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Volumn 5, Issue 3, 2014, Pages

Coordinating bacterial cell division with nutrient availability: A role for glycolysis

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; CARBON; EZRA PROTEIN; FTSZ PROTEIN; PYRUVATE DEHYDROGENASE; PYRUVATE DEHYDROGENASE E1ALPHA SUBUNIT; PYRUVATE KINASE; PYRUVIC ACID; UNCLASSIFIED DRUG; BACTERIAL PROTEIN; CYTOSKELETON PROTEIN; FTSZ PROTEIN, BACTERIA; PROTEIN BINDING;

EID: 84904012197     PISSN: 21612129     EISSN: 21507511     Source Type: Journal    
DOI: 10.1128/mBio.00935-14     Document Type: Article
Times cited : (87)

References (83)
  • 1
    • 33846246039 scopus 로고    scopus 로고
    • Bacterial cell division: The mechanism and its precision
    • In Jeon KW (ed), Academic Press, San Diego, CA
    • Harry E, Monahan L, Thompson L. 2006. Bacterial cell division: the mechanism and its precision, p 27-94. In Jeon KW (ed), International review of cytology: a survey of cell biology, vol. 253. Academic Press, San Diego, CA.
    • (2006) International review of cytology: A survey of cell biology , vol.253 , pp. 27-94
    • Harry, E.1    Monahan, L.2    Thompson, L.3
  • 2
    • 69249126551 scopus 로고    scopus 로고
    • Bacterial cell division: Assembly, maintenance and disassembly of the Z ring
    • Adams DW, Errington J. 2009. Bacterial cell division: assembly, maintenance and disassembly of the Z ring. Nat. Rev. Microbiol. 7: 642-653. http://dx. doi. org/10. 1038/nrmicro2198.
    • (2009) Nat. Rev. Microbiol , vol.7 , pp. 642-653
    • Adams, D.W.1    Errington, J.2
  • 3
    • 78649646536 scopus 로고    scopus 로고
    • Advances in understanding E coli cell fission
    • de Boer PA. 2010. Advances in understanding E. coli cell fission. Curr. Opin. Microbiol. 13: 730-737. http://dx. doi. org/10. 1016/j. mib. 2010. 09. 015.
    • (2010) Curr. Opin. Microbiol , vol.13 , pp. 730-737
    • de Boer, P.A.1
  • 4
    • 78650078263 scopus 로고    scopus 로고
    • FtsZ in bacterial cytokinesis: Cytoskeleton and force generator all in one
    • Erickson HP, Anderson DE, Osawa M. 2010. FtsZ in bacterial cytokinesis: cytoskeleton and force generator all in one. Microbiol. Mol. Biol. Rev. 74: 504-528. http://dx. doi. org/10. 1128/MMBR. 00021-10.
    • (2010) Microbiol. Mol. Biol. Rev , vol.74 , pp. 504-528
    • Erickson, H.P.1    Anderson, D.E.2    Osawa, M.3
  • 5
    • 44049091371 scopus 로고    scopus 로고
    • Reconstitution of contractile FtsZ rings in liposomes
    • Osawa M, Anderson DE, Erickson HP. 2008. Reconstitution of contractile FtsZ rings in liposomes. Science 320: 792-794. http://dx. doi. org/10. 1126/science. 1154520.
    • (2008) Science , vol.320 , pp. 792-794
    • Osawa, M.1    Anderson, D.E.2    Erickson, H.P.3
  • 6
    • 77955271619 scopus 로고    scopus 로고
    • Strong FtsZ is with the force: Mechanisms to constrict bacteria
    • Mingorance J, Rivas G, Vélez M, Gómez-Puertas P, Vicente M. 2010. Strong FtsZ is with the force: mechanisms to constrict bacteria. Trends Microbiol. 18: 348-356. http://dx. doi. org/10. 1016/j. tim. 2010. 06. 001.
    • (2010) Trends Microbiol , vol.18 , pp. 348-356
    • Mingorance, J.1    Rivas, G.2    Vélez, M.3    Gómez-Puertas, P.4    Vicente, M.5
  • 7
    • 84879700551 scopus 로고    scopus 로고
    • Liposome division by a simple bacterial division machinery
    • Osawa M, Erickson HP. 2013. Liposome division by a simple bacterial division machinery. Proc. Natl. Acad. Sci. U. S. A. 110: 11000-11004. http://dx. doi. org/10. 1073/pnas. 1222254110.
    • (2013) Proc. Natl. Acad. Sci. U.S. A , vol.110 , pp. 11000-11004
    • Osawa, M.1    Erickson, H.P.2
  • 8
    • 84897651217 scopus 로고    scopus 로고
    • Division site positioning in bacteria: One size does not fit all
    • Monahan LG, Liew ATF, Bottomley AL, Harry EJ. 2014. Division site positioning in bacteria: one size does not fit all. Front. Microbiol. 5: 19. http://dx. doi. org/10. 3389/fmicb. 2014. 00019.
    • (2014) Front. Microbiol , vol.5 , pp. 19
    • Monahan, L.G.1    Liew, A.T.F.2    Bottomley, A.L.3    Harry, E.J.4
  • 9
    • 71549130716 scopus 로고    scopus 로고
    • Division site selection in rod-shaped bacteria
    • Bramkamp M, van Baarle S. 2009. Division site selection in rod-shaped bacteria. Curr. Opin. Microbiol. 12: 683-688. http://dx. doi. org/10. 1016/j. mib. 2009. 10. 002.
    • (2009) Curr. Opin. Microbiol , vol.12 , pp. 683-688
    • Bramkamp, M.1    van Baarle, S.2
  • 10
    • 30544445654 scopus 로고    scopus 로고
    • Spatial control of bacterial division-site placement
    • Rothfield L, Taghbalout A, Shih YL. 2005. Spatial control of bacterial division-site placement. Nat. Rev. Microbiol. 3: 959-968. http://dx. doi. org/10. 1038/nrmicro1290.
    • (2005) Nat. Rev. Microbiol , vol.3 , pp. 959-968
    • Rothfield, L.1    Taghbalout, A.2    Shih, Y.L.3
  • 11
    • 83855160828 scopus 로고    scopus 로고
    • Nucleoid occlusion and bacterial cell division
    • Wu LJ, Errington J. 2011. Nucleoid occlusion and bacterial cell division. Nat. Rev. Microbiol. 10: 8-12. http://dx. doi. org/10. 1038/nrmicro2671.
    • (2011) Nat. Rev. Microbiol , vol.10 , pp. 8-12
    • Wu, L.J.1    Errington, J.2
  • 12
    • 2942752105 scopus 로고    scopus 로고
    • Coordination of cell division and chromosome segregation by a nucleoid occlusion protein in Bacillus subtilis
    • Wu LJ, Errington J. 2004. Coordination of cell division and chromosome segregation by a nucleoid occlusion protein in Bacillus subtilis. Cell 117: 915-925. http://dx. doi. org/10. 1016/j. cell. 2004. 06. 002.
    • (2004) Cell , vol.117 , pp. 915-925
    • Wu, L.J.1    Errington, J.2
  • 13
    • 19444386428 scopus 로고    scopus 로고
    • SlmA, a nucleoid-associated, FtsZ binding protein required for blocking septal ring assembly over chromosomes in Escherichia coli
    • Bernhardt TG, de Boer PA. 2005. SlmA, a nucleoid-associated, FtsZ binding protein required for blocking septal ring assembly over chromosomes in Escherichia coli. Mol. Cell 18: 555-564. http://dx. doi. org/10. 1016/j. molcel. 2005. 04. 012.
    • (2005) Mol. Cell , vol.18 , pp. 555-564
    • Bernhardt, T.G.1    de Boer, P.A.2
  • 14
    • 84892152898 scopus 로고    scopus 로고
    • Open questions about the function and evolution of bacterial Min systems
    • Barak I. 2013. Open questions about the function and evolution of bacterial Min systems. Front. Microbiol. 4: 378. http://dx. doi. org/10. 3389/fmicb. 2013. 00378.
    • (2013) Front. Microbiol , vol.4 , pp. 378
    • Barak, I.1
  • 15
    • 84859230735 scopus 로고    scopus 로고
    • The Min system and nucleoid occlusion are not required for identifying the division site in Bacillus subtilis but ensure its efficient utilization
    • Rodrigues CD, Harry EJ. 2012. The Min system and nucleoid occlusion are not required for identifying the division site in Bacillus subtilis but ensure its efficient utilization. PLOS Genet. 8: e1002561. http://dx. doi. org/10. 1371/journal. pgen. 1002561.
    • (2012) PLOS Genet , vol.8
    • Rodrigues, C.D.1    Harry, E.J.2
  • 16
    • 0041852612 scopus 로고    scopus 로고
    • Coupling the cell cycle to cell growth
    • Boye E, Nordström K. 2003. Coupling the cell cycle to cell growth. EMBO Rep. 4: 757-760. http://dx. doi. org/10. 1038/sj. embor. embor895.
    • (2003) EMBO Rep , vol.4 , pp. 757-760
    • Boye, E.1    Nordström, K.2
  • 17
    • 0014413357 scopus 로고
    • Chromosome replication and the division cycle of Escherichia coli B/r
    • Cooper S, Helmstetter CE. 1968. Chromosome replication and the division cycle of Escherichia coli B/r. J. Mol. Biol. 31: 519-540. http://dx. doi. org/10. 1016/0022-2836(68)90425-7.
    • (1968) J. Mol. Biol , vol.31 , pp. 519-540
    • Cooper, S.1    Helmstetter, C.E.2
  • 18
    • 42049099692 scopus 로고    scopus 로고
    • The great divide: Coordinating cell cycle events during bacterial growth and division
    • Haeusser DP, Levin PA. 2008. The great divide: coordinating cell cycle events during bacterial growth and division. Curr. Opin. Microbiol. 11: 94-99. http://dx. doi. org/10. 1016/j. mib. 2008. 02. 008.
    • (2008) Curr. Opin. Microbiol , vol.11 , pp. 94-99
    • Haeusser, D.P.1    Levin, P.A.2
  • 19
    • 70350194739 scopus 로고    scopus 로고
    • Metabolism, cell growth and the bacterial cell cycle
    • Wang JD, Levin PA. 2009. Metabolism, cell growth and the bacterial cell cycle. Nat. Rev. Microbiol. 7: 822-827. http://dx. doi. org/10. 1038/nrmicro2202.
    • (2009) Nat. Rev. Microbiol , vol.7 , pp. 822-827
    • Wang, J.D.1    Levin, P.A.2
  • 20
    • 0001140586 scopus 로고
    • Dependency on medium and temperature of cell size and chemical composition during balanced growth of Salmonella typhimurium
    • Schaechter M, Maaloe O, Kjeldgaard NO. 1958. Dependency on medium and temperature of cell size and chemical composition during balanced growth of Salmonella typhimurium. J. Gen. Microbiol. 19: 592-606. http://dx. doi. org/10. 1099/00221287-19-3-592.
    • (1958) J. Gen. Microbiol , vol.19 , pp. 592-606
    • Schaechter, M.1    Maaloe, O.2    Kjeldgaard, N.O.3
  • 21
    • 0016529714 scopus 로고
    • Control of cell length in Bacillus subtilis
    • Sargent MG. 1975. Control of cell length in Bacillus subtilis. J. Bacteriol. 123: 7-19.
    • (1975) J. Bacteriol , vol.123 , pp. 7-19
    • Sargent, M.G.1
  • 22
    • 0024728797 scopus 로고
    • Cell length, nucleoid separation, and cell division of rod-shaped and spherical cells of Escherichia coli
    • Donachie WD, Begg KJ. 1989. Cell length, nucleoid separation, and cell division of rod-shaped and spherical cells of Escherichia coli. J. Bacteriol. 171: 4633-4639.
    • (1989) J. Bacteriol , vol.171 , pp. 4633-4639
    • Donachie, W.D.1    Begg, K.J.2
  • 23
    • 84860752551 scopus 로고    scopus 로고
    • Cell size control in bacteria
    • Chien AC, Hill NS, Levin PA. 2012. Cell size control in bacteria. Curr. Biol. 22: R340-R349. http://dx. doi. org/10. 1016/j. cub. 2012. 02. 032.
    • (2012) Curr. Biol , vol.22
    • Chien, A.C.1    Hill, N.S.2    Levin, P.A.3
  • 24
    • 34447537710 scopus 로고    scopus 로고
    • A metabolic sensor governing cell size in bacteria
    • Weart RB, Lee AH, Chien AC, Haeusser DP, Hill NS, Levin PA. 2007. A metabolic sensor governing cell size in bacteria. Cell 130: 335-347. http://dx. doi. org/10. 1016/j. cell. 2007. 05. 043.
    • (2007) Cell , vol.130 , pp. 335-347
    • Weart, R.B.1    Lee, A.H.2    Chien, A.C.3    Haeusser, D.P.4    Hill, N.S.5    Levin, P.A.6
  • 25
    • 84868146980 scopus 로고    scopus 로고
    • Changes in the oligomerization potential of the division inhibitor UgtP co-ordinate Bacillus subtilis cell size with nutrient availability
    • Chien AC, Zareh SK, Wang YM, Levin PA. 2012. Changes in the oligomerization potential of the division inhibitor UgtP co-ordinate Bacillus subtilis cell size with nutrient availability. Mol. Microbiol. 86: 594-610. http://dx. doi. org/10. 1111/mmi. 12007.
    • (2012) Mol. Microbiol , vol.86 , pp. 594-610
    • Chien, A.C.1    Zareh, S.K.2    Wang, Y.M.3    Levin, P.A.4
  • 26
    • 84880834788 scopus 로고    scopus 로고
    • A moonlighting enzyme links Escherichia coli cell size with central metabolism
    • Hill NS, Buske PJ, Shi Y, Levin PA. 2013. A moonlighting enzyme links Escherichia coli cell size with central metabolism. PLOS Genet. 9: e1003663. http://dx. doi. org/10. 1371/journal. pgen. 1003663.
    • (2013) PLOS Genet , vol.9
    • Hill, N.S.1    Buske, P.J.2    Shi, Y.3    Levin, P.A.4
  • 27
    • 0014567586 scopus 로고
    • Genetic analysis of the developmental processes during germination and outgrowth of Bacillus subtilis spores with temperature-sensitive mutants
    • Nukushina JI, Ikeda Y. 1969. Genetic analysis of the developmental processes during germination and outgrowth of Bacillus subtilis spores with temperature-sensitive mutants. Genetics 63: 63-74.
    • (1969) Genetics , vol.63 , pp. 63-74
    • Nukushina, J.I.1    Ikeda, Y.2
  • 28
    • 33644778043 scopus 로고    scopus 로고
    • Trapping of a spiral-like intermediate of the bacterial cytokinetic protein FtsZ. J
    • Michie KA, Monahan LG, Beech PL, Harry EJ. 2006. Trapping of a spiral-like intermediate of the bacterial cytokinetic protein FtsZ. J. Bacteriol. 188: 1680-1690. http://dx. doi. org/10. 1128/JB. 188. 5. 1680-1690. 2006.
    • (2006) Bacteriol , vol.188 , pp. 1680-1690
    • Michie, K.A.1    Monahan, L.G.2    Beech, P.L.3    Harry, E.J.4
  • 29
    • 70449586634 scopus 로고    scopus 로고
    • Lateral FtsZ association and the assembly of the cytokinetic Z ring in bacteria
    • Monahan LG, Robinson A, Harry EJ. 2009. Lateral FtsZ association and the assembly of the cytokinetic Z ring in bacteria. Mol. Microbiol. 74: 1004-1017. http://dx. doi. org/10. 1111/j. 1365-2958. 2009. 06914. x.
    • (2009) Mol. Microbiol , vol.74 , pp. 1004-1017
    • Monahan, L.G.1    Robinson, A.2    Harry, E.J.3
  • 30
    • 0034910795 scopus 로고    scopus 로고
    • Transcription of glycolytic genes and operons in Bacillus subtilis: Evidence for the presence of multiple levels of control of the gapA operon
    • Ludwig H, Homuth G, Schmalisch M, Dyka FM, Hecker M, Stülke J. 2001. Transcription of glycolytic genes and operons in Bacillus subtilis: evidence for the presence of multiple levels of control of the gapA operon. Mol. Microbiol. 41: 409-422. http://dx. doi. org/10. 1046/j. 1365-2958. 2001. 02523. x.
    • (2001) Mol. Microbiol , vol.41 , pp. 409-422
    • Ludwig, H.1    Homuth, G.2    Schmalisch, M.3    Dyka, F.M.4    Hecker, M.5    Stülke, J.6
  • 31
    • 34247349124 scopus 로고    scopus 로고
    • A new assembly pathway for the cytokinetic Z ring from a dynamic helical structure in vegetatively growing cells of Bacillus subtilis
    • Peters PC, Migocki MD, Thoni C, Harry EJ. 2007. A new assembly pathway for the cytokinetic Z ring from a dynamic helical structure in vegetatively growing cells of Bacillus subtilis. Mol. Microbiol. 64: 487-499. http://dx. doi. org/10. 1111/j. 1365-2958. 2007. 05673. x.
    • (2007) Mol. Microbiol , vol.64 , pp. 487-499
    • Peters, P.C.1    Migocki, M.D.2    Thoni, C.3    Harry, E.J.4
  • 32
    • 6344241323 scopus 로고    scopus 로고
    • The midcell replication factory in Bacillus subtilis is highly mobile: Implications for coordinating chromosome replication with other cell cycle events
    • Migocki MD, Lewis PJ, Wake RG, Harry EJ. 2004. The midcell replication factory in Bacillus subtilis is highly mobile: implications for coordinating chromosome replication with other cell cycle events. Mol. Microbiol. 54: 452-463. http://dx. doi. org/10. 1111/j. 1365-2958. 2004. 04267. x.
    • (2004) Mol. Microbiol , vol.54 , pp. 452-463
    • Migocki, M.D.1    Lewis, P.J.2    Wake, R.G.3    Harry, E.J.4
  • 33
    • 0036958551 scopus 로고    scopus 로고
    • The Min system is not required for precise placement of the midcell Z ring in Bacillus subtilis
    • Migocki MD, Freeman MK, Wake RG, Harry EJ. 2002. The Min system is not required for precise placement of the midcell Z ring in Bacillus subtilis. EMBO Rep. 3: 1163-1167. http://dx. doi. org/10. 1093/emboreports/kvf233.
    • (2002) EMBO Rep , vol.3 , pp. 1163-1167
    • Migocki, M.D.1    Freeman, M.K.2    Wake, R.G.3    Harry, E.J.4
  • 34
    • 0033578438 scopus 로고    scopus 로고
    • Identification and characterization of a negative regulator of FtsZ ring formation in Bacillus subtilis
    • Levin PA, Kurtser IG, Grossman AD. 1999. Identification and characterization of a negative regulator of FtsZ ring formation in Bacillus subtilis. Proc. Natl. Acad. Sci. U. S. A. 96: 9642-9647. http://dx. doi. org/10. 1073/pnas. 96. 17. 9642.
    • (1999) Proc. Natl. Acad. Sci. U.S. A , vol.96 , pp. 9642-9647
    • Levin, P.A.1    Kurtser, I.G.2    Grossman, A.D.3
  • 35
    • 0031765193 scopus 로고    scopus 로고
    • Effect of minCD on FtsZ ring position and polar septation in Bacillus subtilis
    • Levin PA, Shim JJ, Grossman AD. 1998. Effect of minCD on FtsZ ring position and polar septation in Bacillus subtilis. J. Bacteriol. 180: 6048-6051.
    • (1998) J. Bacteriol , vol.180 , pp. 6048-6051
    • Levin, P.A.1    Shim, J.J.2    Grossman, A.D.3
  • 36
    • 0022137060 scopus 로고
    • Overproduction of FtsZ induces minicell formation in E coli
    • Ward JE, Jr, Lutkenhaus J. 1985. Overproduction of FtsZ induces minicell formation in E. coli. Cell 42: 941-949. http://dx. doi. org/10. 1016/0092-8674(85)90290-9.
    • (1985) Cell , vol.42 , pp. 941-949
    • Ward Jr., J.E.1    Lutkenhaus, J.2
  • 37
    • 0037407703 scopus 로고    scopus 로고
    • Growth rate-dependent regulation of medial FtsZ ring formation
    • Weart RB, Levin PA. 2003. Growth rate-dependent regulation of medial FtsZ ring formation. J. Bacteriol. 185: 2826-2834. http://dx. doi. org/10. 1128/JB. 185. 9. 2826-2834. 2003.
    • (2003) J. Bacteriol , vol.185 , pp. 2826-2834
    • Weart, R.B.1    Levin, P.A.2
  • 38
    • 0033827444 scopus 로고    scopus 로고
    • Characterization of growth and acid formation in a Bacillus subtilis pyruvate kinase mutant
    • Fry B, Zhu T, Domach MM, Koepsel RR, Phalakornkule C, Ataai MM. 2000. Characterization of growth and acid formation in a Bacillus subtilis pyruvate kinase mutant. Appl. Environ. Microbiol. 66: 4045-4049. http://dx. doi. org/10. 1128/AEM. 66. 9. 4045-4049. 2000.
    • (2000) Appl. Environ. Microbiol , vol.66 , pp. 4045-4049
    • Fry, B.1    Zhu, T.2    Domach, M.M.3    Koepsel, R.R.4    Phalakornkule, C.5    Ataai, M.M.6
  • 39
    • 33750017570 scopus 로고    scopus 로고
    • Regulating expression of pyruvate kinase in Bacillus subtilis for control of growth rate and formation of acidic byproducts
    • Pan Z, Zhu T, Domagalski N, Khan S, Koepsel RR, Domach MM, Ataai MM. 2006. Regulating expression of pyruvate kinase in Bacillus subtilis for control of growth rate and formation of acidic byproducts. Biotechnol. Prog. 22: 1451-1455. http://dx. doi. org/10. 1021/bp060049u.
    • (2006) Biotechnol. Prog , vol.22 , pp. 1451-1455
    • Pan, Z.1    Zhu, T.2    Domagalski, N.3    Khan, S.4    Koepsel, R.R.5    Domach, M.M.6    Ataai, M.M.7
  • 41
    • 0036011149 scopus 로고    scopus 로고
    • The E1beta and E2 subunits of the Bacillus subtilis pyruvate dehydrogenase complex are involved in regulation of sporulation
    • Gao H, Jiang X, Pogliano K, Aronson AI. 2002. The E1beta and E2 subunits of the Bacillus subtilis pyruvate dehydrogenase complex are involved in regulation of sporulation. J. Bacteriol. 184: 2780-2788. http://dx. doi. org/10. 1128/JB. 184. 10. 2780-2788. 2002.
    • (2002) J. Bacteriol , vol.184 , pp. 2780-2788
    • Gao, H.1    Jiang, X.2    Pogliano, K.3    Aronson, A.I.4
  • 42
    • 0036791675 scopus 로고    scopus 로고
    • A widely conserved bacterial cell division protein that promotes assembly of the tubulin-like protein FtsZ
    • Gueiros-Filho FJ, Losick R. 2002. A widely conserved bacterial cell division protein that promotes assembly of the tubulin-like protein FtsZ. Genes Dev. 16: 2544-2556. http://dx. doi. org/10. 1101/gad. 1014102.
    • (2002) Genes Dev , vol.16 , pp. 2544-2556
    • Gueiros-Filho, F.J.1    Losick, R.2
  • 43
    • 33744479995 scopus 로고    scopus 로고
    • A new FtsZ-interacting protein, YlmF, complements the activity of FtsA during progression of cell division in Bacillus subtilis
    • Ishikawa S, Kawai Y, Hiramatsu K, Kuwano M, Ogasawara N. 2006. A new FtsZ-interacting protein, YlmF, complements the activity of FtsA during progression of cell division in Bacillus subtilis. Mol. Microbiol. 60: 1364-1380. http://dx. doi. org/10. 1111/j. 1365-2958. 2006. 05184. x.
    • (2006) Mol. Microbiol , vol.60 , pp. 1364-1380
    • Ishikawa, S.1    Kawai, Y.2    Hiramatsu, K.3    Kuwano, M.4    Ogasawara, N.5
  • 44
    • 33645055098 scopus 로고    scopus 로고
    • SepF, a novel FtsZ-interacting protein required for a late step in cell division
    • Hamoen LW, Meile JC, de Jong W, Noirot P, Errington J. 2006. SepF, a novel FtsZ-interacting protein required for a late step in cell division. Mol. Microbiol. 59: 989-999. http://dx. doi. org/10. 1111/j. 1365-2958. 2005. 04987. x.
    • (2006) Mol. Microbiol , vol.59 , pp. 989-999
    • Hamoen, L.W.1    Meile, J.C.2    de Jong, W.3    Noirot, P.4    Errington, J.5
  • 45
    • 36248971737 scopus 로고    scopus 로고
    • Control of key metabolic intersections in Bacillus subtilis
    • Sonenshein AL. 2007. Control of key metabolic intersections in Bacillus subtilis. Nat. Rev. Microbiol. 5: 917-927. http://dx. doi. org/10. 1038/nrmicro1772.
    • (2007) Nat. Rev. Microbiol , vol.5 , pp. 917-927
    • Sonenshein, A.L.1
  • 46
    • 0032537554 scopus 로고    scopus 로고
    • Gene and subunit organization of bacterial pyruvate dehydrogenase complexes
    • Neveling U, Bringer-Meyer S, Sahm H. 1998. Gene and subunit organization of bacterial pyruvate dehydrogenase complexes. Biochim. Biophys. Acta 1385: 367-372. http://dx. doi. org/10. 1016/S0167-4838(98)00080-6.
    • (1998) Biochim. Biophys. Acta , vol.1385 , pp. 367-372
    • Neveling, U.1    Bringer-Meyer, S.2    Sahm, H.3
  • 47
    • 0025160796 scopus 로고
    • Secretory S complex of Bacillus subtilis: Sequence analysis and identity to pyruvate dehydrogenase
    • Hemilä H, Palva A, Paulin L, Arvidson S, Palva I. 1990. Secretory S complex of Bacillus subtilis: sequence analysis and identity to pyruvate dehydrogenase. J. Bacteriol. 172: 5052-5063.
    • (1990) J. Bacteriol , vol.172 , pp. 5052-5063
    • Hemilä, H.1    Palva, A.2    Paulin, L.3    Arvidson, S.4    Palva, I.5
  • 48
    • 79952741894 scopus 로고    scopus 로고
    • Nucleoid occlusion factor SlmA is a DNA-activated FtsZ polymerization antagonist
    • Cho H, McManus HR, Dove SL, Bernhardt TG. 2011. Nucleoid occlusion factor SlmA is a DNA-activated FtsZ polymerization antagonist. Proc. Natl. Acad. Sci. U. S. A. 108: 3773-3778. http://dx. doi. org/10. 1073/pnas. 1018674108.
    • (2011) Proc. Natl. Acad. Sci. U.S. A , vol.108 , pp. 3773-3778
    • Cho, H.1    McManus, H.R.2    Dove, S.L.3    Bernhardt, T.G.4
  • 50
    • 67650435786 scopus 로고    scopus 로고
    • Noc protein binds to specific DNA sequences to coordinate cell division with chromosome segregation
    • Wu LJ, Ishikawa S, Kawai Y, Oshima T, Ogasawara N, Errington J. 2009. Noc protein binds to specific DNA sequences to coordinate cell division with chromosome segregation. EMBO J. 28: 1940-1952. http://dx. doi. org/10. 1038/emboj. 2009. 144.
    • (2009) EMBO J , vol.28 , pp. 1940-1952
    • Wu, L.J.1    Ishikawa, S.2    Kawai, Y.3    Oshima, T.4    Ogasawara, N.5    Errington, J.6
  • 51
    • 84880153102 scopus 로고    scopus 로고
    • Bacterial moonlighting proteins and bacterial virulence
    • Henderson B, Martin A. 2013. Bacterial moonlighting proteins and bacterial virulence. Curr. Top. Microbiol. Immunol. 358: 155-213. http://dx. doi. org/10. 1007/82+2011_188.
    • (2013) Curr. Top. Microbiol. Immunol , vol.358 , pp. 155-213
    • Henderson, B.1    Martin, A.2
  • 52
    • 80052329723 scopus 로고    scopus 로고
    • Bacterial virulence in the moonlight: Multitasking bacterial moonlighting proteins are virulence determinants in infectious disease
    • Henderson B, Martin A. 2011. Bacterial virulence in the moonlight: multitasking bacterial moonlighting proteins are virulence determinants in infectious disease. Infect. Immun. 79: 3476-3491. http://dx. doi. org/10. 1128/IAI. 00179-11.
    • (2011) Infect. Immun , vol.79 , pp. 3476-3491
    • Henderson, B.1    Martin, A.2
  • 53
    • 84862324402 scopus 로고    scopus 로고
    • Moonlighting is mainstream: Paradigm adjustment required
    • Copley SD. 2012. Moonlighting is mainstream: paradigm adjustment required. Bioessays 34: 578-588. http://dx. doi. org/10. 1002/bies. 201100191.
    • (2012) Bioessays , vol.34 , pp. 578-588
    • Copley, S.D.1
  • 54
    • 77950369259 scopus 로고    scopus 로고
    • Moonlighting proteins: An intriguing mode of multitasking
    • Huberts DH, van der Klei IJ. 2010. Moonlighting proteins: an intriguing mode of multitasking. Biochim. Biophys. Acta 1803: 520-525. http://dx. doi. org/10. 1016/j. bbamcr. 2010. 01. 022.
    • (2010) Biochim. Biophys. Acta , vol.1803 , pp. 520-525
    • Huberts, D.H.1    van der Klei, I.J.2
  • 55
    • 14744284637 scopus 로고    scopus 로고
    • Multifaceted roles of glycolytic enzymes
    • Kim JW, Dang CV. 2005. Multifaceted roles of glycolytic enzymes. Trends Biochem. Sci. 30: 142-150. http://dx. doi. org/10. 1016/j. tibs. 2005. 01. 005.
    • (2005) Trends Biochem. Sci , vol.30 , pp. 142-150
    • Kim, J.W.1    Dang, C.V.2
  • 57
    • 79957567239 scopus 로고    scopus 로고
    • Pyruvate kinase M2 is a PHD3-stimulated coactivator for hypoxia-inducible factor 1
    • Luo W, Hu H, Chang R, Zhong J, Knabel M, O'Meally R, Cole RN, Pandey A, Semenza GL. 2011. Pyruvate kinase M2 is a PHD3-stimulated coactivator for hypoxia-inducible factor 1. Cell 145: 732-744. http://dx. doi. org/10. 1016/j. cell. 2011. 03. 054.
    • (2011) Cell , vol.145 , pp. 732-744
    • Luo, W.1    Hu, H.2    Chang, R.3    Zhong, J.4    Knabel, M.5    O'Meally, R.6    Cole, R.N.7    Pandey, A.8    Semenza, G.L.9
  • 60
    • 84856913587 scopus 로고    scopus 로고
    • Pyruvate kinase M2-specific siRNA induces apoptosis and tumor regression
    • Goldberg MS, Sharp PA. 2012. Pyruvate kinase M2-specific siRNA induces apoptosis and tumor regression. J. Exp. Med. 209: 217-224. http://dx. doi. org/10. 1084/jem. 20111487.
    • (2012) J. Exp. Med , vol.209 , pp. 217-224
    • Goldberg, M.S.1    Sharp, P.A.2
  • 62
    • 77956147151 scopus 로고    scopus 로고
    • Functional analysis, overexpression, and kinetic characterization of pyruvate kinase from methicillinresistant Staphylococcus aureus
    • Zoraghi R, See RH, Gong H, Lian T, Swayze R, Finlay BB, Brunham RC, McMaster WR, Reiner NE. 2010. Functional analysis, overexpression, and kinetic characterization of pyruvate kinase from methicillinresistant Staphylococcus aureus. Biochemistry 49: 7733-7747. http://dx. doi. org/10. 1021/bi100780t.
    • (2010) Biochemistry , vol.49 , pp. 7733-7747
    • Zoraghi, R.1    See, R.H.2    Gong, H.3    Lian, T.4    Swayze, R.5    Finlay, B.B.6    Brunham, R.C.7    McMaster, W.R.8    Reiner, N.E.9
  • 68
    • 79953166468 scopus 로고    scopus 로고
    • Genetic response to metabolic fluctuations: Correlation between central carbon metabolism and DNA replication in Escherichia coli
    • Macia{ogonek}g M, Nowicki D, Janniere L, Szalewska-Pałasz A, We{ogonek}grzyn G. 2011. Genetic response to metabolic fluctuations: correlation between central carbon metabolism and DNA replication in Escherichia coli. Microb. Cell Fact. 10: 19. http://dx. doi. org/10. 1186/1475-2859-10-S1-S19.
    • (2011) Microb. Cell Fact , vol.10 , pp. 19
    • Maciag, M.1    Nowicki, D.2    Janniere, L.3    Szalewska-Pałasz, A.4    Wegrzyn, G.5
  • 69
    • 0033694339 scopus 로고    scopus 로고
    • Midcell Z ring assembly in the absence of entry into the elongation phase of the round of replication in bacteria: Co-ordinating chromosome replication with cell division
    • Regamey A, Harry EJ, Wake RG. 2000. Midcell Z ring assembly in the absence of entry into the elongation phase of the round of replication in bacteria: co-ordinating chromosome replication with cell division. Mol. Microbiol. 38: 423-434. http://dx. doi. org/10. 1046/j. 1365-2958. 2000. 02130. x.
    • (2000) Mol. Microbiol , vol.38 , pp. 423-434
    • Regamey, A.1    Harry, E.J.2    Wake, R.G.3
  • 70
    • 0033011423 scopus 로고    scopus 로고
    • Co-ordinating DNA replication with cell division in bacteria: A link between the early stages of a round of replication and mid-cell Z ring assembly
    • Harry EJ, Rodwell J, Wake RG. 1999. Co-ordinating DNA replication with cell division in bacteria: a link between the early stages of a round of replication and mid-cell Z ring assembly. Mol. Microbiol. 33: 33-40.
    • (1999) Mol. Microbiol , vol.33 , pp. 33-40
    • Harry, E.J.1    Rodwell, J.2    Wake, R.G.3
  • 71
    • 77951585085 scopus 로고    scopus 로고
    • Influence of the nucleoid and the early stages of DNA replication on positioning the division site in Bacillus subtilis
    • Moriya S, Rashid RA, Rodrigues CD, Harry EJ. 2010. Influence of the nucleoid and the early stages of DNA replication on positioning the division site in Bacillus subtilis. Mol. Microbiol. 76: 634-647. http://dx. doi. org/10. 1111/j. 1365-2958. 2010. 07102. x.
    • (2010) Mol. Microbiol , vol.76 , pp. 634-647
    • Moriya, S.1    Rashid, R.A.2    Rodrigues, C.D.3    Harry, E.J.4
  • 74
    • 0020959710 scopus 로고
    • Studies on transformation of Escherichia coli with plasmids
    • Hanahan D. 1983. Studies on transformation of Escherichia coli with plasmids. J. Mol. Biol. 166: 557-580. http://dx. doi. org/10. 1016/S0022-2836(83)80284-8.
    • (1983) J. Mol. Biol , vol.166 , pp. 557-580
    • Hanahan, D.1
  • 75
    • 0023070462 scopus 로고
    • Cloning cDNA into lambda gt10 and gt11
    • In Berger SL, Kimmel AR (ed), Academic Press, San Diego, CA
    • Jendrisak J, Young RA, Engel JD. 1987. Cloning cDNA into lambda gt10 and gt11, p 359-370. In Berger SL, Kimmel AR (ed), Guide to molecular cloning techniques. Academic Press, San Diego, CA.
    • (1987) Guide to molecular cloning techniques , pp. 359-370
    • Jendrisak, J.1    Young, R.A.2    Engel, J.D.3
  • 76
    • 0021150392 scopus 로고
    • Efficient Bacillus subtilis cloning system using bacteriophage vector phi 105J9
    • Errington J. 1984. Efficient Bacillus subtilis cloning system using bacteriophage vector phi 105J9. J. Gen. Microbiol. 130: 2615-2628.
    • (1984) J. Gen. Microbiol , vol.130 , pp. 2615-2628
    • Errington, J.1
  • 77
    • 0001134202 scopus 로고
    • Requirements for transformation in Bacillus subtilis
    • Anagnostopoulos C, 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
  • 78
    • 21244497829 scopus 로고    scopus 로고
    • The ClpX chaperone modulates assembly of the tubulin-like protein FtsZ
    • Weart RB, Nakano S, Lane BE, Zuber P, Levin PA. 2005. The ClpX chaperone modulates assembly of the tubulin-like protein FtsZ. Mol. Microbiol. 57: 238-249. http://dx. doi. org/10. 1111/j. 1365-2958. 2005. 04673. x.
    • (2005) Mol. Microbiol , vol.57 , pp. 238-249
    • Weart, R.B.1    Nakano, S.2    Lane, B.E.3    Zuber, P.4    Levin, P.A.5
  • 80
    • 0023691425 scopus 로고
    • Genetic applications of an inverse polymerase chain reaction
    • Ochman H, Gerber AS, Hartl DL. 1988. Genetic applications of an inverse polymerase chain reaction. Genetics 120: 621-623.
    • (1988) Genetics , vol.120 , pp. 621-623
    • Ochman, H.1    Gerber, A.S.2    Hartl, D.L.3
  • 82
    • 0029019594 scopus 로고
    • Characterization of cell cycle events during the onset of sporulation in Bacillus subtilis
    • Hauser PM, Errington J. 1995. Characterization of cell cycle events during the onset of sporulation in Bacillus subtilis. J. Bacteriol. 177: 3923-3931.
    • (1995) J. Bacteriol , vol.177 , pp. 3923-3931
    • Hauser, P.M.1    Errington, J.2
  • 83
    • 0028264818 scopus 로고
    • Catabolite repression of the Bacillus subtilis xyl operon involves a cis element functional in the context of an unrelated sequence, and glucose exerts additional xylRdependent repression
    • Kraus A, Hueck C, Gärtner D, Hillen W. 1994. Catabolite repression of the Bacillus subtilis xyl operon involves a cis element functional in the context of an unrelated sequence, and glucose exerts additional xylRdependent repression. J. Bacteriol. 176: 1738-1745.
    • (1994) J. Bacteriol , vol.176 , pp. 1738-1745
    • Kraus, A.1    Hueck, C.2    Gärtner, D.3    Hillen, W.4


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