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Volumn 12, Issue 5, 2013, Pages 1363-1376

The metabolic regulation of sporulation and parasporal crystal formation in Bacillus thuringiensis revealed by transcriptomics and proteomics

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; BACTERIAL ENZYME; CARBON; CYTOCHROME; GLUCONIC ACID; POLY(3 HYDROXYBUTYRIC ACID); TRICARBOXYLIC ACID;

EID: 84877588295     PISSN: 15359476     EISSN: 15359484     Source Type: Journal    
DOI: 10.1074/mcp.M112.023986     Document Type: Article
Times cited : (82)

References (73)
  • 3
    • 77957584698 scopus 로고    scopus 로고
    • Bacillus thuringiensis: A genomics and proteomics perspective
    • Ibrahim, M. A., Griko, N., Junker, M., and Lee, A. (2010) Bacillus thuringiensis: A genomics and proteomics perspective. Bioeng. Bugs 1, 31-50
    • (2010) Bioeng. Bugs , vol.1 , pp. 31-50
    • Ibrahim, M.A.1    Griko, N.2    Junker, M.3    Lee, A.4
  • 4
    • 64049085020 scopus 로고    scopus 로고
    • Insecticidal activity of Bacillus thuringiensis crystal proteins
    • van Frankenhuyzen, K. (2009) Insecticidal activity of Bacillus thuringiensis crystal proteins. J. Invertebr. Pathol. 101, 1-16
    • (2009) J. Invertebr. Pathol. , vol.101 , pp. 1-16
    • Van Frankenhuyzen, K.1
  • 5
    • 79952350102 scopus 로고    scopus 로고
    • Bacillus thuringiensis: A century of research, development and commercial applications
    • Sanahuja, G., Banakar, R., Twyman, R. M., Capell, T., and Christou, P. (2011) Bacillus thuringiensis: a century of research, development and commercial applications. Plant Biotechnol. J. 9, 283-300
    • (2011) Plant Biotechnol. J. , vol.9 , pp. 283-300
    • Sanahuja, G.1    Banakar, R.2    Twyman, R.M.3    Capell, T.4    Christou, P.5
  • 7
    • 0033985114 scopus 로고    scopus 로고
    • Regulation by overlapping promoters of the rate of synthesis and deposition into crystalline inclusions of Bacillus thuringiensis delta- endotoxins
    • DOI 10.1128/JB.182.3.734-741.2000
    • Sedlak, M., Walter, T., and Aronson, A. (2000) Regulation by overlapping promoters of the rate of synthesis and deposition into crystalline inclusions of Bacillus thuringiensis delta-endotoxins. J. Bacteriol. 182, 734-741 (Pubitemid 30054005)
    • (2000) Journal of Bacteriology , vol.182 , Issue.3 , pp. 734-741
    • Sedlak, M.1    Walter, T.2    Aronson, A.3
  • 8
    • 0033583174 scopus 로고    scopus 로고
    • Specific binding of the E2 subunit of pyruvate dehydrogenase to the upstream region of Bacillus thuringiensis protoxin genes
    • Walter, T., and Aronson, A. (1999) Specific binding of the E2 subunit of pyruvate dehydrogenase to the upstream region of Bacillus thuringiensis protoxin genes. J. Biol. Chem. 274, 7901-7906
    • (1999) J. Biol. Chem. , vol.274 , pp. 7901-7906
    • Walter, T.1    Aronson, A.2
  • 9
    • 0029947261 scopus 로고    scopus 로고
    • STAB-SD: A Shine-Dalgarno sequence in the 5′ untranslated region is a determinant of mRNA stability
    • Agaisse, H., and Lereclus, D. (1996) STAB-SD: a Shine-Dalgarno sequence in the 5′ untranslated region is a determinant of mRNA stability. Mol. Microbiol. 20, 633-643
    • (1996) Mol. Microbiol. , vol.20 , pp. 633-643
    • Agaisse, H.1    Lereclus, D.2
  • 10
    • 0028840871 scopus 로고
    • Regulation of insecticidal crystal protein production in Bacillus thuringiensis
    • Baum, J. A., and Malvar, T. (1995) Regulation of insecticidal crystal protein production in Bacillus thuringiensis. Mol. Microbiol. 18, 1-12
    • (1995) Mol. Microbiol. , vol.18 , pp. 1-12
    • Baum, J.A.1    Malvar, T.2
  • 11
    • 79959329680 scopus 로고    scopus 로고
    • Complete genome sequence of Bacillus thuringiensis subsp. chinensis strain CT-43
    • He, J., Wang, J., Yin, W., Shao, X., Zheng, H., Li, M., Zhao, Y., Sun, M., Wang, S., and Yu, Z. (2011) Complete genome sequence of Bacillus thuringiensis subsp. chinensis strain CT-43. J. Bacteriol. 193, 3407-3408
    • (2011) J. Bacteriol. , vol.193 , pp. 3407-3408
    • He, J.1    Wang, J.2    Yin, W.3    Shao, X.4    Zheng, H.5    Li, M.6    Zhao, Y.7    Sun, M.8    Wang, S.9    Yu, Z.10
  • 12
    • 0016158504 scopus 로고
    • Physiology of sporeforming bacteria associated with insects: Radiorespirometric survey of carbohydrate metabolism in the 12 serotypes of Bacillus thuringiensis
    • Nickerson, K. W., St Julian, G., and Bulla, L. A. Jr. (1974) Physiology of sporeforming bacteria associated with insects: radiorespirometric survey of carbohydrate metabolism in the 12 serotypes of Bacillus thuringiensis. Appl. Microbiol. 28, 129-132
    • (1974) Appl. Microbiol. , vol.28 , pp. 129-132
    • Nickerson, K.W.1    St Julian, G.2    Bulla Jr., L.A.3
  • 14
    • 46249106990 scopus 로고    scopus 로고
    • Mapping and quantifying mammalian transcriptomes by RNA-Seq
    • DOI 10.1038/nmeth.1226, PII NMETH.1226
    • Mortazavi, A., Williams, B. A., McCue, K., Schaeffer, L., and Wold, B. (2008) Mapping and quantifying mammalian transcriptomes by RNA-Seq. Nat. Methods 5, 621-628 (Pubitemid 351911867)
    • (2008) Nature Methods , vol.5 , Issue.7 , pp. 621-628
    • Mortazavi, A.1    Williams, B.A.2    McCue, K.3    Schaeffer, L.4    Wold, B.5
  • 15
    • 75249095274 scopus 로고    scopus 로고
    • DEGseq: An R package for identifying differentially expressed genes from RNA-seq data
    • Wang, L., Feng, Z., Wang, X., Wang, X., and Zhang, X. (2010) DEGseq: an R package for identifying differentially expressed genes from RNA-seq data. Bioinformatics 26, 136-138
    • (2010) Bioinformatics , vol.26 , pp. 136-138
    • Wang, L.1    Feng, Z.2    Wang, X.3    Wang, X.4    Zhang, X.5
  • 16
    • 33847340190 scopus 로고    scopus 로고
    • Technical, experimental, and biological variations in isobaric tags for relative and absolute quantitation (iTRAQ)
    • Gan, C. S., Chong, P. K., Pham, T. K., and Wright, P. C. (2007) Technical, experimental, and biological variations in isobaric tags for relative and absolute quantitation (iTRAQ). J. Proteome Res. 6, 821-827
    • (2007) J. Proteome Res. , vol.6 , pp. 821-827
    • Gan, C.S.1    Chong, P.K.2    Pham, T.K.3    Wright, P.C.4
  • 18
    • 84865825138 scopus 로고    scopus 로고
    • Proteomic analysis reveals resistance mechanism against biofuel hexane in Synechocystis sp. PCC 6803
    • Liu, J., Chen, L., Wang, J., Qiao, J., and Zhang, W. (2012) Proteomic analysis reveals resistance mechanism against biofuel hexane in Synechocystis sp. PCC 6803. Biotechnol. Biofuels e5, 68
    • (2012) Biotechnol. Biofuels , vol.E5 , pp. 68
    • Liu, J.1    Chen, L.2    Wang, J.3    Qiao, J.4    Zhang, W.5
  • 19
    • 84874091750 scopus 로고    scopus 로고
    • Proteomic analysis of temporally stimulated ovarian cancer cells for biomarker discovery
    • Marzinke, M. A., Choi, C. H., Chen, L., Shih, I. M., Chan, D. W., and Zhang, H. (2012) Proteomic analysis of temporally stimulated ovarian cancer cells for biomarker discovery. Mol. Cell. Proteomics 12, 356-368
    • (2012) Mol. Cell. Proteomics , vol.12 , pp. 356-368
    • Marzinke, M.A.1    Choi, C.H.2    Chen, L.3    Shih, I.M.4    Chan, D.W.5    Zhang, H.6
  • 21
    • 84864723032 scopus 로고    scopus 로고
    • Delayed protein synthesis reduces the correlation between mRNA and protein fluctuations
    • Gedeon, T., and Bokes, P. (2012) Delayed protein synthesis reduces the correlation between mRNA and protein fluctuations. Biophys. J. 103, 377-385
    • (2012) Biophys. J. , vol.103 , pp. 377-385
    • Gedeon, T.1    Bokes, P.2
  • 22
    • 0036545614 scopus 로고    scopus 로고
    • Complementary profiling of gene expression at the transcriptome and proteome levels in Saccharomyces cerevisiae
    • Griffin, T. J., Gygi, S. P., Ideker, T., Rist, B., Eng, J., Hood, L., and Aebersold, R. (2002) Complementary profiling of gene expression at the transcriptome and proteome levels in Saccharomyces cerevisiae. Mol. Cell. Proteomics 1, 323-333
    • (2002) Mol. Cell. Proteomics , vol.1 , pp. 323-333
    • Griffin, T.J.1    Gygi, S.P.2    Ideker, T.3    Rist, B.4    Eng, J.5    Hood, L.6    Aebersold, R.7
  • 23
    • 84855887936 scopus 로고    scopus 로고
    • Comparative proteomic analysis revealed metabolic changes and the translational regulation of Cry protein synthesis in Bacillus thuringiensis
    • Gong, Y., Li, M., Xu, D., Wang, H., He, J., Wu, D., Chen, D., Qiu, N., Bao, Q., Sun, M., and Yu, Z. (2012) Comparative proteomic analysis revealed metabolic changes and the translational regulation of Cry protein synthesis in Bacillus thuringiensis. J. Proteomics 75, 1235-1246
    • (2012) J. Proteomics , vol.75 , pp. 1235-1246
    • Gong, Y.1    Li, M.2    Xu, D.3    Wang, H.4    He, J.5    Wu, D.6    Chen, D.7    Qiu, N.8    Bao, Q.9    Sun, M.10    Yu, Z.11
  • 24
    • 0008792675 scopus 로고
    • Protein turnover and the formation of protein inclusions during sporulation of Bacillus thuringiensis
    • Monro, R. E. (1961) Protein turnover and the formation of protein inclusions during sporulation of Bacillus thuringiensis. Biochem. J. 81, 225-232
    • (1961) Biochem. J. , vol.81 , pp. 225-232
    • Monro, R.E.1
  • 25
    • 0042366189 scopus 로고    scopus 로고
    • Cannibalism by sporulating bacteria
    • DOI 10.1126/science.1086462
    • González-Pastor, J. E., Hobbs, E. C., and Losick, R. (2003) Cannibalism by sporulating bacteria. Science 301, 510-513 (Pubitemid 36900307)
    • (2003) Science , vol.301 , Issue.5632 , pp. 510-513
    • Gonzalez-Pastor, J.E.1    Hobbs, E.C.2    Losick, R.3
  • 26
    • 79953323267 scopus 로고    scopus 로고
    • Cannibalism: A social behavior in sporulating Bacillus subtilis
    • González-Pastor, J. E. (2011) Cannibalism: a social behavior in sporulating Bacillus subtilis. FEMS Microbiol. Rev. 35, 415-424
    • (2011) FEMS Microbiol. Rev. , vol.35 , pp. 415-424
    • González-Pastor, J.E.1
  • 27
    • 51549089016 scopus 로고    scopus 로고
    • Molecular mechanisms underlying the positive stringent response of the Bacillus subtilis ilv-leu operon, involved in the biosynthesis of branchedchain amino acids
    • Tojo, S., Satomura, T., Kumamoto, K., Hirooka, K., and Fujita, Y. (2008) Molecular mechanisms underlying the positive stringent response of the Bacillus subtilis ilv-leu operon, involved in the biosynthesis of branchedchain amino acids. J. Bacteriol. 190, 6134-6147
    • (2008) J. Bacteriol. , vol.190 , pp. 6134-6147
    • Tojo, S.1    Satomura, T.2    Kumamoto, K.3    Hirooka, K.4    Fujita, Y.5
  • 28
    • 0032965169 scopus 로고    scopus 로고
    • Regulation of expression of the Lactococcus lactis histidine operon
    • Delorme, C., Ehrlich, S. D., and Renault, P. (1999) Regulation of expression of the Lactococcus lactis histidine operon. J. Bacteriol. 181, 2026-2037 (Pubitemid 29164954)
    • (1999) Journal of Bacteriology , vol.181 , Issue.7 , pp. 2026-2037
    • Delorme, C.1    Ehrlich, S.D.2    Renault, P.3
  • 29
    • 47749143603 scopus 로고    scopus 로고
    • Role of Bacillus subtilis RNase J1 endonuclease and 5′-exonuclease activities in trp leader RNA turnover
    • Deikus, G., Condon, C., and Bechhofer, D. H. (2008) Role of Bacillus subtilis RNase J1 endonuclease and 5′-exonuclease activities in trp leader RNA turnover. J. Biol. Chem. 283, 17158-17167
    • (2008) J. Biol. Chem. , vol.283 , pp. 17158-17167
    • Deikus, G.1    Condon, C.2    Bechhofer, D.H.3
  • 30
    • 33846942977 scopus 로고    scopus 로고
    • Clp ATPases and ClpP proteolytic complexes regulate vital biological processes in low GC, Gram-positive bacteria
    • Frees, D., Savijoki, K., Varmanen, P., and Ingmer, H. (2007) Clp ATPases and ClpP proteolytic complexes regulate vital biological processes in low GC, Gram-positive bacteria. Mol. Microbiol. 63, 1285-1295
    • (2007) Mol. Microbiol. , vol.63 , pp. 1285-1295
    • Frees, D.1    Savijoki, K.2    Varmanen, P.3    Ingmer, H.4
  • 31
    • 72049104795 scopus 로고    scopus 로고
    • Chaperone-protease systems in regulation and protein quality control in Bacillus subtilis
    • Molière, N., and Turgay, K. (2009) Chaperone-protease systems in regulation and protein quality control in Bacillus subtilis. Res. Microbiol. 160, 637-644
    • (2009) Res. Microbiol. , vol.160 , pp. 637-644
    • Molière, N.1    Turgay, K.2
  • 32
    • 67650708257 scopus 로고    scopus 로고
    • Cloning of feather-degrading minor extracellular protease from Bacillus cereus DCUW: Dissection of the structural domains
    • Ghosh, A., Chakrabarti, K., and Chattopadhyay, D. (2009) Cloning of feather-degrading minor extracellular protease from Bacillus cereus DCUW: dissection of the structural domains. Microbiology 155, 2049-2057
    • (2009) Microbiology , vol.155 , pp. 2049-2057
    • Ghosh, A.1    Chakrabarti, K.2    Chattopadhyay, D.3
  • 33
    • 0031992963 scopus 로고    scopus 로고
    • A Cysteine-Dependent Serine Protease Associated with the Dormant Spores of Bacillus cereus: Purification of the Protein and Cloning of the Corresponding Gene
    • Moriyama, R., Sugimoto, K., Zhang, H., Inoue, T., and Makino, S. (1998) A cysteine-dependent serine protease associated with the dormant spores of Bacillus cereus: purification of the protein and cloning of the corresponding gene. Biosci. Biotechnol. Biochem. 62, 268-274 (Pubitemid 128475050)
    • (1998) Bioscience, Biotechnology and Biochemistry , vol.62 , Issue.2 , pp. 268-274
    • Moriyama, R.1    Sugimoto, K.2    Zhang, H.3    Inoue, T.4    Makino, S.5
  • 34
    • 17144382779 scopus 로고    scopus 로고
    • Bacillolysin MA, a novel bacterial metalloproteinase that produces angiostatin-like fragments from plasminogen and activates protease zymogens in the coagulation and fibrinolysis systems
    • DOI 10.1074/jbc.M500241200
    • Narasaki, R., Kuribayashi, H., Shimizu, K., Imamura, D., Sato, T., and Hasumi, K. (2005) Bacillolysin MA, a novel bacterial metalloproteinase that produces angiostatin-like fragments from plasminogen and activates protease zymogens in the coagulation and fibrinolysis systems. J. Biol. Chem. 280, 14278-14287 (Pubitemid 40517330)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.14 , pp. 14278-14287
    • Narasaki, R.1    Kuribayashi, H.2    Shimizu, K.3    Imamura, D.4    Sato, T.5    Hasumi, K.6
  • 35
    • 77956184729 scopus 로고    scopus 로고
    • Isolation, characterization and biological role of camelysin from Bacillus thuringiensis subsp. israelensis
    • Nisnevitch, M., Sigawi, S., Cahan, R., and Nitzan, Y. (2010) Isolation, characterization and biological role of camelysin from Bacillus thuringiensis subsp. israelensis. Curr. Microbiol. 61, 176-183
    • (2010) Curr. Microbiol. , vol.61 , pp. 176-183
    • Nisnevitch, M.1    Sigawi, S.2    Cahan, R.3    Nitzan, Y.4
  • 36
    • 33646449949 scopus 로고    scopus 로고
    • Relationship between poly-beta-hydroxybutyrate production and deltaendotoxin for Bacillus thuringiensis var. kurstaki
    • Navarro, A. K., Farrera, R. R., Lüpez, R., and Pérez-Guevara, F. (2006) Relationship between poly-beta-hydroxybutyrate production and deltaendotoxin for Bacillus thuringiensis var. kurstaki. Biotechnol. Lett. 28, 641-644
    • (2006) Biotechnol. Lett. , vol.28 , pp. 641-644
    • Navarro, A.K.1    Farrera, R.R.2    Lüpez, R.3    Pérez-Guevara, F.4
  • 37
    • 33750464109 scopus 로고    scopus 로고
    • Identification and characterization of the Bacillus thuringiensis phaZ gene, encoding new intracellular poly-3-hydroxybutyrate depolymerase
    • Tseng, C. L., Chen, H. J., and Shaw, G. C. (2006) Identification and characterization of the Bacillus thuringiensis phaZ gene, encoding new intracellular poly-3-hydroxybutyrate depolymerase. J. Bacteriol. 188, 7592-7599
    • (2006) J. Bacteriol. , vol.188 , pp. 7592-7599
    • Tseng, C.L.1    Chen, H.J.2    Shaw, G.C.3
  • 38
    • 79959716368 scopus 로고    scopus 로고
    • Proteomic analysis reveals the strategies of Bacillus thuringiensis YBT-1520 for survival under long-term heat stress
    • Wu, D., He, J., Gong, Y., Chen, D., Zhu, X., Qiu, N., Sun, M., Li, M., and Yu, Z. (2011) Proteomic analysis reveals the strategies of Bacillus thuringiensis YBT-1520 for survival under long-term heat stress. Proteomics 11, 2580-2591
    • (2011) Proteomics , vol.11 , pp. 2580-2591
    • Wu, D.1    He, J.2    Gong, Y.3    Chen, D.4    Zhu, X.5    Qiu, N.6    Sun, M.7    Li, M.8    Yu, Z.9
  • 39
    • 0034607367 scopus 로고    scopus 로고
    • Characterization study of the sporulation kinetics of Bacillus thuringiensis
    • Liu, B. L., and Tzeng, Y. M. (2000) Characterization study of the sporulation kinetics of Bacillus thuringiensis. Biotechnol. Bioeng. 68, 11-17
    • (2000) Biotechnol. Bioeng. , vol.68 , pp. 11-17
    • Liu, B.L.1    Tzeng, Y.M.2
  • 40
    • 84865532861 scopus 로고    scopus 로고
    • Proteomic analysis of Bacillus thuringiensis ΔphaC mutant BMB171/PHB(-1) reveals that the PHB synthetic pathway warrants normal carbon metabolism
    • Chen, D., Xu, D., Li, M., He, J., Gong, Y., Wu, D., Sun, M., and Yu, Z. (2012) Proteomic analysis of Bacillus thuringiensis ΔphaC mutant BMB171/PHB(-1) reveals that the PHB synthetic pathway warrants normal carbon metabolism. J. Proteomics 75, 5176-5188
    • (2012) J. Proteomics , vol.75 , pp. 5176-5188
    • Chen, D.1    Xu, D.2    Li, M.3    He, J.4    Gong, Y.5    Wu, D.6    Sun, M.7    Yu, Z.8
  • 41
    • 73049149853 scopus 로고
    • Assay of poly-beta-hydroxybutyric acid
    • Law, J. H., and Slepecky, R. A. (1961) Assay of poly-beta-hydroxybutyric acid. J. Bacteriol. 82, 33-36
    • (1961) J. Bacteriol. , vol.82 , pp. 33-36
    • Law, J.H.1    Slepecky, R.A.2
  • 42
    • 0035110760 scopus 로고    scopus 로고
    • Control of hemA expression in Rhodobacter sphaeroides 2.4.1: Effect of a transposon insertion in the hbdA gene
    • DOI 10.1128/JB.183.5.1568-1576.2001
    • Fales, L., Kryszak, L., and Zeilstra-Ryalls, J. (2001) Control of hemA expression in Rhodobacter sphaeroides 2.4.1: effect of a transposon insertion in the hbdA gene. J. Bacteriol. 183, 1568-1576 (Pubitemid 32172299)
    • (2001) Journal of Bacteriology , vol.183 , Issue.5 , pp. 1568-1576
    • Fales, L.1    Kryszak, L.2    Zeilstra-Ryalls, J.3
  • 43
    • 34250166461 scopus 로고    scopus 로고
    • Acetoin metabolism in bacteria
    • DOI 10.1080/10408410701364604, PII 779367204
    • Xiao, Z., and Xu, P. (2007) Acetoin metabolism in bacteria. Crit. Rev. Microbiol. 33, 127-140 (Pubitemid 46897713)
    • (2007) Critical Reviews in Microbiology , vol.33 , Issue.2 , pp. 127-140
    • Xiao, Z.1    Xu, P.2
  • 44
    • 0027167447 scopus 로고
    • Regulation of the Bacillus subtilis alsS, alsD, and alsR genes involved in post-exponential-phase production of acetoin
    • Renna, M. C., Najimudin, N., Winik, L. R., and Zahler, S. A. (1993) Regulation of the Bacillus subtilis alsS, alsD, and alsR genes involved in post-exponentialphase production of acetoin. J. Bacteriol. 175, 3863-3875 (Pubitemid 23173348)
    • (1993) Journal of Bacteriology , vol.175 , Issue.12 , pp. 3863-3875
    • Renna, M.C.1    Najimudin, N.2    Winik, L.R.3    Zahler, S.A.4
  • 45
    • 0027497020 scopus 로고
    • Identification of genes involved in utilization of acetate and acetoin in Bacillus subtilis
    • DOI 10.1111/j.1365-2958.1993.tb01952.x
    • Grundy, F. J., Waters, D. A., Takova, T. Y., and Henkin, T. M. (1993) Identification of genes involved in utilization of acetate and acetoin in Bacillus subtilis. Mol. Microbiol. 10, 259-271 (Pubitemid 23316736)
    • (1993) Molecular Microbiology , vol.10 , Issue.2 , pp. 259-271
    • Grundy, F.J.1    Waters, D.A.2    Takova, T.Y.3    Henkin, T.M.4
  • 46
    • 0033797251 scopus 로고    scopus 로고
    • An operon for a putative ATP-binding cassette transport system involved in acetoin utilization of Bacillus subtilis
    • Yoshida, K. I., Fujita, Y., and Ehrlich, S. D. (2000) An operon for a putative ATP-binding cassette transport system involved in acetoin utilization of Bacillus subtilis. J. Bacteriol. 182, 5454-5461
    • (2000) J. Bacteriol. , vol.182 , pp. 5454-5461
    • Yoshida, K.I.1    Fujita, Y.2    Ehrlich, S.D.3
  • 47
    • 0033055035 scopus 로고    scopus 로고
    • Biochemical and molecular characterization of the Bacillus subtilis acetoin catabolic pathway
    • Huang, M., Oppermann-Sanio, F. B., and Steinbüchel, A. (1999) Biochemical and molecular characterization of the Bacillus subtilis acetoin catabolic pathway. J. Bacteriol. 181, 3837-3841 (Pubitemid 29283815)
    • (1999) Journal of Bacteriology , vol.181 , Issue.12 , pp. 3837-3841
    • Huang, M.1    Oppermann-Sanio, F.B.2    Steinbuchel, A.3
  • 48
    • 0028157328 scopus 로고
    • Identification and molecular characterization of the aco genes encoding the Pelobacter carbinolicus acetoin dehydrogenase enzyme system
    • Oppermann, F. B., and Steinbüchel, A. (1994) Identification and molecular characterization of the aco genes encoding the Pelobacter carbinolicus acetoin dehydrogenase enzyme system. J. Bacteriol. 176, 469-485 (Pubitemid 24034066)
    • (1994) Journal of Bacteriology , vol.176 , Issue.2 , pp. 469-485
    • Oppermann, F.B.1    Steinbuchel, A.2
  • 49
    • 0033113677 scopus 로고    scopus 로고
    • Properties of maltose-inducible alpha-glucosidase MalL (sucrase-isomaltase-maltase) in Bacillus subtilis: Evidence for its contribution to maltodextrin utilization
    • Schönert, S., Buder, T., and Dahl, M. K. (1999) Properties of maltose-inducible alpha-glucosidase MalL (sucrase-isomaltase-maltase) in Bacillus subtilis: evidence for its contribution to maltodextrin utilization. Res. Microbiol. 150, 167-177 (Pubitemid 129673069)
    • (1999) Research in Microbiology , vol.150 , Issue.3 , pp. 167-177
    • Schonert, S.1    Buder, T.2    Dahl, M.K.3
  • 50
    • 34548287921 scopus 로고    scopus 로고
    • Mechanism of GlvA from Bacillus subtilis: A detailed kinetic analysis of a 6-phospho-alpha-glucosidase from glycoside hydrolase family 4
    • DOI 10.1021/bi700536p
    • Yip, V. L., Thompson, J., and Withers, S. G. (2007) Mechanism of GlvA from Bacillus subtilis: a detailed kinetic analysis of a 6-phospho-alpha- glucosidase from glycoside hydrolase family 4. Biochemistry 46, 9840-9852 (Pubitemid 47328590)
    • (2007) Biochemistry , vol.46 , Issue.34 , pp. 9840-9852
    • Yip, V.L.Y.1    Thompson, J.2    Withers, S.G.3
  • 51
    • 0028915966 scopus 로고
    • Krebs cycle function is required for activation of the Spo0A transcription factor in Bacillus subtilis
    • Ireton, K., Jin, S., Grossman, A. D., and Sonenshein, A. L. (1995) Krebs cycle function is required for activation of the Spo0A transcription factor in Bacillus subtilis. Proc. Natl. Acad. Sci. U.S.A. 92, 2845-2849
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 2845-2849
    • Ireton, K.1    Jin, S.2    Grossman, A.D.3    Sonenshein, A.L.4
  • 53
    • 0023368843 scopus 로고
    • The gluconate operon gnt of Bacillus subtilis encodes its own transcriptional negative regulator
    • Fujita, Y., and Fujita, T. (1987) The gluconate operon gnt of Bacillus subtilis encodes its own transcriptional negative regulator. Proc. Natl. Acad. Sci. U.S.A. 84, 4524-4528
    • (1987) Proc. Natl. Acad. Sci. U.S.A. , vol.84 , pp. 4524-4528
    • Fujita, Y.1    Fujita, T.2
  • 54
    • 77957814635 scopus 로고    scopus 로고
    • Crystal structures of Bacillus cereus NCTU2 chitinase complexes with chitooligomers reveal novel substrate binding for catalysis: A chitinase without chitin binding and insertion domains
    • Hsieh, Y. C., Wu, Y. J., Chiang, T. Y., Kuo, C. Y., Shrestha, K. L., Chao, C. F., Huang, Y. C., Chuankhayan, P., Wu, W. G., Li, Y. K., and Chen, C. J. (2010) Crystal structures of Bacillus cereus NCTU2 chitinase complexes with chitooligomers reveal novel substrate binding for catalysis: a chitinase without chitin binding and insertion domains. J. Biol. Chem. 285, 31603-31615
    • (2010) J. Biol. Chem. , vol.285 , pp. 31603-31615
    • Hsieh, Y.C.1    Wu, Y.J.2    Chiang, T.Y.3    Kuo, C.Y.4    Shrestha, K.L.5    Chao, C.F.6    Huang, Y.C.7    Chuankhayan, P.8    Wu, W.G.9    Li, Y.K.10    Chen, C.J.11
  • 55
    • 83155163749 scopus 로고    scopus 로고
    • Functional analyses of multiple lichenin-degrading enzymes from the rumen bacterium Ruminococcus albus 8
    • Iakiviak, M., Mackie, R. I., and Cann, I. K. (2011) Functional analyses of multiple lichenin-degrading enzymes from the rumen bacterium Ruminococcus albus 8. Appl. Environ. Microbiol. 77, 7541-7550
    • (2011) Appl. Environ. Microbiol. , vol.77 , pp. 7541-7550
    • Iakiviak, M.1    Mackie, R.I.2    Cann, I.K.3
  • 57
    • 0032882589 scopus 로고    scopus 로고
    • Salmonella typhimurium LT2 catabolizes propionate via the 2-methylcitric acid cycle
    • Horswill, A. R., and Escalante-Semerena, J. C. (1999) Salmonella typhimurium LT2 catabolizes propionate via the 2-methylcitric acid cycle. J. Bacteriol. 181, 5615-5623 (Pubitemid 29437131)
    • (1999) Journal of Bacteriology , vol.181 , Issue.18 , pp. 5615-5623
    • Horswill, A.R.1    Escalante-Semerena, J.C.2
  • 58
    • 0027994424 scopus 로고
    • Identification of two distinct Bacillus subtilis citrate synthase genes
    • Jin, S., and Sonenshein, A. L. (1994) Identification of two distinct Bacillus subtilis citrate synthase genes. J. Bacteriol. 176, 4669-4679 (Pubitemid 24237972)
    • (1994) Journal of Bacteriology , vol.176 , Issue.15 , pp. 4669-4679
    • Jin, S.1    Sonenshein, A.L.2
  • 59
    • 0016840835 scopus 로고
    • Gamma-aminobutyric acid pathway and modified tricarboxylic acid cycle activity during growth and sporulation of Bacillus thuringiensis
    • Aronson, J. N., Borris, D. P., Doerner, J. F., and Akers, E. (1975) Gamma-aminobutyric acid pathway and modified tricarboxylic acid cycle activity during growth and sporulation of Bacillus thuringiensis. Appl. Microbiol. 30, 489-492
    • (1975) Appl. Microbiol. , vol.30 , pp. 489-492
    • Aronson, J.N.1    Borris, D.P.2    Doerner, J.F.3    Akers, E.4
  • 60
    • 55549091098 scopus 로고    scopus 로고
    • Atomic resolution structures of Escherichia coli and Bacillus anthracis malate synthase A: Comparison with isoform G and implications for structure-based drug discovery
    • Lohman, J. R., Olson, A. C., and Remington, S. J. (2008) Atomic resolution structures of Escherichia coli and Bacillus anthracis malate synthase A: comparison with isoform G and implications for structure-based drug discovery. Protein Sci. 17, 1935-1945
    • (2008) Protein Sci. , vol.17 , pp. 1935-1945
    • Lohman, J.R.1    Olson, A.C.2    Remington, S.J.3
  • 61
    • 73849114178 scopus 로고    scopus 로고
    • Structure and regulation of the gab gene cluster, involved in the gamma-aminobutyric acid shunt, are controlled by a sigma54 factor in Bacillus thuringiensis
    • Zhu, L., Peng, Q., Song, F., Jiang, Y., Sun, C., Zhang, J., and Huang, D. (2010) Structure and regulation of the gab gene cluster, involved in the gamma-aminobutyric acid shunt, are controlled by a sigma54 factor in Bacillus thuringiensis. J. Bacteriol. 192, 346-355
    • (2010) J. Bacteriol. , vol.192 , pp. 346-355
    • Zhu, L.1    Peng, Q.2    Song, F.3    Jiang, Y.4    Sun, C.5    Zhang, J.6    Huang, D.7
  • 62
    • 33748576606 scopus 로고    scopus 로고
    • Enhancement of gamma-aminobutyric acid production in Chungkukjang by applying a Bacillus subtilis strain expressing glutamate decarboxylase from Lactobacillus brevis
    • Park, K. B., and Oh, S. H. (2006) Enhancement of gamma-aminobutyric acid production in Chungkukjang by applying a Bacillus subtilis strain expressing glutamate decarboxylase from Lactobacillus brevis. Biotechnol. Lett. 28, 1459-1463
    • (2006) Biotechnol. Lett. , vol.28 , pp. 1459-1463
    • Park, K.B.1    Oh, S.H.2
  • 63
    • 0032464364 scopus 로고    scopus 로고
    • Mutational analysis of the TnrA-binding sites in the Bacillus subtilis nrgAB and gabP promoter regions
    • Wray, L.V. Jr., Zalieckas, J. M., Ferson, A. E., and Fisher, S. H. (1998) Mutational analysis of the TnrA-binding sites in the Bacillus subtilis nrgAB and gabP promoter regions. J. Bacteriol. 180, 2943-2949 (Pubitemid 29122124)
    • (1998) Journal of Bacteriology , vol.180 , Issue.11 , pp. 2943-2949
    • Wray Jr., L.V.1    Zalieckas, J.M.2    Ferson, A.E.3    Fisher, S.H.4
  • 64
    • 34250375658 scopus 로고    scopus 로고
    • Enzymology and evolution of the pyruvate pathway to 2-oxobutyrate in Methanocaldococcus jannaschii
    • DOI 10.1128/JB.00166-07
    • Drevland, R. M., Waheed, A., and Graham, D. E. (2007) Enzymology and evolution of the pyruvate pathway to 2-oxobutyrate in Methanocaldococcus jannaschii. J. Bacteriol. 189, 4391-4400 (Pubitemid 46919625)
    • (2007) Journal of Bacteriology , vol.189 , Issue.12 , pp. 4391-4400
    • Drevland, R.M.1    Waheed, A.2    Graham, D.E.3
  • 65
    • 0027515241 scopus 로고
    • 3-Isopropylmalate dehydrogenase from chemolithoautotroph Thiobacillus ferrooxidans: DNA sequence, enzyme purification, and characterization
    • Kawaguchi, H., Inagaki, K., Kuwata, Y., Tanaka, H., and Tano, T. (1993) 3-Isopropylmalate dehydrogenase from chemolithoautotroph Thiobacillus ferrooxidans: DNA sequence, enzyme purification, and characterization. J. Biochem. 114, 370-377 (Pubitemid 23285015)
    • (1993) Journal of Biochemistry , vol.114 , Issue.3 , pp. 370-377
    • Kawaguchi, H.1    Inagaki, K.2    Kuwata, Y.3    Tanaka, H.4    Tano, T.5
  • 66
    • 0032913240 scopus 로고    scopus 로고
    • Role of bkdR, a transcriptional activator of the SigL-dependent isoleucine and valine degradation pathway in Bacillus subtilis
    • Debarbouille, M., Gardan, R., Arnaud, M., and Rapoport, G. (1999) Role of bkdR, a transcriptional activator of the sigL-dependent isoleucine and valine degradation pathway in Bacillus subtilis. J. Bacteriol. 181, 2059-2066 (Pubitemid 29164958)
    • (1999) Journal of Bacteriology , vol.181 , Issue.7 , pp. 2059-2066
    • Debarbouille, M.1    Gardan, R.2    Arnaud, M.3    Rapoport, G.4
  • 67
    • 0026485287 scopus 로고
    • Carbon and energy metabolism of atp mutants of Escherichia coli
    • Jensen, P. R., and Michelsen, O. (1992) Carbon and energy metabolism of atp mutants of Escherichia coli. J. Bacteriol. 174, 7635-7641
    • (1992) J. Bacteriol. , vol.174 , pp. 7635-7641
    • Jensen, P.R.1    Michelsen, O.2
  • 68
  • 69
    • 80052068980 scopus 로고    scopus 로고
    • Structure of the membrane domain of respiratory complex I
    • Efremov, R. G., and Sazanov, L. A. (2011) Structure of the membrane domain of respiratory complex I. Nature 476, 414-420
    • (2011) Nature , vol.476 , pp. 414-420
    • Efremov, R.G.1    Sazanov, L.A.2
  • 70
    • 66349088622 scopus 로고    scopus 로고
    • Limited reversibility of transmembrane proton transfer assisting transmembrane electron transfer in a dihaem-containing succinate: Quinone oxidoreductase
    • Madej, M. G., Müller, F. G., Ploch, J., and Lancaster, C. R. (2009) Limited reversibility of transmembrane proton transfer assisting transmembrane electron transfer in a dihaem-containing succinate: quinone oxidoreductase. Biochim. Biophys. Acta 1787, 593-600
    • (2009) Biochim. Biophys. Acta , vol.1787 , pp. 593-600
    • Madej, M.G.1    Müller, F.G.2    Ploch, J.3    Lancaster, C.R.4
  • 71
    • 0034460089 scopus 로고    scopus 로고
    • 3 or cytochrome bd, is required for aerobic growth
    • DOI 10.1128/JB.182.23.6557-6564.2000
    • Winstedt, L., and von Wachenfeldt, C. (2000) Terminal oxidases of Bacillus subtilis strain 168: one quinol oxidase, cytochrome aa(3) or cytochrome bd, is required for aerobic growth. J. Bacteriol. 182, 6557-6564 (Pubitemid 32249233)
    • (2000) Journal of Bacteriology , vol.182 , Issue.23 , pp. 6557-6564
    • Winstedt, L.1    Von Wachenfeldt, C.2
  • 73
    • 0015349851 scopus 로고
    • Development of a membrane-bound resiratory system prior to and during sporulation in Bacillus cereus and its relationship to membrane structure
    • Lang, D. R., Felix, J., and Lundgren, D. G. (1972) Development of a membrane-bound resiratory system prior to and during sporulation in Bacillus cereus and its relationship to membrane structure. J. Bacteriol. 110, 968-977
    • (1972) J. Bacteriol. , vol.110 , pp. 968-977
    • Lang, D.R.1    Felix, J.2    Lundgren, D.G.3


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