, M., Falkow, S., Rosenberg, E., Schleifer, K.H., and Stackebrandt, E. (eds). Berlin, Germany: Springer-Verlag
    • Schrempf, H. (2007) The family of Streptomycetaceae: part II molecular biology. In The Prokaryotes, Vol. 3. Dworkin, M., Falkow, S., Rosenberg, E., Schleifer, K.H., and Stackebrandt, E. (eds). Berlin, Germany: Springer-Verlag, pp. 605-622.
    • (2007) The family of Streptomycetaceae: part II molecular biology , vol.3 , pp. 605-622
    • Schrempf, H.1
  • 46
    • 46749142941 scopus 로고    scopus 로고
    • Analysis of outer membrane vesicle associated proteins isolated from the plant pathogenic bacterium Xanthomonas campestris pv. campestris
    • doi:10.1186/1471-2180-8-87
    • Sidhu, V.K., Vorhölter, F.J., Niehaus, K., and Watt, S.A. (2008) Analysis of outer membrane vesicle associated proteins isolated from the plant pathogenic bacterium Xanthomonas campestris pv. campestris. BMC Microbiol 8: 87. doi:10.1186/1471-2180-8-87.
    • (2008) BMC Microbiol , vol.8 , pp. 87
    • Sidhu, V.K.1    Vorhölter, F.J.2    Niehaus, K.3    Watt, S.A.4
  • 47
    • 33847212848 scopus 로고    scopus 로고
    • Concerted responses between the chitin-binding protein secreting Streptomyces olivaceoviridis and Aspergillus proliferans
    • Siemieniewicz, K.W., and Schrempf, H. (2007) Concerted responses between the chitin-binding protein secreting Streptomyces olivaceoviridis and Aspergillus proliferans. Microbiology 153: 593-600.
    • (2007) Microbiology , vol.153 , pp. 593-600
    • Siemieniewicz, K.W.1    Schrempf, H.2
  • 48
    • 33846699574 scopus 로고    scopus 로고
    • Elucidating the biosynthesis of chitin filaments and their configuration with specific proteins and electron microscopy
    • Siemieniewicz, K.W., Kajla, M.K., and Schrempf, H. (2007) Elucidating the biosynthesis of chitin filaments and their configuration with specific proteins and electron microscopy. Macromol Biosci 7: 40-47.
    • (2007) Macromol Biosci , vol.7 , pp. 40-47
    • Siemieniewicz, K.W.1    Kajla, M.K.2    Schrempf, H.3
  • 50
    • 77049131147 scopus 로고
    • Degeneration and regeneration of Streptomyces griseus
    • Williams, A.M., and McCoy, E. (1953) Degeneration and regeneration of Streptomyces griseus. Appl Microbiol 1: 307-313.
    • (1953) Appl Microbiol , vol.1 , pp. 307-313
    • Williams, A.M.1    McCoy, E.2
  • 51
    • 79951847845 scopus 로고    scopus 로고
    • Protein transport across and into cell membranes in bacteria and archaea
    • Yuan, J., Zweers, J.C., van Dijl, J.M., and Dalbey, R.E. (2010) Protein transport across and into cell membranes in bacteria and archaea. Protein Sci 17: 785-789.
    • (2010) Protein Sci , vol.17 , pp. 785-789
    • Yuan, J.1    Zweers, J.C.2    van Dijl, J.M.3    Dalbey, R.E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.