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Volumn 8, Issue 1, 2019, Pages 70-81

Modular Pathway Engineering of Bacillus subtilis to Promote de Novo Biosynthesis of Menaquinone-7

Author keywords

Bacillus subtilis 168; glycerol metabolism pathway; menaquinone 7; methylerythritol phosphate (MEP) pathway; MK 7 biosynthesis pathway; modular pathway engineering; shikimate (SA) pathway

Indexed keywords

GLYCEROL; MENAQUINONE; MENAQUINONE 7; PHOSPHATE; SHIKIMIC ACID; UNCLASSIFIED DRUG; FARNOQUINONE; VITAMIN MK 7;

EID: 85060135976     PISSN: None     EISSN: 21615063     Source Type: Journal    
DOI: 10.1021/acssynbio.8b00258     Document Type: Article
Times cited : (59)

References (66)
  • 1
    • 45849118924 scopus 로고    scopus 로고
    • Metabolism and cell biology of vitamin K
    • Shearer, M. J. and Newman, P. (2008) Metabolism and cell biology of vitamin K. Thromb. Haemostasis 99, 530-547, 10.1160/TH08-03-0147
    • (2008) Thromb. Haemostasis , vol.99 , pp. 530-547
    • Shearer, M.J.1    Newman, P.2
  • 2
    • 77950354085 scopus 로고    scopus 로고
    • 2 biosynthesis promising drug targets?
    • 2 biosynthesis promising drug targets?. Molecules 15, 1531-1553, 10.3390/molecules15031531
    • (2010) Molecules , vol.15 , pp. 1531-1553
    • Kurosu, M.1    Begari, E.2
  • 3
    • 84859465580 scopus 로고    scopus 로고
    • Vitamin K: The effect on health beyond coagulation - An overview
    • Cees, V. (2012) Vitamin K: the effect on health beyond coagulation-an overview. Food Nutr. Res. 56, 77-81, 10.3402/fnr.v56i0.5329
    • (2012) Food Nutr. Res. , vol.56 , pp. 77-81
    • Cees, V.1
  • 4
    • 85047692812 scopus 로고
    • Vitamin K and vitamin K-dependent proteins
    • Shearer, M. J. (1990) Vitamin K and vitamin K-dependent proteins. Br. J. Haematol. 75, 156-162, 10.1111/j.1365-2141.1990.tb02642.x
    • (1990) Br. J. Haematol. , vol.75 , pp. 156-162
    • Shearer, M.J.1
  • 5
    • 84931864560 scopus 로고    scopus 로고
    • Vitamin K: An old vitamin in a new perspective
    • Grober, U., Reichrath, J., Holick, M. F., and Kisters, K. (2014) Vitamin K: an old vitamin in a new perspective. Derm.-Endocrinol. 6, e968490 10.4161/19381972.2014.968490
    • (2014) Derm.-Endocrinol. , vol.6 , pp. e968490
    • Grober, U.1    Reichrath, J.2    Holick, M.F.3    Kisters, K.4
  • 6
    • 0029133120 scopus 로고
    • Bioavailability of phylloquinone and menaquinones after oral and colorectal administration in vitamin K-deficient rats
    • Groenen-van Dooren, M. M., Ronden, J. E., Soute, B. A., and Vermeer, C. (1995) Bioavailability of phylloquinone and menaquinones after oral and colorectal administration in vitamin K-deficient rats. Biochem. Pharmacol. (Amsterdam, Neth.) 50, 797-801, 10.1016/0006-2952(95)00202-B
    • (1995) Biochem. Pharmacol. (Amsterdam, Neth.) , vol.50 , pp. 797-801
    • Groenen-Van Dooren, M.M.1    Ronden, J.E.2    Soute, B.A.3    Vermeer, C.4
  • 7
    • 84868634391 scopus 로고    scopus 로고
    • Comparison of menaquinone-4 and menaquinone-7 bioavailability in healthy women
    • Sato, T., Schurgers, L. J., and Uenishi, K. (2012) Comparison of menaquinone-4 and menaquinone-7 bioavailability in healthy women. Nutr. J. 11, 93-96, 10.1186/1475-2891-11-93
    • (2012) Nutr. J. , vol.11 , pp. 93-96
    • Sato, T.1    Schurgers, L.J.2    Uenishi, K.3
  • 8
    • 84881668029 scopus 로고    scopus 로고
    • Three-year low-dose menaquinone-7 supplementation helps decrease bone loss in healthy postmenopausal women
    • Knapen, M. H., Drummen, N. E., Smit, E., Vermeer, C., and Theuwissen, E. (2013) Three-year low-dose menaquinone-7 supplementation helps decrease bone loss in healthy postmenopausal women. Osteoporosis Int. 24, 2499-2507, 10.1007/s00198-013-2325-6
    • (2013) Osteoporosis Int. , vol.24 , pp. 2499-2507
    • Knapen, M.H.1    Drummen, N.E.2    Smit, E.3    Vermeer, C.4    Theuwissen, E.5
  • 9
    • 84940836409 scopus 로고    scopus 로고
    • High-dose menaquinone-7 supplementation reduces cardiovascular calcification in a murine model of extraosseous calcification
    • Scheiber, D., Veulemans, V., Horn, P., Chatrou, M. L., Potthoff, S. A., Kelm, M., Schurgers, L. J., and Westenfeld, R. (2015) High-dose menaquinone-7 supplementation reduces cardiovascular calcification in a murine model of extraosseous calcification. Nutrients 7, 6991-7011, 10.3390/nu7085318
    • (2015) Nutrients , vol.7 , pp. 6991-7011
    • Scheiber, D.1    Veulemans, V.2    Horn, P.3    Chatrou, M.L.4    Potthoff, S.A.5    Kelm, M.6    Schurgers, L.J.7    Westenfeld, R.8
  • 11
    • 84932133919 scopus 로고    scopus 로고
    • Vitamin K series: Current status and future prospects
    • Berenjian, A., Mahanama, R., Kavanagh, J., and Dehghani, F. (2015) Vitamin K series: current status and future prospects. Crit. Rev. Biotechnol. 35, 199-208, 10.3109/07388551.2013.832142
    • (2015) Crit. Rev. Biotechnol. , vol.35 , pp. 199-208
    • Berenjian, A.1    Mahanama, R.2    Kavanagh, J.3    Dehghani, F.4
  • 13
    • 85009799801 scopus 로고    scopus 로고
    • Effect of media components and morphology of Bacillus natto on menaquinone-7 synthesis in submerged fermentation
    • Luo, M. M., Ren, L. J., Chen, S. L., Ji, X. J., and Huang, H. (2016) Effect of media components and morphology of Bacillus natto on menaquinone-7 synthesis in submerged fermentation. Biotechnol. Bioprocess Eng. 21, 777-786, 10.1007/s12257-016-0202-9
    • (2016) Biotechnol. Bioprocess Eng. , vol.21 , pp. 777-786
    • Luo, M.M.1    Ren, L.J.2    Chen, S.L.3    Ji, X.J.4    Huang, H.5
  • 16
    • 85021644811 scopus 로고    scopus 로고
    • Enhancing menaquinone-7 production in recombinant Bacillus amyloliquefaciens by metabolic pathway engineering
    • Xu, J. Z., Yan, W. L., and Zhang, W. G. (2017) Enhancing menaquinone-7 production in recombinant Bacillus amyloliquefaciens by metabolic pathway engineering. RSC Adv. 7, 28527-28534, 10.1039/C7RA03388E
    • (2017) RSC Adv. , vol.7 , pp. 28527-28534
    • Xu, J.Z.1    Yan, W.L.2    Zhang, W.G.3
  • 17
    • 1942538348 scopus 로고    scopus 로고
    • Developments in the use of Bacillus species for industrial production
    • Schallmey, M., Singh, A., and Ward, O. P. (2004) Developments in the use of Bacillus species for industrial production. Can. J. Microbiol. 50, 1-17, 10.1139/w03-076
    • (2004) Can. J. Microbiol. , vol.50 , pp. 1-17
    • Schallmey, M.1    Singh, A.2    Ward, O.P.3
  • 19
    • 84873657319 scopus 로고    scopus 로고
    • Generation of an artificial double promoter for protein expression in Bacillus subtilis through a promoter trap system
    • Yang, M., Zhang, W., Ji, S., Cao, P., Chen, Y., and Xin, Z. (2013) Generation of an artificial double promoter for protein expression in Bacillus subtilis through a promoter trap system. PLoS One 8, e56321 10.1371/journal.pone.0056321
    • (2013) PLoS One , vol.8 , pp. e56321
    • Yang, M.1    Zhang, W.2    Ji, S.3    Cao, P.4    Chen, Y.5    Xin, Z.6
  • 21
    • 0037321888 scopus 로고    scopus 로고
    • The biosynthesis of shikimate metabolites
    • Knaggs, A. R. (2003) The biosynthesis of shikimate metabolites. Nat. Prod. Rep. 34, 119-136, 10.1039/b100399m
    • (2003) Nat. Prod. Rep. , vol.34 , pp. 119-136
    • Knaggs, A.R.1
  • 22
    • 84928014943 scopus 로고    scopus 로고
    • Metabolic and genetic factors affecting the productivity of pyrimidine nucleoside in Bacillus subtilis
    • Zhu, H., Yang, S. M., Yuan, Z. M., and Ban, R. (2015) Metabolic and genetic factors affecting the productivity of pyrimidine nucleoside in Bacillus subtilis. Microb. Cell Fact. 14, 1-12, 10.1186/s12934-015-0237-1
    • (2015) Microb. Cell Fact. , vol.14 , pp. 1-12
    • Zhu, H.1    Yang, S.M.2    Yuan, Z.M.3    Ban, R.4
  • 23
    • 0024652299 scopus 로고
    • Chromosomal location, cloning and nucleotide sequence of the Bacillus subtilis cdd gene encoding cytidine/deoxycytidine deaminase
    • Song, B. H. and Neuhard, J. (1989) Chromosomal location, cloning and nucleotide sequence of the Bacillus subtilis cdd gene encoding cytidine/deoxycytidine deaminase. Mol. Gen. Genet. 216, 462-468, 10.1007/BF00334391
    • (1989) Mol. Gen. Genet. , vol.216 , pp. 462-468
    • Song, B.H.1    Neuhard, J.2
  • 25
    • 79959259581 scopus 로고    scopus 로고
    • Metabolic engineering of menaquinone-8 pathway of Escherichia coli as a microbial platform for vitamin K production
    • Kong, M. K. and Lee, P. C. (2011) Metabolic engineering of menaquinone-8 pathway of Escherichia coli as a microbial platform for vitamin K production. Biotechnol. Bioeng. 108, 1997-2002, 10.1002/bit.23142
    • (2011) Biotechnol. Bioeng. , vol.108 , pp. 1997-2002
    • Kong, M.K.1    Lee, P.C.2
  • 26
    • 0035219809 scopus 로고    scopus 로고
    • 2 ) and ubiquinone (coenzyme Q): A perspective on enzymatic mechanisms
    • 2 ) and ubiquinone (coenzyme Q): a perspective on enzymatic mechanisms. Vitam. Horm. (London, U. K.) 61, 173-218, 10.1016/S0083-6729(01)61006-9
    • (2001) Vitam. Horm. (London, U. K.) , vol.61 , pp. 173-218
    • Meganathan, R.1
  • 27
    • 84958969892 scopus 로고    scopus 로고
    • Engineering the shikimate pathway for biosynthesis of molecules with pharmaceutical activities in E. coli
    • Jiang, M. and Zhang, H. (2016) Engineering the shikimate pathway for biosynthesis of molecules with pharmaceutical activities in E. coli. Curr. Opin. Biotechnol. 42, 1-6, 10.1016/j.copbio.2016.01.016
    • (2016) Curr. Opin. Biotechnol. , vol.42 , pp. 1-6
    • Jiang, M.1    Zhang, H.2
  • 30
    • 0020479277 scopus 로고
    • The nucleotide sequence of aroG, the gene for 3-deoxy-D-arabinoheptulosonate-7-phosphate synthetase (phe) in Escherichia coli K12
    • Davies, W. and Davidson, B. (1982) The nucleotide sequence of aroG, the gene for 3-deoxy-D-arabinoheptulosonate-7-phosphate synthetase (phe) in Escherichia coli K12. Nucleic Acids Res. 10, 4045-4058, 10.1093/nar/10.13.4045
    • (1982) Nucleic Acids Res. , vol.10 , pp. 4045-4058
    • Davies, W.1    Davidson, B.2
  • 31
    • 0019382235 scopus 로고
    • Structure and regulation of aroH, the structural gene for the tryptophan-repressible 3-deoxy-D-arabino-heptulosonic acid-7-phosphate synthetase of Escherichia coli
    • Zurawski, G., Gunsalus, R. P., Brown, K. D., and Yanofsky, C. (1981) Structure and regulation of aroH, the structural gene for the tryptophan-repressible 3-deoxy-D-arabino-heptulosonic acid-7-phosphate synthetase of Escherichia coli. J. Mol. Biol. 145, 47-73, 10.1016/0022-2836(81)90334-X
    • (1981) J. Mol. Biol. , vol.145 , pp. 47-73
    • Zurawski, G.1    Gunsalus, R.P.2    Brown, K.D.3    Yanofsky, C.4
  • 32
    • 10044287191 scopus 로고    scopus 로고
    • Stimulation, monitoring, and analysis of pathway dynamics by metabolic profiling in the aromatic amino acid pathway
    • Oldiges, M., Kunze, M., Degenring, D., Sprenger, G. A., and Takors, R. (2010) Stimulation, monitoring, and analysis of pathway dynamics by metabolic profiling in the aromatic amino acid pathway. Biotechnol. Prog. 20, 1623-1633, 10.1021/bp0498746
    • (2010) Biotechnol. Prog. , vol.20 , pp. 1623-1633
    • Oldiges, M.1    Kunze, M.2    Degenring, D.3    Sprenger, G.A.4    Takors, R.5
  • 33
    • 39849084210 scopus 로고    scopus 로고
    • Combinatorial pathway analysis for improved L-tyrosine production in Escherichia coli: Identification of enzymatic bottlenecks by systematic gene overexpression
    • Lutke-Eversloh, T. and Stephanopoulos, G. (2008) Combinatorial pathway analysis for improved L-tyrosine production in Escherichia coli: identification of enzymatic bottlenecks by systematic gene overexpression. Metab. Eng. 10, 69-77, 10.1016/j.ymben.2007.12.001
    • (2008) Metab. Eng. , vol.10 , pp. 69-77
    • Lutke-Eversloh, T.1    Stephanopoulos, G.2
  • 34
    • 84899143621 scopus 로고    scopus 로고
    • Metabolic flux responses to genetic modification for shikimic acid production by Bacillus subtilis strains
    • Liu, D. F., Ai, G. M., Zheng, Q. X., Liu, C., Jiang, C. Y., Liu, L. X., Zhang, B., Liu, Y. M., Yang, C., and Liu, S. J. (2014) Metabolic flux responses to genetic modification for shikimic acid production by Bacillus subtilis strains. Microb. Cell Fact. 13, 1-11, 10.1186/1475-2859-13-40
    • (2014) Microb. Cell Fact. , vol.13 , pp. 1-11
    • Liu, D.F.1    Ai, G.M.2    Zheng, Q.X.3    Liu, C.4    Jiang, C.Y.5    Liu, L.X.6    Zhang, B.7    Liu, Y.M.8    Yang, C.9    Liu, S.J.10
  • 35
    • 0033966887 scopus 로고    scopus 로고
    • Isoprene biosynthesis in Bacillus subtilis via the methylerythritol phosphate pathway
    • Wagner, W. P., Helmig, D., and Fall, R. (2000) Isoprene biosynthesis in Bacillus subtilis via the methylerythritol phosphate pathway. J. Nat. Prod. 63, 37-40, 10.1021/np990286p
    • (2000) J. Nat. Prod. , vol.63 , pp. 37-40
    • Wagner, W.P.1    Helmig, D.2    Fall, R.3
  • 36
    • 3042810286 scopus 로고    scopus 로고
    • Biosynthesis of isoprenoids via the non-mevalonate pathway
    • Eisenreich, W., Bacher, A., Arigoni, D., and Rohdich, F. (2004) Biosynthesis of isoprenoids via the non-mevalonate pathway. Cell. Mol. Life Sci. 61, 1401-1426, 10.1007/s00018-004-3381-z
    • (2004) Cell. Mol. Life Sci. , vol.61 , pp. 1401-1426
    • Eisenreich, W.1    Bacher, A.2    Arigoni, D.3    Rohdich, F.4
  • 37
    • 79953268907 scopus 로고    scopus 로고
    • Enhancing isoprene production by genetic modification of the 1-deoxy-d-xylulose-5-phosphate pathway in Bacillus subtilis
    • Xue, J. and Ahring, B. K. (2011) Enhancing isoprene production by genetic modification of the 1-deoxy-d-xylulose-5-phosphate pathway in Bacillus subtilis. Appl. Environ. Microbiol. 77, 2399-2405, 10.1128/AEM.02341-10
    • (2011) Appl. Environ. Microbiol. , vol.77 , pp. 2399-2405
    • Xue, J.1    Ahring, B.K.2
  • 38
    • 34250828514 scopus 로고    scopus 로고
    • Functional analysis of genes involved in biosynthesis of isoprene in Bacillus subtilis
    • Julsing, M. K., Rijpkema, M., Woerdenbag, H. J., Quax, W. J., and Kayser, O. (2007) Functional analysis of genes involved in biosynthesis of isoprene in Bacillus subtilis. Appl. Microbiol. Biotechnol. 75, 1377-1384, 10.1007/s00253-007-0953-5
    • (2007) Appl. Microbiol. Biotechnol. , vol.75 , pp. 1377-1384
    • Julsing, M.K.1    Rijpkema, M.2    Woerdenbag, H.J.3    Quax, W.J.4    Kayser, O.5
  • 39
    • 84879232156 scopus 로고    scopus 로고
    • Coregulation of terpenoid pathway genes and prediction of isoprene production in Bacillus subtilis using transcriptomics
    • Hess, B. M., Xue, J., Markillie, L. M., Taylor, R. C., Wiley, H. S., Ahring, B. K., and Linggi, B. (2013) Coregulation of terpenoid pathway genes and prediction of isoprene production in Bacillus subtilis using transcriptomics. PLoS One 8, e66104 10.1371/journal.pone.0066104
    • (2013) PLoS One , vol.8 , pp. e66104
    • Hess, B.M.1    Xue, J.2    Markillie, L.M.3    Taylor, R.C.4    Wiley, H.S.5    Ahring, B.K.6    Linggi, B.7
  • 40
    • 33846183593 scopus 로고    scopus 로고
    • Improved subtilisin YaB production in Bacillus subtilis using engineered synthetic expression control sequences
    • Wang, J. P., Yeh, C. M., and Tsai, Y. C. (2006) Improved subtilisin YaB production in Bacillus subtilis using engineered synthetic expression control sequences. J. Agric. Food Chem. 54, 9405-9410, 10.1021/jf061982f
    • (2006) J. Agric. Food Chem. , vol.54 , pp. 9405-9410
    • Wang, J.P.1    Yeh, C.M.2    Tsai, Y.C.3
  • 42
    • 84994469233 scopus 로고    scopus 로고
    • A structural and functional study on the 2-C-methyl-d-erythritol-4-phosphate cytidyltransferase (IspD) from Bacillus subtilis
    • Jin, Y., Liu, Z., Li, Y., Liu, W., Tao, Y., and Wang, G. (2016) A structural and functional study on the 2-C-methyl-d-erythritol-4-phosphate cytidyltransferase (IspD) from Bacillus subtilis. Sci. Rep. 6, 1-11, 10.1038/srep36379
    • (2016) Sci. Rep. , vol.6 , pp. 1-11
    • Jin, Y.1    Liu, Z.2    Li, Y.3    Liu, W.4    Tao, Y.5    Wang, G.6
  • 43
    • 85043266557 scopus 로고    scopus 로고
    • Crystal structure of IspF from Bacillus subtilis and absence of protein complex assembly among IspD/IspE/IspF enzymes in the MEP pathway
    • Liu, Z., Jin, Y., Liu, W., Tao, Y., and Wang, G. (2018) Crystal structure of IspF from Bacillus subtilis and absence of protein complex assembly among IspD/IspE/IspF enzymes in the MEP pathway. Biosci. Rep. 38, 1-14, 10.1042/BSR20171370
    • (2018) Biosci. Rep. , vol.38 , pp. 1-14
    • Liu, Z.1    Jin, Y.2    Liu, W.3    Tao, Y.4    Wang, G.5
  • 44
    • 59849123384 scopus 로고    scopus 로고
    • Structural characterizations of glycerol kinase: Unraveling phosphorylation-induced long-range activation
    • Yeh, J. I., Kettering, R., Saxl, R., Bourand, A., Darbon, E., Joly, N., Briozzo, P., and Deutscher, J. (2009) Structural characterizations of glycerol kinase: unraveling phosphorylation-induced long-range activation. Biochemistry 48, 346-356, 10.1021/bi8009407
    • (2009) Biochemistry , vol.48 , pp. 346-356
    • Yeh, J.I.1    Kettering, R.2    Saxl, R.3    Bourand, A.4    Darbon, E.5    Joly, N.6    Briozzo, P.7    Deutscher, J.8
  • 45
    • 0025647659 scopus 로고
    • Glycerol catabolism in Bacillus subtilis: Nucleotide sequence of the genes encoding glycerol kinase (glpK) and glycerol-3-phosphate dehydrogenase (glpD)
    • Holmberg, C., Beijer, L., Rutberg, B., and Rutberg, L. (1990) Glycerol catabolism in Bacillus subtilis: nucleotide sequence of the genes encoding glycerol kinase (glpK) and glycerol-3-phosphate dehydrogenase (glpD). J. Gen. Microbiol. 136, 2367-2375, 10.1099/00221287-136-12-2367
    • (1990) J. Gen. Microbiol. , vol.136 , pp. 2367-2375
    • Holmberg, C.1    Beijer, L.2    Rutberg, B.3    Rutberg, L.4
  • 46
    • 0027502308 scopus 로고
    • The glpP and glpF genes of the glycerol regulon in Bacillus subtilis
    • Beijer, L., Nilsson, R. P., Holmberg, C., and Rutberg, L. (1993) The glpP and glpF genes of the glycerol regulon in Bacillus subtilis. J. Gen. Microbiol. 139, 349-359, 10.1099/00221287-139-2-349
    • (1993) J. Gen. Microbiol. , vol.139 , pp. 349-359
    • Beijer, L.1    Nilsson, R.P.2    Holmberg, C.3    Rutberg, L.4
  • 47
    • 0031886850 scopus 로고    scopus 로고
    • Antiterminator protein GlpP of Bacillus subtilis binds to glpD leader mRNA
    • Glatz, E., Persson, M., and Rutberg, B. (1998) Antiterminator protein GlpP of Bacillus subtilis binds to glpD leader mRNA. Microbiology 144, 449-456, 10.1099/00221287-144-2-449
    • (1998) Microbiology , vol.144 , pp. 449-456
    • Glatz, E.1    Persson, M.2    Rutberg, B.3
  • 48
    • 0036227754 scopus 로고    scopus 로고
    • Antitermination by GlpP, catabolite repression via CcpA and inducer exclusion triggered by P∼GlpK dephosphorylation control Bacillus subtilis glpFK expression
    • Darbon, E., Servant, P., Poncet, S., and Deutscher, J. (2002) Antitermination by GlpP, catabolite repression via CcpA and inducer exclusion triggered by P∼GlpK dephosphorylation control Bacillus subtilis glpFK expression. Mol. Microbiol. 43, 1039-1052, 10.1046/j.1365-2958.2002.02800.x
    • (2002) Mol. Microbiol. , vol.43 , pp. 1039-1052
    • Darbon, E.1    Servant, P.2    Poncet, S.3    Deutscher, J.4
  • 49
    • 27144540194 scopus 로고    scopus 로고
    • Coordinated patterns of cytochrome bd and lactate dehydrogenase expression in Bacillus subtilis
    • Larsson, J. T., Rogstam, A., and Von, W. C. (2005) Coordinated patterns of cytochrome bd and lactate dehydrogenase expression in Bacillus subtilis. Microbiology (London, U. K.) 151, 3323-3335, 10.1099/mic.0.28124-0
    • (2005) Microbiology (London, U. K.) , vol.151 , pp. 3323-3335
    • Larsson, J.T.1    Rogstam, A.2    Von, W.C.3
  • 50
    • 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-exponential-phase production of acetoin. J. Bacteriol. 175, 3863-3875, 10.1128/jb.175.12.3863-3875.1993
    • (1993) J. Bacteriol. , vol.175 , pp. 3863-3875
    • Renna, M.C.1    Najimudin, N.2    Winik, L.R.3    Zahler, S.A.4
  • 51
    • 85035804809 scopus 로고    scopus 로고
    • Sequential induction of Fur-regulated genes in response to iron limitation in Bacillus subtilis
    • Pi, H. and Helmann, J. D. (2017) Sequential induction of Fur-regulated genes in response to iron limitation in Bacillus subtilis. Proc. Natl. Acad. Sci. U. S. A. 114, 12785-12790, 10.1073/pnas.1713008114
    • (2017) Proc. Natl. Acad. Sci. U. S. A. , vol.114 , pp. 12785-12790
    • Pi, H.1    Helmann, J.D.2
  • 52
    • 0142252493 scopus 로고    scopus 로고
    • Sequence and genetic organization of a Bacillus subtilis operon encoding 2,3-dihydroxybenzoate biosynthetic enzymes
    • Rowland, B. M., Grossman, T. H., Osburne, M. S., and Taber, H. W. (1996) Sequence and genetic organization of a Bacillus subtilis operon encoding 2,3-dihydroxybenzoate biosynthetic enzymes. Gene 178, 119-123, 10.1016/0378-1119(96)00349-6
    • (1996) Gene , vol.178 , pp. 119-123
    • Rowland, B.M.1    Grossman, T.H.2    Osburne, M.S.3    Taber, H.W.4
  • 53
    • 0035831486 scopus 로고    scopus 로고
    • The dhb operon of Bacillus subtilis encodes the biosynthetic template for the catecholic siderophore 2,3-dihydroxybenzoate-glycine-threonine trimeric ester bacillibactin
    • May, J. J., Wendrich, T. M., and Marahiel, M. A. (2001) The dhb operon of Bacillus subtilis encodes the biosynthetic template for the catecholic siderophore 2,3-dihydroxybenzoate-glycine-threonine trimeric ester bacillibactin. J. Biol. Chem. 276, 7209-7217, 10.1074/jbc.M009140200
    • (2001) J. Biol. Chem. , vol.276 , pp. 7209-7217
    • May, J.J.1    Wendrich, T.M.2    Marahiel, M.A.3
  • 54
    • 23744469930 scopus 로고    scopus 로고
    • Natto Bacillus contains a large amount of water-soluble vitamin K (menaquinone-7)
    • Yanagisawa, Y. and Sumi, H. (2005) Natto Bacillus contains a large amount of water-soluble vitamin K (menaquinone-7). J. Food Biochem. 29, 267-277, 10.1111/j.1745-4514.2005.00016.x
    • (2005) J. Food Biochem. , vol.29 , pp. 267-277
    • Yanagisawa, Y.1    Sumi, H.2
  • 55
    • 0025195459 scopus 로고
    • 2 -binding factor secreted from Bacillus subtilis
    • 2 -binding factor secreted from Bacillus subtilis. Eur. J. Biochem. 192, 219-224, 10.1111/j.1432-1033.1990.tb19218.x
    • (1990) Eur. J. Biochem. , vol.192 , pp. 219-224
    • Ikeda, H.1    Doi, Y.2
  • 56
    • 0036034078 scopus 로고    scopus 로고
    • A new mutation delivery system for genome-scale approaches in Bacillus subtilis
    • Fabret, C., Ehrlich, S. D., and Noirot, P. (2010) A new mutation delivery system for genome-scale approaches in Bacillus subtilis. Mol. Microbiol. 46, 25-36, 10.1046/j.1365-2958.2002.03140.x
    • (2010) Mol. Microbiol. , vol.46 , pp. 25-36
    • Fabret, C.1    Ehrlich, S.D.2    Noirot, P.3
  • 57
    • 0003225732 scopus 로고    scopus 로고
    • Molecular cloning: A laboratory manual (3rd edition)
    • Sambrook, J. F. and Russell, D. W. (2001) Molecular cloning: a laboratory manual (3rd edition). Immunology 49, 895-909
    • (2001) Immunology , vol.49 , pp. 895-909
    • Sambrook, J.F.1    Russell, D.W.2
  • 58
    • 0001134202 scopus 로고
    • Requirements for transformation in Bacillus subtilis
    • Anagnostopoulos, C. and Spizizen, J. (1961) Requirements for transformation in Bacillus subtilis. J. Bacteriol. 81, 741-746
    • (1961) J. Bacteriol. , vol.81 , pp. 741-746
    • Anagnostopoulos, C.1    Spizizen, J.2
  • 59
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • Ho, S. N., Hunt, H. D., Horton, R. M., Pullen, J. K., and Pease, L. R. (1989) Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 77, 51-59, 10.1016/0378-1119(89)90358-2
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 60
  • 61
    • 53449095004 scopus 로고    scopus 로고
    • Introduction of marker-free deletions in Bacillus subtilis using the AraR repressor and the ara promoter
    • Liu, S., Endo, K., Ara, K., Ozaki, K., and Ogasawara, N. (2008) Introduction of marker-free deletions in Bacillus subtilis using the AraR repressor and the ara promoter. Microbiology (London, U. K.) 154, 2562-2570, 10.1099/mic.0.2008/016881-0
    • (2008) Microbiology (London, U. K.) , vol.154 , pp. 2562-2570
    • Liu, S.1    Endo, K.2    Ara, K.3    Ozaki, K.4    Ogasawara, N.5
  • 62
    • 84901459476 scopus 로고    scopus 로고
    • Current development in genetic engineering strategies of Bacillus species
    • Dong, H. and Zhang, D. (2014) Current development in genetic engineering strategies of Bacillus species. Microb. Cell Fact. 13, 63, 10.1186/1475-2859-13-63
    • (2014) Microb. Cell Fact. , vol.13 , pp. 63
    • Dong, H.1    Zhang, D.2
  • 63
    • 84896698691 scopus 로고    scopus 로고
    • Establishment of a markerless mutation delivery system in Bacillus subtilis stimulated by a double-strand break in the chromosome
    • Shi, T., Wang, G., Wang, Z., Fu, J., Chen, T., and Zhao, X. (2013) Establishment of a markerless mutation delivery system in Bacillus subtilis stimulated by a double-strand break in the chromosome. PLoS One 8, e81370 10.1371/journal.pone.0081370
    • (2013) PLoS One , vol.8 , pp. e81370
    • Shi, T.1    Wang, G.2    Wang, Z.3    Fu, J.4    Chen, T.5    Zhao, X.6
  • 65
    • 34247141488 scopus 로고    scopus 로고
    • Bacillus minimum genome factory: Effective utilization of microbial genome information
    • Ara, K., Ozaki, K., Nakamura, K., Yamane, K., Sekiguchi, J., and Ogasawara, N. (2011) Bacillus minimum genome factory: effective utilization of microbial genome information. Biotechnol. Appl. Biochem. 46, 169-178, 10.1042/BA20060111
    • (2011) Biotechnol. Appl. Biochem. , vol.46 , pp. 169-178
    • Ara, K.1    Ozaki, K.2    Nakamura, K.3    Yamane, K.4    Sekiguchi, J.5    Ogasawara, N.6
  • 66
    • 17344392308 scopus 로고    scopus 로고
    • A new mathematical model for relative quantification in real-time RT-PCR
    • Pfaffl, M. W. (2001) A new mathematical model for relative quantification in real-time RT-PCR. Nucleic Acids Res. 29, e45 10.1093/nar/29.9.e45
    • (2001) Nucleic Acids Res. , vol.29 , pp. e45
    • Pfaffl, M.W.1


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