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Volumn 164, Issue 6, 2009, Pages 680-687

Expression and localization of the Corynebacterium glutamicum NCgl1221 protein encoding an l-glutamic acid exporter

Author keywords

Confocal microscope; Corynebacterium glutamicum; l glutamate secretion

Indexed keywords

BACTERIAL CELLS; C TERMINUS; CONFOCAL MICROSCOPE; CONFOCAL MICROSCOPES; CORYNEBACTERIUM GLUTAMICUM; CYTOPLASMIC MEMBRANE; E. COLI; FATTY ACID ESTERS; FERMENTATIVE PRODUCTION; FUSION PROTEINS; GREEN FLUORESCENCE PROTEINS; L-GLUTAMATE; L-GLUTAMATE SECRETION; L-GLUTAMIC ACIDS; MECHANOSENSITIVE CHANNEL; MEMBRANE PROTEINS; PROTEIN ENCODING; TOPOLOGY STRUCTURE; TRANSMEMBRANE SEGMENTS;

EID: 70449122478     PISSN: 09445013     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.micres.2009.01.001     Document Type: Article
Times cited : (13)

References (31)
  • 1
    • 33847207787 scopus 로고    scopus 로고
    • Altered metabolic flux due to deletion of odhA causes l-glutamate overproduction in Corynebacterium glutamicum
    • Asakura Y., Kimura E., Usuda Y., Kawahara Y., Matsui K., Osumi T., et al. Altered metabolic flux due to deletion of odhA causes l-glutamate overproduction in Corynebacterium glutamicum. Appl Environ Microbiol 73 (2007) 1308-1319
    • (2007) Appl Environ Microbiol , vol.73 , pp. 1308-1319
    • Asakura, Y.1    Kimura, E.2    Usuda, Y.3    Kawahara, Y.4    Matsui, K.5    Osumi, T.6
  • 2
    • 23944501318 scopus 로고    scopus 로고
    • Subcellular localization and functional expression of the glycerol uptake protein 1 (GUP1) of Saccharomyces cerevisiae tagged with green fluorescent protein
    • Bleve G., Zacheo G., Cappello M.S., Dellaglio F., and Grieco F. Subcellular localization and functional expression of the glycerol uptake protein 1 (GUP1) of Saccharomyces cerevisiae tagged with green fluorescent protein. Biochem J 390 (2005) 145-155
    • (2005) Biochem J , vol.390 , pp. 145-155
    • Bleve, G.1    Zacheo, G.2    Cappello, M.S.3    Dellaglio, F.4    Grieco, F.5
  • 3
    • 33745932646 scopus 로고    scopus 로고
    • Construction and characterization of a bi-functional EGFP/sBAFF fusion protein
    • Cao P., Zhang S.Q., Zhang J., and Wang M. Construction and characterization of a bi-functional EGFP/sBAFF fusion protein. Biochimie 88 (2006) 629-635
    • (2006) Biochimie , vol.88 , pp. 629-635
    • Cao, P.1    Zhang, S.Q.2    Zhang, J.3    Wang, M.4
  • 4
    • 33645454462 scopus 로고    scopus 로고
    • Optimization of membrane protein overexpression and purification using GFP fusions
    • Drew D., Lerch M., Kunji E., Slotboom D.J., and de Gier J.W. Optimization of membrane protein overexpression and purification using GFP fusions. Nat Methods 3 (2006) 303-313
    • (2006) Nat Methods , vol.3 , pp. 303-313
    • Drew, D.1    Lerch, M.2    Kunji, E.3    Slotboom, D.J.4    de Gier, J.W.5
  • 5
    • 0035955445 scopus 로고    scopus 로고
    • Green fluorescent protein as an indicator to monitor membrane protein overexpression in Escherichia coli
    • Drew D.E., von Heijne G., Nordlund P., and de Gier J.W. Green fluorescent protein as an indicator to monitor membrane protein overexpression in Escherichia coli. FEBS Lett 507 (2001) 220-224
    • (2001) FEBS Lett , vol.507 , pp. 220-224
    • Drew, D.E.1    von Heijne, G.2    Nordlund, P.3    de Gier, J.W.4
  • 6
    • 23644458922 scopus 로고    scopus 로고
    • A scalable, GFP-based pipeline for membrane protein overexpression screening and purification
    • Drew D., Slotboom D.J., Friso G., Reda T., Genevaux P., Rapp M., et al. A scalable, GFP-based pipeline for membrane protein overexpression screening and purification. Protein Sci 14 (2005) 2011-2017
    • (2005) Protein Sci , vol.14 , pp. 2011-2017
    • Drew, D.1    Slotboom, D.J.2    Friso, G.3    Reda, T.4    Genevaux, P.5    Rapp, M.6
  • 7
    • 0037022611 scopus 로고    scopus 로고
    • Rapid topology mapping of Escherichia coli inner-membrane proteins by prediction and PhoA/GFP fusion analysis
    • Drew D., Sjöstrand D., Nilsson J., Urbig T., Chin C.N., de Gier J.W., et al. Rapid topology mapping of Escherichia coli inner-membrane proteins by prediction and PhoA/GFP fusion analysis. Proc Natl Acad Sci USA 99 (2002) 2690-2695
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 2690-2695
    • Drew, D.1    Sjöstrand, D.2    Nilsson, J.3    Urbig, T.4    Chin, C.N.5    de Gier, J.W.6
  • 8
    • 0026601812 scopus 로고
    • Excretion of glutamate from Corynebacterium glutamicum triggered by amine surfactants
    • Duperray F., Jezequel D., Ghazi A., Letellier L., and Shechter E. Excretion of glutamate from Corynebacterium glutamicum triggered by amine surfactants. Biochim Biophys Acta 1103 (1992) 250-258
    • (1992) Biochim Biophys Acta , vol.1103 , pp. 250-258
    • Duperray, F.1    Jezequel, D.2    Ghazi, A.3    Letellier, L.4    Shechter, E.5
  • 10
    • 0033917124 scopus 로고    scopus 로고
    • Green fluorescent protein functions as a reporter for protein localization in Escherichia coli
    • Feilmeier B.J., Iseminger G., Schroeder D., Webber H., and Phillips G.J. Green fluorescent protein functions as a reporter for protein localization in Escherichia coli. J Bacteriol 182 (2000) 4068-4076
    • (2000) J Bacteriol , vol.182 , pp. 4068-4076
    • Feilmeier, B.J.1    Iseminger, G.2    Schroeder, D.3    Webber, H.4    Phillips, G.J.5
  • 11
    • 0041429540 scopus 로고    scopus 로고
    • Industrial production of amino acids by coryneform bacteria
    • Hermann T. Industrial production of amino acids by coryneform bacteria. J Biotechnol 104 (2003) 155-172
    • (2003) J Biotechnol , vol.104 , pp. 155-172
    • Hermann, T.1
  • 12
    • 0000482285 scopus 로고
    • Evidence for an efflux carrier system involved in the secretion of glutamate by Corynebacterium glutamicum
    • Hoischen C., and Krämer R. Evidence for an efflux carrier system involved in the secretion of glutamate by Corynebacterium glutamicum. Arch Microbiol 151 (1989) 342-347
    • (1989) Arch Microbiol , vol.151 , pp. 342-347
    • Hoischen, C.1    Krämer, R.2
  • 13
    • 0025300483 scopus 로고
    • Membrane alteration is necessary but not sufficient for effective glutamate secretion in Corynebacterium glutamicum
    • Hoischen C., and Krämer R. Membrane alteration is necessary but not sufficient for effective glutamate secretion in Corynebacterium glutamicum. J Bacteriol 172 (1990) 3409-3416
    • (1990) J Bacteriol , vol.172 , pp. 3409-3416
    • Hoischen, C.1    Krämer, R.2
  • 14
    • 0030919128 scopus 로고    scopus 로고
    • A dtsR gene-disrupted mutant of Brevibacterium lactofermentum requires fatty acids for growth and efficiency produces l-glutamate in the presence of an excess of biotin
    • Kimura E., Abe C., Kawahara Y., Nakamatsu T., and Tokuda H. A dtsR gene-disrupted mutant of Brevibacterium lactofermentum requires fatty acids for growth and efficiency produces l-glutamate in the presence of an excess of biotin. Biochem Biophys Res Commun 234 (1997) 157-161
    • (1997) Biochem Biophys Res Commun , vol.234 , pp. 157-161
    • Kimura, E.1    Abe, C.2    Kawahara, Y.3    Nakamatsu, T.4    Tokuda, H.5
  • 15
    • 0001239046 scopus 로고    scopus 로고
    • Glutamate over-production in Corynebacterium glutamicum triggered by decrease in the level of a complex comprising DtsR and a biotin-containing subunit
    • Kimura E., Yagoshi C., Kawahara Y., Ohsumi T., and Nakamatsu T. Glutamate over-production in Corynebacterium glutamicum triggered by decrease in the level of a complex comprising DtsR and a biotin-containing subunit. Biosci Biotechnol Biochem 63 (1999) 1274-1278
    • (1999) Biosci Biotechnol Biochem , vol.63 , pp. 1274-1278
    • Kimura, E.1    Yagoshi, C.2    Kawahara, Y.3    Ohsumi, T.4    Nakamatsu, T.5
  • 16
    • 0036299777 scopus 로고    scopus 로고
    • Export of l-isoleucine from Corynebacterium glutamicum: a two-gene-encoded member of a new translocator family
    • Kennerknecht N., Sahm H., Yen M.R., Patek M., Saier Jr. M.H., and Eggeling L. Export of l-isoleucine from Corynebacterium glutamicum: a two-gene-encoded member of a new translocator family. J Bacteriol 184 (2002) 3947-3956
    • (2002) J Bacteriol , vol.184 , pp. 3947-3956
    • Kennerknecht, N.1    Sahm, H.2    Yen, M.R.3    Patek, M.4    Saier Jr., M.H.5    Eggeling, L.6
  • 17
    • 85008095806 scopus 로고
    • Studies on the amino acid fermentation. I. Production of l-glutamic acid by various microorganisms
    • Kinoshita S., Udaka S., and Shimono M. Studies on the amino acid fermentation. I. Production of l-glutamic acid by various microorganisms. J Gen Appl Microbiol 3 (1957) 193-205
    • (1957) J Gen Appl Microbiol , vol.3 , pp. 193-205
    • Kinoshita, S.1    Udaka, S.2    Shimono, M.3
  • 18
    • 28344455644 scopus 로고    scopus 로고
    • Biotechnological production of amino acids and derivates: current status and prospects
    • Leuchtenberger W., Huthmacher K., and Drauz K. Biotechnological production of amino acids and derivates: current status and prospects. Appl Microbiol Biotechnol 69 (2005) 1-8
    • (2005) Appl Microbiol Biotechnol , vol.69 , pp. 1-8
    • Leuchtenberger, W.1    Huthmacher, K.2    Drauz, K.3
  • 19
    • 34547211797 scopus 로고    scopus 로고
    • Mutations of the Corynebacterium glutamicum NCgl1221 gene, encoding a mechanosensitive channel homolog, induce l-glutamic acid production
    • Nakamura J., Hirano S., Ito H., and Wachi M. Mutations of the Corynebacterium glutamicum NCgl1221 gene, encoding a mechanosensitive channel homolog, induce l-glutamic acid production. Appl Environ Microbiol 73 (2007) 4491-4498
    • (2007) Appl Environ Microbiol , vol.73 , pp. 4491-4498
    • Nakamura, J.1    Hirano, S.2    Ito, H.3    Wachi, M.4
  • 20
    • 33744950488 scopus 로고    scopus 로고
    • Corynebacterial protein kinase G controls 2-oxoglutarate dehydrogenase activity via the phosphorylation status of the OdhI protein
    • Niebisch A., Schultz A.C., Weil B., and Bott M. Corynebacterial protein kinase G controls 2-oxoglutarate dehydrogenase activity via the phosphorylation status of the OdhI protein. J Biol Chem 281 (2006) 12300-12307
    • (2006) J Biol Chem , vol.281 , pp. 12300-12307
    • Niebisch, A.1    Schultz, A.C.2    Weil, B.3    Bott, M.4
  • 21
    • 0014828434 scopus 로고
    • Product inhibition of the fermentative formation of glutamic acid
    • Nunheimer T.D., Birnbaum J.E., Ihnen D., and Demain A.L. Product inhibition of the fermentative formation of glutamic acid. Appl Microbiol 20 (1970) 215-217
    • (1970) Appl Microbiol , vol.20 , pp. 215-217
    • Nunheimer, T.D.1    Birnbaum, J.E.2    Ihnen, D.3    Demain, A.L.4
  • 24
    • 19044364618 scopus 로고    scopus 로고
    • Ethambutol, a cell wall inhibitor of Mycobacterium tuberculosis, elicits l-glutamate efflux of Corynebacterium glutamicum
    • Radmacher E., Stansen K.C., Besra G.S., Alderwick L.J., Maughan W.N., Hollweg G., et al. Ethambutol, a cell wall inhibitor of Mycobacterium tuberculosis, elicits l-glutamate efflux of Corynebacterium glutamicum. Microbiology 151 (2005) 1359-1368
    • (2005) Microbiology , vol.151 , pp. 1359-1368
    • Radmacher, E.1    Stansen, K.C.2    Besra, G.S.3    Alderwick, L.J.4    Maughan, W.N.5    Hollweg, G.6
  • 25
    • 34548008354 scopus 로고    scopus 로고
    • Glutamate production by Corynebacterium glutamicum: dependence on the oxoglutarate dehydrogenase inhibitor protein OdhI and protein kinase PknG
    • Schultz C., Niebisch A., Gebel L., and Bott M. Glutamate production by Corynebacterium glutamicum: dependence on the oxoglutarate dehydrogenase inhibitor protein OdhI and protein kinase PknG. Appl Microbiol Biotechnol 76 (2007) 691-700
    • (2007) Appl Microbiol Biotechnol , vol.76 , pp. 691-700
    • Schultz, C.1    Niebisch, A.2    Gebel, L.3    Bott, M.4
  • 26
    • 0002640894 scopus 로고
    • Effect of biotin on the bacterial formation of glutamic acid. I. Glutamate formation and cellular permeability of amino acids
    • Shiio I., Otsuka S., and Takahashi M. Effect of biotin on the bacterial formation of glutamic acid. I. Glutamate formation and cellular permeability of amino acids. J Biochem 51 (1962) 56-62
    • (1962) J Biochem , vol.51 , pp. 56-62
    • Shiio, I.1    Otsuka, S.2    Takahashi, M.3
  • 27
    • 0034864184 scopus 로고    scopus 로고
    • l-threonine export: use of peptides to identify a new translocator from Corynebacterium glutamicum
    • Simic P., Sahm H., and Eggeling L. l-threonine export: use of peptides to identify a new translocator from Corynebacterium glutamicum. J Bacteriol 183 (2001) 5317-5324
    • (2001) J Bacteriol , vol.183 , pp. 5317-5324
    • Simic, P.1    Sahm, H.2    Eggeling, L.3
  • 29
    • 0001021102 scopus 로고
    • Biochemical effects of fatty acid and its derivates on l-glutamic acid and the growth of Brevibacterium lactofermentum
    • Takinami K., Yoshii H., Tsuji H., and Okada H. Biochemical effects of fatty acid and its derivates on l-glutamic acid and the growth of Brevibacterium lactofermentum. Agric Biol Chem 29 (1965) 351-359
    • (1965) Agric Biol Chem , vol.29 , pp. 351-359
    • Takinami, K.1    Yoshii, H.2    Tsuji, H.3    Okada, H.4
  • 30
    • 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. A heat shock following electroporation induces highly efficient transformation of Corynebacterium glutamicum with xenogeneic plasmid DNA. Appl Microbiol Biotechnol 52 (1999) 541-545
    • (1999) Appl Microbiol Biotechnol , vol.52 , pp. 541-545
    • van der Rest, M.E.1    Lange, C.2    Molenaar, D.3
  • 31
    • 0029818343 scopus 로고    scopus 로고
    • A new type of transporter with a new type of cellular function: l-lysine export from Corynebacterium glutamicum
    • Vrljic M., Sahm H., and Eggeling L. A new type of transporter with a new type of cellular function: l-lysine export from Corynebacterium glutamicum. Mol Microbiol 22 (1996) 815-826
    • (1996) Mol Microbiol , vol.22 , pp. 815-826
    • Vrljic, M.1    Sahm, H.2    Eggeling, L.3


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