메뉴 건너뛰기




Volumn 73, Issue 10, 2007, Pages 3300-3306

Proteomic approach for characterization of hop-inducible proteins in Lactobacillus brevis

Author keywords

[No Author keywords available]

Indexed keywords

BEVERAGES; BIOLOGICAL MEMBRANES; CELLS; LACTIC ACID; METABOLISM; PROTEINS;

EID: 34249668342     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/AEM.00124-07     Document Type: Article
Times cited : (52)

References (37)
  • 1
    • 0019163514 scopus 로고
    • Regulation of the synthesis of nucleoside catabolic enzymes in Escherichia coli: Further analysis of a deo Oc mutant strain
    • Albrechtsen, H., and S. I. Ahmad. 1980. Regulation of the synthesis of nucleoside catabolic enzymes in Escherichia coli: further analysis of a deo Oc mutant strain. Mol. Gen. Genet. 179:457-460.
    • (1980) Mol. Gen. Genet , vol.179 , pp. 457-460
    • Albrechtsen, H.1    Ahmad, S.I.2
  • 2
    • 0027535581 scopus 로고
    • Purification and properties of the RecR protein from Bacillus subtilis 168
    • Alonso, J. C., A. C. Stiege, B. Dobrinski, and R. Lurz. 1993. Purification and properties of the RecR protein from Bacillus subtilis 168. J. Biol. Chem. 268:1424-1429.
    • (1993) J. Biol. Chem , vol.268 , pp. 1424-1429
    • Alonso, J.C.1    Stiege, A.C.2    Dobrinski, B.3    Lurz, R.4
  • 3
    • 0035184515 scopus 로고    scopus 로고
    • Some Lactobacillus L-lactate dehydrogenases exhibit comparable catalytic activities for pyruvate and oxaloacetate
    • Arai, K., T. Kamata, H. Uchikoba, S. Fushinobu, H. Matsuzawa, and H. Taguchi. 2001. Some Lactobacillus L-lactate dehydrogenases exhibit comparable catalytic activities for pyruvate and oxaloacetate. J. Bacteriol. 183:397-400.
    • (2001) J. Bacteriol , vol.183 , pp. 397-400
    • Arai, K.1    Kamata, T.2    Uchikoba, H.3    Fushinobu, S.4    Matsuzawa, H.5    Taguchi, H.6
  • 4
    • 0021248136 scopus 로고
    • Manganese acquisition by Lactobacillus plantarum
    • Archibald, F. S., and M. N. Duong. 1984. Manganese acquisition by Lactobacillus plantarum. J. Bacteriol. 158:1-8.
    • (1984) J. Bacteriol , vol.158 , pp. 1-8
    • Archibald, F.S.1    Duong, M.N.2
  • 7
    • 33750052293 scopus 로고    scopus 로고
    • Characterization of a highly hop-resistant Lactobacillus brevis strain lacking hop transport
    • Behr, J., M. G. Gänzle, and R. F. Vogel. 2006. Characterization of a highly hop-resistant Lactobacillus brevis strain lacking hop transport. Appl. Environ. Microbiol. 72:6483-6492.
    • (2006) Appl. Environ. Microbiol , vol.72 , pp. 6483-6492
    • Behr, J.1    Gänzle, M.G.2    Vogel, R.F.3
  • 8
    • 0030826911 scopus 로고    scopus 로고
    • Acid habituation of Escherichia coli and the potential role of cyclopropane fatty acids in low pH tolerance
    • Brown, J. L., T. Ross, T. A. McMeekin, and P. D. Nichols. 1997. Acid habituation of Escherichia coli and the potential role of cyclopropane fatty acids in low pH tolerance. Int. J. Food Microbiol. 37:163-173.
    • (1997) Int. J. Food Microbiol , vol.37 , pp. 163-173
    • Brown, J.L.1    Ross, T.2    McMeekin, T.A.3    Nichols, P.D.4
  • 9
    • 0032461412 scopus 로고    scopus 로고
    • A superfamily of metalloenzymes unifies phosphopentomutase and cofactor-independent phosphoglycerate mutase with alkaline phosphatases and sulfatases
    • Galperin, M. Y., A. Bairoch, and E. V. Koonin. 1998. A superfamily of metalloenzymes unifies phosphopentomutase and cofactor-independent phosphoglycerate mutase with alkaline phosphatases and sulfatases. Protein Sci. 7:1829-1835.
    • (1998) Protein Sci , vol.7 , pp. 1829-1835
    • Galperin, M.Y.1    Bairoch, A.2    Koonin, E.V.3
  • 11
    • 34249666144 scopus 로고    scopus 로고
    • Harder, A. 2001. Wissenschaftszentrum für Ernährung, Landnutzung und Umwelt. Dissertation. FG Proteomik, Technische Universität München, Munich, Germany.
    • Harder, A. 2001. Wissenschaftszentrum für Ernährung, Landnutzung und Umwelt. Dissertation. FG Proteomik, Technische Universität München, Munich, Germany.
  • 12
    • 0035000291 scopus 로고    scopus 로고
    • Molecular cloning of a putative divalent-cation transporter gene as a new genetic marker for the identification of Lactobacillus brevis strains capable of growing in beer
    • Hayashi, N., M. Ito, S. Horiike, and H. Taguchi. 2001. Molecular cloning of a putative divalent-cation transporter gene as a new genetic marker for the identification of Lactobacillus brevis strains capable of growing in beer. Appl. Microbiol. Biotechnol. 55:596-603.
    • (2001) Appl. Microbiol. Biotechnol , vol.55 , pp. 596-603
    • Hayashi, N.1    Ito, M.2    Horiike, S.3    Taguchi, H.4
  • 13
    • 0030881850 scopus 로고    scopus 로고
    • Proteolytic activity of the ATP-dependent protease HslVU can be uncoupled from ATP hydrolysis
    • Huang, H., and A. L. Goldberg. 1997. Proteolytic activity of the ATP-dependent protease HslVU can be uncoupled from ATP hydrolysis. J. Biol. Chem. 272:21364-21372.
    • (1997) J. Biol. Chem , vol.272 , pp. 21364-21372
    • Huang, H.1    Goldberg, A.L.2
  • 14
    • 0035958869 scopus 로고    scopus 로고
    • Functional assignment of the 20 S proteasome from Trypanosoma brucei using mass spectrometry and new bioinformatics approaches
    • Huang, L., R. J. Jacob, S. C. Pegg, M. A. Baldwin, C. C. Wang, A. L. Burlingame, and P. C. Babbitt. 2001. Functional assignment of the 20 S proteasome from Trypanosoma brucei using mass spectrometry and new bioinformatics approaches. J. Biol. Chem. 276:28327-28339.
    • (2001) J. Biol. Chem , vol.276 , pp. 28327-28339
    • Huang, L.1    Jacob, R.J.2    Pegg, S.C.3    Baldwin, M.A.4    Wang, C.C.5    Burlingame, A.L.6    Babbitt, P.C.7
  • 15
    • 13844271209 scopus 로고    scopus 로고
    • Informatics for protein identification by mass spectrometry
    • Johnson, R. S., M. T. Davis, J. A. Taylor, and S. D. Patterson. 2005. Informatics for protein identification by mass spectrometry. Methods 35:223-236.
    • (2005) Methods , vol.35 , pp. 223-236
    • Johnson, R.S.1    Davis, M.T.2    Taylor, J.A.3    Patterson, S.D.4
  • 16
    • 0038240674 scopus 로고    scopus 로고
    • Emerging themes in manganese transport, biochemistry and pathogenesis in bacteria
    • Kehres, D. G., and M. E. Maguire. 2003. Emerging themes in manganese transport, biochemistry and pathogenesis in bacteria. FEMS Microbiol. Rev. 27:263-290.
    • (2003) FEMS Microbiol. Rev , vol.27 , pp. 263-290
    • Kehres, D.G.1    Maguire, M.E.2
  • 17
    • 0034931104 scopus 로고    scopus 로고
    • Quantitative and reproducible two-dimensional gel analysis using Phoretix 2D Full
    • Mahon, P., and P. Dupree. 2001. Quantitative and reproducible two-dimensional gel analysis using Phoretix 2D Full. Electrophoresis 22:2075-2085.
    • (2001) Electrophoresis , vol.22 , pp. 2075-2085
    • Mahon, P.1    Dupree, P.2
  • 18
    • 0037013983 scopus 로고    scopus 로고
    • Glucosamine-6-phosphate synthase - the multi-facets enzyme
    • Milewski, S. 2002. Glucosamine-6-phosphate synthase - the multi-facets enzyme. Biochim. Biophys. Acta 1597:173-192.
    • (2002) Biochim. Biophys. Acta , vol.1597 , pp. 173-192
    • Milewski, S.1
  • 21
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins, D. N., D. J. Pappin, D. M. Creasy, and J. S. Cottrell. 1999. Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 20:3551-3567.
    • (1999) Electrophoresis , vol.20 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.2    Creasy, D.M.3    Cottrell, J.S.4
  • 22
    • 0015935354 scopus 로고
    • Purification and properties of purine nucleoside phosphorylase from Salmonella typhimurium
    • Robertson, B. C., and P. A. Hoffee. 1973. Purification and properties of purine nucleoside phosphorylase from Salmonella typhimurium. J. Biol. Chem. 248:2040-2043.
    • (1973) J. Biol. Chem , vol.248 , pp. 2040-2043
    • Robertson, B.C.1    Hoffee, P.A.2
  • 23
    • 0242659822 scopus 로고    scopus 로고
    • Beer spoilage bacteria and hop resistance
    • Sakamoto, K., and W. N. Konings. 2003. Beer spoilage bacteria and hop resistance. Int. J. Food Microbiol. 89:105-124.
    • (2003) Int. J. Food Microbiol , vol.89 , pp. 105-124
    • Sakamoto, K.1    Konings, W.N.2
  • 24
    • 0034870399 scopus 로고    scopus 로고
    • Hop resistance in the beer spoilage bacterium Lactobacillus brevis is mediated by the ATP-binding cassette multidrug transporter HorA
    • Sakamoto, K., A. Margolles, H. W. van Veen, and W. N. Konings. 2001. Hop resistance in the beer spoilage bacterium Lactobacillus brevis is mediated by the ATP-binding cassette multidrug transporter HorA. J. Bacteriol. 183: 5371-5375.
    • (2001) J. Bacteriol , vol.183 , pp. 5371-5375
    • Sakamoto, K.1    Margolles, A.2    van Veen, H.W.3    Konings, W.N.4
  • 25
    • 0035326344 scopus 로고    scopus 로고
    • Charting the proteomes of organisms with unsequenced genomes by MALD1-quadrupole time-of-flight mass spectrometry and BLAST homology searching
    • Shevchenko, A., S. Sunyaev, A. Loboda, P. Bork, W. Ens, and K. G. Standing. 2001. Charting the proteomes of organisms with unsequenced genomes by MALD1-quadrupole time-of-flight mass spectrometry and BLAST homology searching. Anal. Chem. 73:1917-1926.
    • (2001) Anal. Chem , vol.73 , pp. 1917-1926
    • Shevchenko, A.1    Sunyaev, S.2    Loboda, A.3    Bork, P.4    Ens, W.5    Standing, K.G.6
  • 26
    • 84987341351 scopus 로고
    • Studies on the sensitivity of lactic acid bacteria to hop bitter acids
    • Simpson, W. J. 1993. Studies on the sensitivity of lactic acid bacteria to hop bitter acids. J. Inst. Brew 99:405-411.
    • (1993) J. Inst. Brew , vol.99 , pp. 405-411
    • Simpson, W.J.1
  • 27
    • 0026541449 scopus 로고
    • Selection of beer-spoilage lactic acid bacteria and induction of their ability to grow in beer
    • Simpson, W. J., and J. L. Fernandez. 1992. Selection of beer-spoilage lactic acid bacteria and induction of their ability to grow in beer. Lett. Appl. Microbiol. 14:13-16.
    • (1992) Lett. Appl. Microbiol , vol.14 , pp. 13-16
    • Simpson, W.J.1    Fernandez, J.L.2
  • 28
    • 0015813653 scopus 로고
    • Control of metabolite secretion in Bacillus subtilis
    • Speck, E. L., and E. Freese. 1973. Control of metabolite secretion in Bacillus subtilis. J. Gen. Microbiol. 78:261-275.
    • (1973) J. Gen. Microbiol , vol.78 , pp. 261-275
    • Speck, E.L.1    Freese, E.2
  • 29
    • 0027253971 scopus 로고
    • Utilisation of maltose and glucose by lactobacilli isolated from sourdough
    • Stolz, P., G. Bocker, R. F. Vogel, and W. P. Hammes. 1993. Utilisation of maltose and glucose by lactobacilli isolated from sourdough. FEMS Microbiol. Lett. 109:237-242.
    • (1993) FEMS Microbiol. Lett , vol.109 , pp. 237-242
    • Stolz, P.1    Bocker, G.2    Vogel, R.F.3    Hammes, W.P.4
  • 30
    • 4444307127 scopus 로고    scopus 로고
    • Comparative analysis of conserved genetic markers and adjacent DNA regions identified in beer-spoilage lactic acid bacteria
    • Suzuki, K., K. Ozaki, and H. Yamashita. 2004. Comparative analysis of conserved genetic markers and adjacent DNA regions identified in beer-spoilage lactic acid bacteria. Lett. Appl. Microbiol. 39:240-245.
    • (2004) Lett. Appl. Microbiol , vol.39 , pp. 240-245
    • Suzuki, K.1    Ozaki, K.2    Yamashita, H.3
  • 31
    • 0030959279 scopus 로고    scopus 로고
    • Sequence database searches via de novo peptide sequencing by tandem mass spectrometry
    • Taylor, J. A., and R. S. Johnson. 1997. Sequence database searches via de novo peptide sequencing by tandem mass spectrometry. Rapid Commun. Mass Spectrom. 11:1067-1075.
    • (1997) Rapid Commun. Mass Spectrom , vol.11 , pp. 1067-1075
    • Taylor, J.A.1    Johnson, R.S.2
  • 32
    • 0037974543 scopus 로고    scopus 로고
    • Stability and oligomerization of recombinant GadX, a transcriptional activator of the Escherichia coli glutamate decarboxylase system
    • Tramonti, A., M. De Canio, F. Bossa, and D. De Biase. 2003. Stability and oligomerization of recombinant GadX, a transcriptional activator of the Escherichia coli glutamate decarboxylase system. Biochim. Biophys. Acta 1647:376-380.
    • (2003) Biochim. Biophys. Acta , vol.1647 , pp. 376-380
    • Tramonti, A.1    De Canio, M.2    Bossa, F.3    De Biase, D.4
  • 33
    • 0037867770 scopus 로고    scopus 로고
    • Imidazole ring-opened DNA purines and their biological significance
    • Tudek, B. 2003. Imidazole ring-opened DNA purines and their biological significance. J. Biochem. Mol. Biol. 36:12-19.
    • (2003) J. Biochem. Mol. Biol , vol.36 , pp. 12-19
    • Tudek, B.1
  • 34
    • 0028979581 scopus 로고
    • Repair, refold, recycle: How bacteria can deal with spontaneous and environmental damage to proteins
    • Visick, J. E., and S. Clarke. 1995. Repair, refold, recycle: how bacteria can deal with spontaneous and environmental damage to proteins. Mol. Microbiol. 16:835-845.
    • (1995) Mol. Microbiol , vol.16 , pp. 835-845
    • Visick, J.E.1    Clarke, S.2
  • 35
    • 0029644596 scopus 로고
    • Method to correlate tandem mass spectra of modified peptides to amino acid sequences in the protein database
    • Yates, J. R., III, J. K. Eng, A. L. McCormack, and D. Schieltz. 1995. Method to correlate tandem mass spectra of modified peptides to amino acid sequences in the protein database. Anal. Chem. 67:1426-1436.
    • (1995) Anal. Chem , vol.67 , pp. 1426-1436
    • Yates III, J.R.1    Eng, J.K.2    McCormack, A.L.3    Schieltz, D.4
  • 36
    • 0027450059 scopus 로고
    • Cysteine desulfurase activity indicates a role for N1FS in metallocluster biosynthesis
    • Zheng, L., R. H. White, V. L. Cash, R. F. Jack, and D. R. Dean. 1993. Cysteine desulfurase activity indicates a role for N1FS in metallocluster biosynthesis. Proc. Natl. Acad. Sci. USA 90:2754-2758.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 2754-2758
    • Zheng, L.1    White, R.H.2    Cash, V.L.3    Jack, R.F.4    Dean, D.R.5
  • 37
    • 4444282445 scopus 로고    scopus 로고
    • Shotgun proteomics of Methanococcus jannaschii and insights into methanogenesis
    • Zhu, W., C. I. Reich, G. J. Olsen, C. S. Giometti, and J. R. Yates III. 2004. Shotgun proteomics of Methanococcus jannaschii and insights into methanogenesis. J. Proteome Res. 3:538-548.
    • (2004) J. Proteome Res , vol.3 , pp. 538-548
    • Zhu, W.1    Reich, C.I.2    Olsen, G.J.3    Giometti, C.S.4    Yates III, J.R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.