메뉴 건너뛰기




Volumn 49, Issue 4, 2003, Pages 1119-1134

Three pathways for trehalose metabolism in Corynebacterium glutamicum ATCC13032 and their significance in response to osmotic stress

Author keywords

[No Author keywords available]

Indexed keywords

MYCOLIC ACID; TREHALOSE;

EID: 0041528533     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2958.2003.03625.x     Document Type: Article
Times cited : (159)

References (42)
  • 1
    • 85008585468 scopus 로고
    • Taxonomical studies on glutamic acid producing bacteria
    • Abe, S., Takayama, K., and Kinoshita, S. (1967) Taxonomical studies on glutamic acid producing bacteria. J Gen Appl Microbiol 13: 279-301.
    • (1967) J Gen Appl Microbiol , vol.13 , pp. 279-301
    • Abe, S.1    Takayama, K.2    Kinoshita, S.3
  • 2
    • 0022032982 scopus 로고
    • The stabilization of proteins by osmolytes
    • Arakawa, T., and Timasheff, S.N. (1985) The stabilization of proteins by osmolytes. Biophys J 47: 411-414.
    • (1985) Biophys J , vol.47 , pp. 411-414
    • Arakawa, T.1    Timasheff, S.N.2
  • 3
    • 0033771067 scopus 로고    scopus 로고
    • Physiological roles of trehalose in bacteria and yeasts: A comparative analysis
    • Argüelles, J.C. (2000) Physiological roles of trehalose in bacteria and yeasts: a comparative analysis. Arch Microbiol 174: 217-224.
    • (2000) Arch Microbiol , vol.174 , pp. 217-224
    • Argüelles, J.C.1
  • 4
    • 0021457854 scopus 로고
    • Infrared spectroscopic studies on interactions of water and carbohydrates with a biological membrane
    • Crowe, J.H., Crowe, L.M., and Chapman, D. (1984a) Infrared spectroscopic studies on interactions of water and carbohydrates with a biological membrane. Arch Biochem Biophys 232: 400-407.
    • (1984) Arch Biochem Biophys , vol.232 , pp. 400-407
    • Crowe, J.H.1    Crowe, L.M.2    Chapman, D.3
  • 8
    • 0027446935 scopus 로고
    • Disruption of TPS2, the gene encoding the 100-kDa subunit of the trehalose-6-phosphate synthase/phosphatase complex in Saccharomyces cerevisiae, causes accumulation of trehalose-6-phosphate and loss of trehalose-6-phosphate phosphatase activity
    • De Virgilio, C., Bürckert, N., Bell, W., Jenö, W., Boller, T., and Wiemken, A. (1993) Disruption of TPS2, the gene encoding the 100-kDa subunit of the trehalose-6-phosphate synthase/phosphatase complex in Saccharomyces cerevisiae, causes accumulation of trehalose-6-phosphate and loss of trehalose-6-phosphate phosphatase activity. Eur J Biochem 212: 315-323.
    • (1993) Eur J Biochem , vol.212 , pp. 315-323
    • De Virgilio, C.1    Bürckert, N.2    Bell, W.3    Jenö, W.4    Boller, T.5    Wiemken, A.6
  • 9
    • 0025356674 scopus 로고
    • The role of trehalose as a substitute for nitrogen-containing compatible solutes (Ectorhodospira halochloris)
    • Galinski, E., and Herzog, R.M. (1990) The role of trehalose as a substitute for nitrogen-containing compatible solutes (Ectorhodospira halochloris). Arch Microbiol 153: 607-613.
    • (1990) Arch Microbiol , vol.153 , pp. 607-613
    • Galinski, E.1    Herzog, R.M.2
  • 10
    • 0024025446 scopus 로고
    • Biochemical and genetic characterization of osmo-regulatory trehalose synthesis in Escherichia coli
    • Giæver, H.M., Styrvold, O.B., Kaasen, I., and Strøm, A.R. (1988) Biochemical and genetic characterization of osmo-regulatory trehalose synthesis in Escherichia coli. J Bacteriol 170: 2841-2849.
    • (1988) J Bacteriol , vol.170 , pp. 2841-2849
    • Giæver, H.M.1    Styrvold, O.B.2    Kaasen, I.3    Strøm, A.R.4
  • 11
    • 0041688054 scopus 로고
    • Differential plasmid rescue from transgenic mouse DNAs into Escherichia coli K-12
    • Grant, S.G.N., Jessee, J., Bloom, F.R., and Hanahan, D. (1990) Differential plasmid rescue from transgenic mouse DNAs into Escherichia coli K-12. J Bacteriol 166: 253-259.
    • (1990) J Bacteriol , vol.166 , pp. 253-259
    • Grant, S.G.N.1    Jessee, J.2    Bloom, F.R.3    Hanahan, D.4
  • 12
    • 0029562439 scopus 로고
    • Sodium and proline accumulation in Corynebacterium glutamicum as a response to an osmotic saline upshock
    • Guillouet, S., and Engasser, J.M. (1995) Sodium and proline accumulation in Corynebacterium glutamicum as a response to an osmotic saline upshock. Appl Microbiol Biotechnol 44: 496-500.
    • (1995) Appl Microbiol Biotechnol , vol.44 , pp. 496-500
    • Guillouet, S.1    Engasser, J.M.2
  • 13
    • 0031883515 scopus 로고    scopus 로고
    • Role of trehalose in survival of Saccharomyces cerevisiae under osmotic stress
    • Hounsa, C.-G., Brandt, E.V., Thevelein, J., Hohmann, S., and Prior, B.A. (1998) Role of trehalose in survival of Saccharomyces cerevisiae under osmotic stress. Microbiology 144: 671-680.
    • (1998) Microbiology , vol.144 , pp. 671-680
    • Hounsa, C.-G.1    Brandt, E.V.2    Thevelein, J.3    Hohmann, S.4    Prior, B.A.5
  • 14
    • 0025675856 scopus 로고
    • High efficiency transformation of Escherichia coli with plasmids
    • Inoue, H., Nojima, H., and Okayama, H. (1990) High efficiency transformation of Escherichia coli with plasmids. Gene 96: 23-28.
    • (1990) Gene , vol.96 , pp. 23-28
    • Inoue, H.1    Nojima, H.2    Okayama, H.3
  • 15
    • 0028360269 scopus 로고
    • Analysis of the otsBA operon for osmoregulatory trehalose synthesis in Escherichia coli and homology of the OtsA and OtsB proteins to the yeast trehalose-6-phosphate synthase/phosphatase complex
    • Kaasen, I., McDougall, J., and Strøm, A.R. (1994) Analysis of the otsBA operon for osmoregulatory trehalose synthesis in Escherichia coli and homology of the OtsA and OtsB proteins to the yeast trehalose-6-phosphate synthase/phosphatase complex. Gene 145: 9-15.
    • (1994) Gene , vol.145 , pp. 9-15
    • Kaasen, I.1    McDougall, J.2    Strøm, A.R.3
  • 16
    • 0027164654 scopus 로고
    • Isoleucine synthesis in Corynebacterium glutamicum: Molecular analysis of the ilvB-ilvN-ilvC operon
    • Keilhauer, C., Eggeling, L., and Sahm, H. (1993) Isoleucine synthesis in Corynebacterium glutamicum: molecular analysis of the ilvB-ilvN-ilvC operon. J Bacteriol 175: 5595-5603.
    • (1993) J Bacteriol , vol.175 , pp. 5595-5603
    • Keilhauer, C.1    Eggeling, L.2    Sahm, H.3
  • 17
    • 0030294908 scopus 로고    scopus 로고
    • Gene cloning and expression of new trehalose-producing enzymes from the hyperthermophilic archaeum Sulfolobus solfataricus KM1
    • Kobayashi, K., Kato, M., Miura, Y., Kettoku, M., Komeda, T., and Iwamatsu, A. (1996) Gene cloning and expression of new trehalose-producing enzymes from the hyperthermophilic archaeum Sulfolobus solfataricus KM1. Biosci Biotech Biochem 60: 1882-1885.
    • (1996) Biosci Biotech Biochem , vol.60 , pp. 1882-1885
    • Kobayashi, K.1    Kato, M.2    Miura, Y.3    Kettoku, M.4    Komeda, T.5    Iwamatsu, A.6
  • 18
    • 0027512627 scopus 로고
    • Biosynthesis and function of trehalose in Ectothiorhodospira halochloris
    • Lippert, K., Galinski, E.A., and Trüper, H.G. (1993) Biosynthesis and function of trehalose in Ectothiorhodospira halochloris. Antonie Van Leeuwenhoek 63: 85-91.
    • (1993) Antonie Van Leeuwenhoek , vol.63 , pp. 85-91
    • Lippert, K.1    Galinski, E.A.2    Trüper, H.G.3
  • 19
    • 0030573162 scopus 로고    scopus 로고
    • Cloning and sequencing of a cluster of genes encoding novel enzymes of trehalose biosynthesis from thermophilic archaebacterium Sulfolobus acidocaldarius
    • Maruta, K., Mitsuzumi, H., Nakada, T., Kubota, M., Chaen, H., Fukuda, S., et al. (1996) Cloning and sequencing of a cluster of genes encoding novel enzymes of trehalose biosynthesis from thermophilic archaebacterium Sulfolobus acidocaldarius. Biochim Biophys Acta 1291: 177-181.
    • (1996) Biochim Biophys Acta , vol.1291 , pp. 177-181
    • Maruta, K.1    Mitsuzumi, H.2    Nakada, T.3    Kubota, M.4    Chaen, H.5    Fukuda, S.6
  • 20
    • 0028912370 scopus 로고
    • Expression and function of the trehalase genes NTH1 and YBR0106 in Saccharomyces cerevisiae
    • Nwaka, S., Kopp, M., and Holzer, H. (1995a) Expression and function of the trehalase genes NTH1 and YBR0106 in Saccharomyces cerevisiae. J Biol Chem 270: 10193-10198.
    • (1995) J Biol Chem , vol.270 , pp. 10193-10198
    • Nwaka, S.1    Kopp, M.2    Holzer, H.3
  • 21
    • 0028912106 scopus 로고
    • Phenotypic features of trehalose mutants in Saccharomyces cerevisiae
    • Nwaka, S., Mechler, B., Destruelle, M., and Holzer, H. (1995b) Phenotypic features of trehalose mutants in Saccharomyces cerevisiae. FEBS Lett 360: 286-290.
    • (1995) FEBS Lett , vol.360 , pp. 286-290
    • Nwaka, S.1    Mechler, B.2    Destruelle, M.3    Holzer, H.4
  • 22
    • 0031763549 scopus 로고    scopus 로고
    • Corynebacterium glutamicum is equipped with four secondary carriers for compatible solutes: Identification, sequencing, and characterization of the proline/ectoine uptake system, ProP, and the ectoine/proline/glycine betaine carrier, EctP
    • Peter, H., Weil, B., Burkovski, A., Krämer, R., and Morbach, S. (1998) Corynebacterium glutamicum is equipped with four secondary carriers for compatible solutes: identification, sequencing, and characterization of the proline/ectoine uptake system, ProP, and the ectoine/proline/glycine betaine carrier, EctP. J Bacteriol 180: 6005-6012.
    • (1998) J Bacteriol , vol.180 , pp. 6005-6012
    • Peter, H.1    Weil, B.2    Burkovski, A.3    Krämer, R.4    Morbach, S.5
  • 23
    • 0034145295 scopus 로고    scopus 로고
    • Characterization of the in vivo acceptors of the mycoloyl residues transferred by the corynebactedal PS1 and the related mycobacterial antigens 85
    • Puech, V., Bayan, N., Salim, K., Leblon, G., and Daffé, M. (2000) Characterization of the in vivo acceptors of the mycoloyl residues transferred by the corynebactedal PS1 and the related mycobacterial antigens 85. Mol Microbiol 35: 1026-1041.
    • (2000) Mol Microbiol , vol.35 , pp. 1026-1041
    • Puech, V.1    Bayan, N.2    Salim, K.3    Leblon, G.4    Daffé, M.5
  • 24
    • 0027215649 scopus 로고
    • Accumulation of intracellular carbon reserves in relation to chloramphenicol biosynthesis by Streptomyces venezuelae
    • Ranade, N., and Vining, L.C. (1993) Accumulation of intracellular carbon reserves in relation to chloramphenicol biosynthesis by Streptomyces venezuelae. Can J Microbiol 39: 377-383.
    • (1993) Can J Microbiol , vol.39 , pp. 377-383
    • Ranade, N.1    Vining, L.C.2
  • 25
    • 0342545957 scopus 로고    scopus 로고
    • Osmosensor and osmoregulator properties of the betaine carrier BetP from Corynebacterium glutamicum in proteoliposomes
    • Rübenhagen, R., Rönsch, H., Jung, H., Krämer, R., and Morbach, S. (2000) Osmosensor and osmoregulator properties of the betaine carrier BetP from Corynebacterium glutamicum in proteoliposomes. J Biol Chem 275: 735-741.
    • (2000) J Biol Chem , vol.275 , pp. 735-741
    • Rübenhagen, R.1    Rönsch, H.2    Jung, H.3    Krämer, R.4    Morbach, S.5
  • 28
    • 0028289983 scopus 로고
    • Small mobilizable multi-purpose cloning vectors derived from the Escherichia coli plasmids pK18 and pK19: Selection of defined deletions in the chromosome of Corynebacterium glutamicum
    • Schäfer, A., Tauch, A., Jäger, W., Kalinowski, J., Thierbach, G., and Pühler, A. (1994) Small mobilizable multi-purpose cloning vectors derived from the Escherichia coli plasmids pK18 and pK19: selection of defined deletions in the chromosome of Corynebacterium glutamicum. Gene 145: 69-73.
    • (1994) Gene , vol.145 , pp. 69-73
    • Schäfer, A.1    Tauch, A.2    Jäger, W.3    Kalinowski, J.4    Thierbach, G.5    Pühler, A.6
  • 29
    • 0034663370 scopus 로고    scopus 로고
    • Essential role of trehalose in the synthesis and subsequent metabolism of corynomycolic acid in Corynebacterium matruchotii
    • Shimakata, T., and Minatogawa, Y. (2000) Essential role of trehalose in the synthesis and subsequent metabolism of corynomycolic acid in Corynebacterium matruchotii. Arch Biochem Biophys 380: 331-338.
    • (2000) Arch Biochem Biophys , vol.380 , pp. 331-338
    • Shimakata, T.1    Minatogawa, Y.2
  • 30
    • 0043190860 scopus 로고
    • Requirement of glucose for mycolic acid biosynthetic activity localized in the cell wall of Bacterionema matruchii
    • Shimakata, T., Tsubokura, K., and Kusaka, T. (1986) Requirement of glucose for mycolic acid biosynthetic activity localized in the cell wall of Bacterionema matruchii. Arch Biochem Biophys 380: 331-338.
    • (1986) Arch Biochem Biophys , vol.380 , pp. 331-338
    • Shimakata, T.1    Tsubokura, K.2    Kusaka, T.3
  • 31
    • 0029084689 scopus 로고
    • Glutamine uptake by a sodium-dependent secondary transport system in Corynebacterium glutamicum
    • Siewe, R., Well, B., and Krämer, R. (1995) Glutamine uptake by a sodium-dependent secondary transport system in Corynebacterium glutamicum. Arch Microbiol 164: 98-103.
    • (1995) Arch Microbiol , vol.164 , pp. 98-103
    • Siewe, R.1    Well, B.2    Krämer, R.3
  • 32
    • 0032039542 scopus 로고    scopus 로고
    • Multiple effect of trehalose on protein folding in vitro and in vivo
    • Singer, A.A., and Lindquist, S. (1998) Multiple effect of trehalose on protein folding in vitro and in vivo. Mol Cell 1: 639-648.
    • (1998) Mol Cell , vol.1 , pp. 639-648
    • Singer, A.A.1    Lindquist, S.2
  • 33
    • 0027166941 scopus 로고
    • Trehalose metabolism in Escherichia coli: Stress protection and stress regulation of gene expression
    • Strøm, A.R., and Kaasen, I. (1993) Trehalose metabolism in Escherichia coli: stress protection and stress regulation of gene expression. Mol Microbiol 8: 205-210.
    • (1993) Mol Microbiol , vol.8 , pp. 205-210
    • Strøm, A.R.1    Kaasen, I.2
  • 34
    • 0021336752 scopus 로고
    • Regulation of trehalose mobilization in fungi
    • Thevelein, J.M. (1984) Regulation of trehalose mobilization in fungi. Microbiol Rev 48: 42-59.
    • (1984) Microbiol Rev , vol.48 , pp. 42-59
    • Thevelein, J.M.1
  • 36
    • 0032741016 scopus 로고    scopus 로고
    • A heat shock following electroporation induces highly efficient transformation of Corynebacterium glutamicum with xenogeneic plasmid DNA
    • Van der Rest, M.E., Lange, C., and Molenaar, D. (1999) A heat shock following electroporation induces highly efficient transformation of Corynebacterium glutamicum with xenogeneic plasmid DNA. Appl Microbiol Biotechnol 52: 541-545.
    • (1999) Appl Microbiol Biotechnol , vol.52 , pp. 541-545
    • Van Der Rest, M.E.1    Lange, C.2    Molenaar, D.3
  • 37
    • 0032033313 scopus 로고    scopus 로고
    • Trehalose-6-phosphate phosphatases from Arabidopsis thaliana: Identification by functional complementation of the yeast tps2 mutant
    • Vogel, G., Aeschbacher, R.A., Müller, J., Boller, T., and Wiemken, A. (1998) Trehalose-6-phosphate phosphatases from Arabidopsis thaliana: identification by functional complementation of the yeast tps2 mutant. Plant J 13: 673-683.
    • (1998) Plant J , vol.13 , pp. 673-683
    • Vogel, G.1    Aeschbacher, R.A.2    Müller, J.3    Boller, T.4    Wiemken, A.5
  • 38
    • 0024997351 scopus 로고
    • Trehalose in yeast, stress protectant rather than reserve carbohydrate
    • Wiemken, A. (1990) Trehalose in yeast, stress protectant rather than reserve carbohydrate. Antonie Van Leeuwenhoek 58: 209-217.
    • (1990) Antonie Van Leeuwenhoek , vol.58 , pp. 209-217
    • Wiemken, A.1
  • 39
    • 0033014719 scopus 로고    scopus 로고
    • Osmosensing by bacteria: Signals and membrane-based sensors
    • Wood, J.M. (1999) Osmosensing by bacteria: signals and membrane-based sensors. Microbiol Mol Biol Rev 63: 230-262.
    • (1999) Microbiol Mol Biol Rev , vol.63 , pp. 230-262
    • Wood, J.M.1
  • 40
    • 0030973690 scopus 로고    scopus 로고
    • The thermodynamic mechanism of protein stabilization by trehalose
    • Xie, G., and Timasheff, S.N. (1997) The thermodynamic mechanism of protein stabilization by trehalose. Biophys Chem 64: 25-43.
    • (1997) Biophys Chem , vol.64 , pp. 25-43
    • Xie, G.1    Timasheff, S.N.2
  • 41
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors and host strains: Nucleotide sequences of the M13mp18 and pUC19 vectors
    • Yanisch-Perron, C., Vieira, J., and Messing, J. (1985) Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors. Gene 33: 103-119.
    • (1985) Gene , vol.33 , pp. 103-119
    • Yanisch-Perron, C.1    Vieira, J.2    Messing, J.3
  • 42
    • 0032483027 scopus 로고    scopus 로고
    • Osmolytedriven contraction of a random coil protein
    • Youxing, Q., Bolen, C.L., and Bolen, W. (1998) Osmolytedriven contraction of a random coil protein. Proc Natl Acad Sci USA 95: 9268-9273.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 9268-9273
    • Youxing, Q.1    Bolen, C.L.2    Bolen, W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.