메뉴 건너뛰기




Volumn 196, Issue 4, 2014, Pages 740-753

Defects in the flagellar motor increase synthesis of poly-γ-glutamate in bacillus subtilis

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; MOTA PROTEIN; MOTB PROTEIN; MOTP PROTEIN; MOTS PROTEIN; PGS PROTEIN; POLYGLUTAMIC ACID; UNCLASSIFIED DRUG;

EID: 84892987310     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.01217-13     Document Type: Article
Times cited : (50)

References (116)
  • 1
    • 43849098574 scopus 로고    scopus 로고
    • Coordinating assembly of a bacterial macromolecular machine
    • Chevance FFV, Hughes KT. 2008. Coordinating assembly of a bacterial macromolecular machine. Nat. Rev. Microbiol. 6:455-465. http://dx.doi .org/10.1038/nrmicro1887.
    • (2008) Nat. Rev. Microbiol. , vol.6 , pp. 455-465
    • Chevance, F.F.V.1    Hughes, K.T.2
  • 2
    • 0041673353 scopus 로고    scopus 로고
    • The rotary motor of bacterial flagella
    • Berg HC. 2003. The rotary motor of bacterial flagella. Annu. Rev. Biochem. 72:19-54. http://dx.doi.org/10.1146/annurev.biochem.72.121801.161737.
    • (2003) Annu. Rev. Biochem. , vol.72 , pp. 19-54
    • Berg, H.C.1
  • 3
    • 0024295536 scopus 로고
    • Restoration of torque in defective flagellar motors
    • Blair DF, Berg HC. 1988. Restoration of torque in defective flagellar motors. Science 242:1678-1681. http://dx.doi.org/10.1126/science.2849208.
    • (1988) Science , vol.242 , pp. 1678-1681
    • Blair, D.F.1    Berg, H.C.2
  • 4
    • 0023750050 scopus 로고
    • Effects of mot gene expression on the structure of the flagellar motor
    • Khan S, Dapice M, Reese TS. 1988. Effects of mot gene expression on the structure of the flagellar motor. J. Mol. Biol. 202:575-584. http://dx.doi .org/10.1016/0022-2836(88)90287-2.
    • (1988) J. Mol. Biol. , vol.202 , pp. 575-584
    • Khan, S.1    Dapice, M.2    Reese, T.S.3
  • 5
    • 0027365641 scopus 로고
    • Torque generated by the flagellar motor of Escherichia coli
    • Berg HC, Turner L. 1993. Torque generated by the flagellar motor of Escherichia coli. Biophys. J. 65:2201-2216. http://dx.doi.org/10.1016 /S0006-3495(93)81278-5.
    • (1993) Biophys. J. , vol.65 , pp. 2201-2216
    • Berg, H.C.1    Turner, L.2
  • 6
    • 0041806636 scopus 로고    scopus 로고
    • The speed of the flagellar rotary motor of Escherichia coli varies linearly with proton motive force
    • Gabel CV, Berg HC. 2003. The speed of the flagellar rotary motor of Escherichia coli varies linearly with proton motive force. Proc. Natl. Acad. Sci. U. S. A. 100:8748-8751. http://dx.doi.org/10.1073/pnas.1533 395100.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 8748-8751
    • Gabel, C.V.1    Berg, H.C.2
  • 7
    • 33744476417 scopus 로고    scopus 로고
    • The maximum number of torque-generating units in the flagellar motor of Escherichia coli is at least 11
    • Reid SW, Leake MC, Chandler JH, Lo CJ, Armitage JP, Berry RM. 2006. The maximum number of torque-generating units in the flagellar motor of Escherichia coli is at least 11. Proc. Natl. Acad. Sci. U. S. A. 103:8066-8071. http://dx.doi.org/10.1073/pnas.0509932103.
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 8066-8071
    • Reid, S.W.1    Leake, M.C.2    Chandler, J.H.3    Lo, C.J.4    Armitage, J.P.5    Berry, R.M.6
  • 8
    • 0021280816 scopus 로고
    • Successive incorporation of force generating units in the bacterial rotary motor
    • Block SM, Berg HC. 1984. Successive incorporation of force generating units in the bacterial rotary motor. Nature 309:470-472. http://dx.doi .org/10.1038/309470a0.
    • (1984) Nature , vol.309 , pp. 470-472
    • Block, S.M.1    Berg, H.C.2
  • 9
    • 0347357933 scopus 로고    scopus 로고
    • Solubilization and purification of the MotA/ MotB complex of Escherichia coli
    • Kojima S, Blair DF. 2004. Solubilization and purification of the MotA/ MotB complex of Escherichia coli. Biochemistry 43:26-34. http://dx.doi .org/10.1021/bi035405l.
    • (2004) Biochemistry , vol.43 , pp. 26-34
    • Kojima, S.1    Blair, D.F.2
  • 10
    • 0024286468 scopus 로고
    • Bacterial motility: membrane topology of the Escherichia coli MotB protein
    • Chun SY, Parkinson JS. 1988. Bacterial motility: membrane topology of the Escherichia coli MotB protein. Science 239:276-278. http://dx.doi .org/10.1126/science.2447650.
    • (1988) Science , vol.239 , pp. 276-278
    • Chun, S.Y.1    Parkinson, J.S.2
  • 11
    • 0031944413 scopus 로고    scopus 로고
    • Function of protonatable residues in the flagellar motor of Escherichia coli: a critical role for Asp 32 of MotB
    • Zhou J, Sharp Tang LL, Lloyd HL SA, Billings S, Braun TY, Blair DF. 1998. Function of protonatable residues in the flagellar motor of Escherichia coli: a critical role for Asp 32 of MotB. J. Bacteriol. 180:2729-2735.
    • (1998) J. Bacteriol , vol.180 , pp. 2729-2735
    • Zhou, J.1    Sharp Tang, L.L.2    Lloyd, H.L.S.A.3    Billings, S.4    Braun, T.Y.5    Blair, D.F.6
  • 12
    • 70350152604 scopus 로고    scopus 로고
    • Stator assembly and activation mechanism of the flagella motor by the periplasmic region of MotB
    • Kojima S, Imada K, Sakuma M, Sudo Y, Kojima C, Minamino T, Homma M, Namba K. 2009. Stator assembly and activation mechanism of the flagella motor by the periplasmic region of MotB. Mol. Microbiol. 73:710-718. http://dx.doi.org/10.1111/j.1365-2958.2009.06802.x.
    • (2009) Mol. Microbiol. , vol.73 , pp. 710-718
    • Kojima, S.1    Imada, K.2    Sakuma, M.3    Sudo, Y.4    Kojima, C.5    Minamino, T.6    Homma, M.7    Namba, K.8
  • 13
    • 0029165325 scopus 로고
    • Membrane topology of the MotA protein of Escherichia coli
    • Zhou J, Fazzio RT, Blair DF. 1995. Membrane topology of the MotA protein of Escherichia coli. J. Mol. Biol. 251:237-242. http://dx.doi.org/10 .1006/jmbi.1995.0431.
    • (1995) J. Mol. Biol. , vol.251 , pp. 237-242
    • Zhou, J.1    Fazzio, R.T.2    Blair, D.F.3
  • 14
    • 0035980267 scopus 로고    scopus 로고
    • Conformational change in the stator of the bacterial flagellar motor
    • Kojima S, Blair DF. 2001. Conformational change in the stator of the bacterial flagellar motor. Biochemistry 40:13041-13050. http://dx.doi .org/10.1021/bi011263o.
    • (2001) Biochemistry , vol.40 , pp. 13041-13050
    • Kojima, S.1    Blair, D.F.2
  • 16
    • 77955924240 scopus 로고    scopus 로고
    • Structure of the torque ring of the flagellar motor and the molecular basis for rotational switching
    • Lee LK, Ginsburg MA, Crovace C, Donohoe M, Stock D. 2010. Structure of the torque ring of the flagellar motor and the molecular basis for rotational switching. Nature 466:996-1000. http://dx.doi.org/10 .1038/nature09300.
    • (2010) Nature , vol.466 , pp. 996-1000
    • Lee, L.K.1    Ginsburg, M.A.2    Crovace, C.3    Donohoe, M.4    Stock, D.5
  • 17
    • 0030776508 scopus 로고    scopus 로고
    • Residues of the cytoplasmic domain of MotA essential for torque generation in the bacterial flagellar motor
    • Zhou J, Blair DF. 1997. Residues of the cytoplasmic domain of MotA essential for torque generation in the bacterial flagellar motor. J. Mol. Biol. 273:428-439. http://dx.doi.org/10.1006/jmbi.1997.1316.
    • (1997) J. Mol. Biol. , vol.273 , pp. 428-439
    • Zhou, J.1    Blair, D.F.2
  • 18
    • 0032568636 scopus 로고    scopus 로고
    • Electrostatic interactions between rotor and stator in the bacterial flagellar motor
    • Zhou J, Lloyd SA, Blair DF. 1998. Electrostatic interactions between rotor and stator in the bacterial flagellar motor. Proc. Natl. Acad. Sci. U. S. A. 95:6436-6441. http://dx.doi.org/10.1073/pnas.95.11.6436.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 6436-6441
    • Zhou, J.1    Lloyd, S.A.2    Blair, D.F.3
  • 19
    • 33745289074 scopus 로고    scopus 로고
    • Poly-gamma-glutamate in bacteria
    • Candela T, Fouet A. 2006. Poly-gamma-glutamate in bacteria. Mol. Microbiol. 60:1091-1098. http://dx.doi.org/10.1111/j.1365-2958.2006 .05179.x.
    • (2006) Mol. Microbiol. , vol.60 , pp. 1091-1098
    • Candela, T.1    Fouet, A.2
  • 20
    • 0001432880 scopus 로고
    • The formation of extracellular d(-)-glutamic acid polypeptide by Bacillus subtilis
    • Bovarnick M. 1942. The formation of extracellular d(-)-glutamic acid polypeptide by Bacillus subtilis. J. Biol. Chem. 145:415-424.
    • (1942) J. Biol. Chem , vol.145 , pp. 415-424
    • Bovarnick, M.1
  • 21
    • 0000885284 scopus 로고
    • The capsular substance of Bacillus anthracis
    • Hanby WE, Rydon HN. 1946. The capsular substance of Bacillus anthracis. Biochem. J. 40:297-309.
    • (1946) Biochem. J , vol.40 , pp. 297-309
    • Hanby, W.E.1    Rydon, H.N.2
  • 22
    • 22644436621 scopus 로고    scopus 로고
    • Bacillus anthracis CapD, belonging to the γ-glutamyltranspeptidase family, is required for the covalent anchoring of capsule to peptidoglycan
    • Candela T, Fouet A. 2005. Bacillus anthracis CapD, belonging to the γ-glutamyltranspeptidase family, is required for the covalent anchoring of capsule to peptidoglycan. Mol. Microbiol. 57:717-726. http://dx.doi .org/10.1111/j.1365-2958.2005.04718.x.
    • (2005) Mol. Microbiol. , vol.57 , pp. 717-726
    • Candela, T.1    Fouet, A.2
  • 23
    • 0024595710 scopus 로고
    • Molecular characterization and protein analysis of the cap region, which is essential for encapsulation in Bacillus anthracis
    • Makino SI, Uchida I, Terakado N, Sasakawa C, Yoshikawa M. 1989. Molecular characterization and protein analysis of the cap region, which is essential for encapsulation in Bacillus anthracis. J. Bacteriol. 171:722-730.
    • (1989) J. Bacteriol , vol.171 , pp. 722-730
    • Makino, S.I.1    Uchida, I.2    Terakado, N.3    Sasakawa, C.4    Yoshikawa, M.5
  • 24
    • 0033575870 scopus 로고    scopus 로고
    • A poly-γ-glutamate synthetic system of Bacillus subtilis IFO 3336: gene cloning and biochemical analysis of poly-γ-glutamate produced by Escherichia coli clone cells
    • Ashiuchi M, Soda K, Misono H. 1999. A poly-γ-glutamate synthetic system of Bacillus subtilis IFO 3336: gene cloning and biochemical analysis of poly-γ-glutamate produced by Escherichia coli clone cells. Biochem. Biophys. Res. Commun. 263:6-12. http://dx.doi.org/10.1006 /bbrc.1999.1298.
    • (1999) Biochem. Biophys. Res. Commun. , vol.263 , pp. 6-12
    • Ashiuchi, M.1    Soda, K.2    Misono, H.3
  • 25
    • 0036134960 scopus 로고    scopus 로고
    • Characterization of the Bacillus subtilis ywsC gene, involved in γ-polyglutamic acid production
    • Urushibata Y, Tokuyama S, Tahara Y. 2002. Characterization of the Bacillus subtilis ywsC gene, involved in γ-polyglutamic acid production. J. Bacteriol. 184:337-343. http://dx.doi.org/10.1128/JB.184.2.337-343 .2002.
    • (2002) J. Bacteriol. , vol.184 , pp. 337-343
    • Urushibata, Y.1    Tokuyama, S.2    Tahara, Y.3
  • 26
    • 67049155609 scopus 로고    scopus 로고
    • Expression of pgsB encoding the poly gamma-DL-glutamate of Bacillus subtilis natto
    • Kimura K, Tran LSP, Do TH, Itoh Y. 2009. Expression of pgsB encoding the poly gamma-DL-glutamate of Bacillus subtilis natto. Biosci. Biotechnol. Biochem. 73:1149-1155. http://dx.doi.org/10.1271/bbb.80913.
    • (2009) Biosci. Biotechnol. Biochem. , vol.73 , pp. 1149-1155
    • Kimura, K.1    Tran, L.S.P.2    Do, T.H.3    Itoh, Y.4
  • 27
    • 0037379280 scopus 로고    scopus 로고
    • Characterization of the Bacillus subtilis ywtD gene, whose product is involved inγ-polyglutamic acid degradation
    • Suzuki T, Tahara Y. 2003. Characterization of the Bacillus subtilis ywtD gene, whose product is involved inγ-polyglutamic acid degradation. J. Bacteriol. 185: 2379-2382. http://dx.doi.org/10.1128/JB.185.7.2379-2382.2003.
    • (2003) J. Bacteriol. , vol.185 , pp. 2379-2382
    • Suzuki, T.1    Tahara, Y.2
  • 28
    • 33748459631 scopus 로고    scopus 로고
    • Novel poly-γ-glutamate-processing enzyme catalyzing γ-glutamyl DDamidohydrolysis
    • Ashiuchi M, Nakamura H, Yamamoto M, Misono H. 2006. Novel poly-γ-glutamate-processing enzyme catalyzing γ-glutamyl DDamidohydrolysis. J. Biosci. Bioeng. 1:60-65. http://dx.doi.org/10.1263 /jbb.102.60.
    • (2006) J. Biosci. Bioeng. , vol.1 , pp. 60-65
    • Ashiuchi, M.1    Nakamura, H.2    Yamamoto, M.3    Misono, H.4
  • 29
    • 33644857535 scopus 로고    scopus 로고
    • In vivo random mutagenesis of Bacillus subtilis by use of TnYLB-1, a mariner-based transposon
    • Le Breton Y, Mohapatra NP, Haldenwang WG. 2006. In vivo random mutagenesis of Bacillus subtilis by use of TnYLB-1, a mariner-based transposon. Appl. Environ. Microbiol. 72:327-333. http://dx.doi.org/10 .1128/AEM.72.1.327-333.2006.
    • (2006) Appl. Environ. Microbiol. , vol.72 , pp. 327-333
    • Le Breton, Y.1    Mohapatra, N.P.2    Haldenwang, W.G.3
  • 30
    • 0033813157 scopus 로고    scopus 로고
    • Divergent structure of the ComQXPA quorum-sensing components: molecular basis of strain-specific communication mechanism in Bacillus subtilis
    • Tran LSP, Nagai T, Itoh Y. 2000. Divergent structure of the ComQXPA quorum-sensing components: molecular basis of strain-specific communication mechanism in Bacillus subtilis. Mol. Microbiol. 37:1159-1171. http://dx.doi.org/10.1046/j.1365-2958.2000.02069.x.
    • (2000) Mol. Microbiol. , vol.37 , pp. 1159-1171
    • Tran, L.S.P.1    Nagai, T.2    Itoh, Y.3
  • 31
    • 0016352815 scopus 로고
    • Transduction in Bacillus subtilis by Bacteriophage SPP1
    • Yasbin RE, Young FE. 1974. Transduction in Bacillus subtilis by Bacteriophage SPP1. J. Virol. 14:1343-1348.
    • (1974) J. Virol , vol.14 , pp. 1343-1348
    • Yasbin, R.E.1    Young, F.E.2
  • 32
    • 55349109965 scopus 로고    scopus 로고
    • MinJ (YvjD) is a topological determinant of cell division in Bacillus subtilis
    • Patrick JE, Kearns DB. 2008. MinJ (YvjD) is a topological determinant of cell division in Bacillus subtilis. Mol. Microbiol. 70:1166-1179. http: //dx.doi.org/10.1111/j.1365-2958.2008.06469.x.
    • (2008) Mol. Microbiol. , vol.70 , pp. 1166-1179
    • Patrick, J.E.1    Kearns, D.B.2
  • 33
    • 0037462540 scopus 로고    scopus 로고
    • RacA, a bacterial protein that anchors chromosomes to cell poles
    • Ben-Yehuda S, Rudner DZ, Losick R. 2003. RacA, a bacterial protein that anchors chromosomes to cell poles. Science 299:532-536. http://dx .doi.org/10.1126/science.1079914.
    • (2003) Science , vol.299 , pp. 532-536
    • Ben-Yehuda, S.1    Rudner, D.Z.2    Losick, R.3
  • 34
    • 0025020272 scopus 로고
    • The spoIIJ gene, which regulates early developmental steps in Bacillus subtilis, belongs to a class of environmentally responsive genes
    • Antoniewski C, Savelli B, Stragier P. 1990. The spoIIJ gene, which regulates early developmental steps in Bacillus subtilis, belongs to a class of environmentally responsive genes. J. Bacteriol. 172:86-93.
    • (1990) J. Bacteriol , vol.172 , pp. 86-93
    • Antoniewski, C.1    Savelli, B.2    Stragier, P.3
  • 35
    • 0029590029 scopus 로고
    • Antibiotic resistance cassettes for Bacillus subtilis
    • Guérout-Fleury AM, Shazand K, Frandsen N, Stragier P. 1995. Antibiotic resistance cassettes for Bacillus subtilis. Gene 167:335-336. http: //dx.doi.org/10.1016/0378-1119(95)00652-4.
    • (1995) Gene , vol.167 , pp. 335-336
    • Guérout-Fleury, A.M.1    Shazand, K.2    Frandsen, N.3    Stragier, P.4
  • 36
    • 0029871347 scopus 로고    scopus 로고
    • PCR-synthesis of marker cassettes with long flanking homology regions for gene disruptions in S
    • Wach A. 1996. PCR-synthesis of marker cassettes with long flanking homology regions for gene disruptions in S. cerevisiae. Yeast 12:259-265.
    • (1996) cerevisiae Yeast , vol.12 , pp. 259-265
    • Wach, A.1
  • 37
    • 0026629441 scopus 로고
    • An operon of Bacillus subtilis motility genes transcribed by the σD form of RNA polymerase
    • Mirel DB, Lustre VM, Chamberlin MJ. 1992. An operon of Bacillus subtilis motility genes transcribed by the σD form of RNA polymerase. J. Bacteriol. 174:4197-4204.
    • (1992) J. Bacteriol , vol.174 , pp. 4197-4204
    • Mirel, D.B.1    Lustre, V.M.2    Chamberlin, M.J.3
  • 38
    • 4544233498 scopus 로고    scopus 로고
    • The complex flagellar torque generator of Pseudomonas aeruginosa
    • Doyle TB, Hawkins AC, McCarter LL. 2004. The complex flagellar torque generator of Pseudomonas aeruginosa. J. Bacteriol. 186:6341-6350. http://dx.doi.org/10.1128/JB.186.19.6341-6350.2004.
    • (2004) J. Bacteriol. , vol.186 , pp. 6341-6350
    • Doyle, T.B.1    Hawkins, A.C.2    McCarter, L.L.3
  • 39
    • 4344703019 scopus 로고    scopus 로고
    • MotPS is the stator-force generator for motility of alkaliphilic Bacillus, and its homologue is a second functional Mot in Bacillus subtilis
    • Ito M, Hicks DB, Henkin TM, Guffanti AA, Powers BD, Zvi L, Uematsu K, Krulwich TA. 2004. MotPS is the stator-force generator for motility of alkaliphilic Bacillus, and its homologue is a second functional Mot in Bacillus subtilis. Mol. Microbiol. 53:1035-1049. http://dx.doi.org /10.1111/j.1365-2958.2004.04173.x.
    • (2004) Mol. Microbiol. , vol.53 , pp. 1035-1049
    • Ito, M.1    Hicks, D.B.2    Henkin, T.M.3    Guffanti, A.A.4    Powers, B.D.5    Zvi, L.6    Uematsu, K.7    Krulwich, T.A.8
  • 40
    • 11844277106 scopus 로고    scopus 로고
    • Evidence for two flagellar stators and their role in the motility of Pseudomonas aeruginosa
    • Toutain CM, Zegans ME, O'Toole GA. 2005. Evidence for two flagellar stators and their role in the motility of Pseudomonas aeruginosa. J. Bacteriol. 187:771-777. http://dx.doi.org/10.1128/JB.187.2.771-777.2005.
    • (2005) J. Bacteriol. , vol.187 , pp. 771-777
    • Toutain, C.M.1    Zegans, M.E.2    O'Toole, G.A.3
  • 41
    • 23944443794 scopus 로고    scopus 로고
    • Properties of motility in Bacillus subtilis powered by the H-coupled MotAB flagellar stator, Na-coupled MotPS or hybrid stators MotAS or MotPB
    • Ito M, Terahara N, Fujinami S, Krulwich TA. 2005. Properties of motility in Bacillus subtilis powered by the H-coupled MotAB flagellar stator, Na-coupled MotPS or hybrid stators MotAS or MotPB. J. Mol. Biol. 352:396-408. http://dx.doi.org/10.1016/j.jmb.2005.07.030.
    • (2005) J. Mol. Biol. , vol.352 , pp. 396-408
    • Ito, M.1    Terahara, N.2    Fujinami, S.3    Krulwich, T.A.4
  • 42
    • 0027289507 scopus 로고
    • Sequence and analysis of the genetic locus responsible for surfactin synthesis in Bacillus subtilis
    • Cosmina P, Rodriguez F, de Ferra F, Grandi G, Perego M, Venema G, van Sinderen D. 1993. Sequence and analysis of the genetic locus responsible for surfactin synthesis in Bacillus subtilis. Mol. Microbiol. 8:821-831. http://dx.doi.org/10.1111/j.1365-2958.1993.tb01629.x.
    • (1993) Mol. Microbiol. , vol.8 , pp. 821-831
    • Cosmina, P.1    Rodriguez, F.2    de Ferra, F.3    Grandi, G.4    Perego, M.5    Venema, G.6    van Sinderen, D.7
  • 44
    • 33645085864 scopus 로고    scopus 로고
    • A major protein component of the Bacillus subtilis biofilm matrix
    • Branda SS, Chu F, Kearns DB, Losick R, Kolter R. 2006. A major protein component of the Bacillus subtilis biofilm matrix. Mol. Microbiol. 59: 1229-1238. http://dx.doi.org/10.1111/j.1365-2958.2005.05020.x.
    • (2006) Mol. Microbiol. , vol.59 , pp. 1229-1238
    • Branda, S.S.1    Chu, F.2    Kearns, D.B.3    Losick, R.4    Kolter, R.5
  • 45
    • 13444292348 scopus 로고    scopus 로고
    • A master regulator for biofilm formation by Bacillus subtilis
    • Kearns DB, Chu F, Branda SS, Kolter R, Losick R. 2005. A master regulator for biofilm formation by Bacillus subtilis. Mol. Microbiol. 55: 739-749. http://dx.doi.org/10.1111/j.1365-2958.2004.04440.x.
    • (2005) Mol. Microbiol. , vol.55 , pp. 739-749
    • Kearns, D.B.1    Chu, F.2    Branda, S.S.3    Kolter, R.4    Losick, R.5
  • 46
    • 84862760267 scopus 로고    scopus 로고
    • BslA (YuaB) forms a hydrophobic layer on the surface of Bacillus subtilis biofilms
    • Kobayashi K, Iwano M. 2012. BslA (YuaB) forms a hydrophobic layer on the surface of Bacillus subtilis biofilms. Mol. Microbiol. 85:51-66. http://dx.doi.org/10.1111/j.1365-2958.2012.08094.x.
    • (2012) Mol. Microbiol. , vol.85 , pp. 51-66
    • Kobayashi, K.1    Iwano, M.2
  • 48
    • 84884700405 scopus 로고    scopus 로고
    • A mechanical signal transmitted by the flagellum controls signaling in Bacillus subtilis
    • Cairns LS, Marlow VL, Bissett E, Ostrowski A, Stanley-Wall NR. 2013. A mechanical signal transmitted by the flagellum controls signaling in Bacillus subtilis. Mol. Microbiol. 90:6-21. http://dx.doi.org/10.1111 /mmi.12342.
    • (2013) Mol. Microbiol. , vol.90 , pp. 6-21
    • Cairns, L.S.1    Marlow, V.L.2    Bissett, E.3    Ostrowski, A.4    Stanley-Wall, N.R.5
  • 49
    • 0028071261 scopus 로고
    • Coupling of flagellin gene transcription to flagellar assembly in Bacillus subtilis
    • Barilla D, Caramori T, Galizzi A. 1994. Coupling of flagellin gene transcription to flagellar assembly in Bacillus subtilis. J. Bacteriol. 176: 4558-4564.
    • (1994) J. Bacteriol , vol.176 , pp. 4558-4564
    • Barilla, D.1    Caramori, T.2    Galizzi, A.3
  • 50
    • 0029118564 scopus 로고
    • Functional analysis of the flagellar genes in the fliD operon of Salmonella typhimurium
    • Yokoseki T, Kutsukake K, Ohnishi K, Iino T. 1995. Functional analysis of the flagellar genes in the fliD operon of Salmonella typhimurium. Microbiology 141:1715-1722. http://dx.doi.org/10.1099/13500872-141-7-1715.
    • (1995) Microbiology , vol.141 , pp. 1715-1722
    • Yokoseki, T.1    Kutsukake, K.2    Ohnishi, K.3    Iino, T.4
  • 51
    • 0030596502 scopus 로고    scopus 로고
    • Self-assembly of the filament capping protein, FliD, of bacterial flagella into an annular structure
    • Ikeda T, Oosawa K, Hotani H. 1996. Self-assembly of the filament capping protein, FliD, of bacterial flagella into an annular structure. J. Mol. Biol. 259:679-686. http://dx.doi.org/10.1006/jmbi.1996.0349.
    • (1996) J. Mol. Biol. , vol.259 , pp. 679-686
    • Ikeda, T.1    Oosawa, K.2    Hotani, H.3
  • 52
    • 84872168146 scopus 로고    scopus 로고
    • FliW and FliS function independently to control cytoplasmic flagellin levels in Bacillus subtilis
    • Mukherjee S, Babitzke P, Kearns DB. 2013. FliW and FliS function independently to control cytoplasmic flagellin levels in Bacillus subtilis. J. Bacteriol. 195:297-306. http://dx.doi.org/10.1128/JB.01654-12.
    • (2013) J. Bacteriol. , vol.195 , pp. 297-306
    • Mukherjee, S.1    Babitzke, P.2    Kearns, D.B.3
  • 53
    • 0032906245 scopus 로고    scopus 로고
    • Substrate-specific binding of hook-associated proteins bu FlgN and FliT, putative chaperones for flagellum assembly
    • Fraser GM, Bennett JCQ, Hughes C. 1999. Substrate-specific binding of hook-associated proteins bu FlgN and FliT, putative chaperones for flagellum assembly. Mol. Microbiol. 32:569-580. http://dx.doi.org/10 .1046/j.1365-2958.1999.01372.x.
    • (1999) Mol. Microbiol. , vol.32 , pp. 569-580
    • Fraser, G.M.1    Bennett, J.C.Q.2    Hughes, C.3
  • 54
    • 0035133472 scopus 로고    scopus 로고
    • Substrate complexes and domain organization of the Salmonella flagellar export chaperones FlgN and FliT
    • Bennett JCQ, Thomas J, Fraser GM, Hughes C. 2001. Substrate complexes and domain organization of the Salmonella flagellar export chaperones FlgN and FliT. Mol. Microbiol. 39:781-791. http://dx.doi.org/10 .1046/j.1365-2958.2001.02268.x.
    • (2001) Mol. Microbiol. , vol.39 , pp. 781-791
    • Bennett, J.C.Q.1    Thomas, J.2    Fraser, G.M.3    Hughes, C.4
  • 55
    • 0021362454 scopus 로고
    • Hook-associated proteins essential for flagellar filament formation in Salmonella typhimurium
    • Homma M, Kutsukake K, Iino T, Yamaguchi S. 1984. Hook-associated proteins essential for flagellar filament formation in Salmonella typhimurium. J. Bacteriol. 157:100-108.
    • (1984) J. Bacteriol , vol.157 , pp. 100-108
    • Homma, M.1    Kutsukake, K.2    Iino, T.3    Yamaguchi, S.4
  • 56
    • 0021159373 scopus 로고
    • Excretion of unassembled flagellin by Salmonella typhimurium mutants deficient in hookassociated proteins
    • Homma M, Fukita H, Yamaguchi S, Iino T. 1984. Excretion of unassembled flagellin by Salmonella typhimurium mutants deficient in hookassociated proteins. J. Bacteriol. 159:1056-1059.
    • (1984) J. Bacteriol , vol.159 , pp. 1056-1059
    • Homma, M.1    Fukita, H.2    Yamaguchi, S.3    Iino, T.4
  • 57
    • 0027244508 scopus 로고
    • Flagellar growth in a filamentless Salmonella fliD mutant supplemented with purified hook-associated protein 2
    • Ikeda T, Yamaguchi S, Hotani H. 1993. Flagellar growth in a filamentless Salmonella fliD mutant supplemented with purified hook-associated protein 2. J. Biochem. 114:39-44.
    • (1993) J. Biochem , vol.114 , pp. 39-44
    • Ikeda, T.1    Yamaguchi, S.2    Hotani, H.3
  • 58
    • 0023663101 scopus 로고
    • Selective removal of transcription-blocking DNA damage from the transcribed strand of the mammalian DHFR gene
    • Mellon I, Spivak G, Hanawalt PC. 1987. Selective removal of transcription-blocking DNA damage from the transcribed strand of the mammalian DHFR gene. Cell 51:241-249. http://dx.doi.org/10.1016/0092-8674(87)90151-6.
    • (1987) Cell , vol.51 , pp. 241-249
    • Mellon, I.1    Spivak, G.2    Hanawalt, P.C.3
  • 59
    • 0024426244 scopus 로고
    • Induction of the Escherichia coli lactose operon selectively increases repair of its transcribed DNA strand
    • Mellon I, Hanawalt PC. 1989. Induction of the Escherichia coli lactose operon selectively increases repair of its transcribed DNA strand. Nature 342:95-98. http://dx.doi.org/10.1038/342095a0.
    • (1989) Nature , vol.342 , pp. 95-98
    • Mellon, I.1    Hanawalt, P.C.2
  • 60
    • 0026354699 scopus 로고
    • Escherichia coli mfd mutant deficient in "mutation frequency decline" lacks strand-specific repair: in vitro complementation with purified coupling factor
    • Selby CP, Witkin EM, Sancar A. 1991. Escherichia coli mfd mutant deficient in "mutation frequency decline" lacks strand-specific repair: in vitro complementation with purified coupling factor. Proc. Natl. Acad. Sci. U. S. A. 88:11574-11578. http://dx.doi.org/10.1073/pnas.88.24 .11574.
    • (1991) Proc. Natl. Acad. Sci. U. S. A. , vol.88 , pp. 11574-11578
    • Selby, C.P.1    Witkin, E.M.2    Sancar, A.3
  • 61
    • 0026472384 scopus 로고
    • Transcriptionrepair coupling determines the strandedness of ultraviolet mutagenesis in Escherichia coli
    • Oller AR, Fijalkowska IJ, Dunn RL, Schaaper RM. 1992. Transcriptionrepair coupling determines the strandedness of ultraviolet mutagenesis in Escherichia coli. Proc. Natl. Acad. Sci. U. S. A. 89:11036-11040. http: //dx.doi.org/10.1073/pnas.89.22.11036.
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 11036-11040
    • Oller, A.R.1    Fijalkowska, I.J.2    Dunn, R.L.3    Schaaper, R.M.4
  • 62
    • 34347332162 scopus 로고    scopus 로고
    • The molecular mechanism of transcription-coupled DNA repair
    • Savery NJ. 2007. The molecular mechanism of transcription-coupled DNA repair. Trends Microbiol. 15:326-333. http://dx.doi.org/10.1016/j .tim.2007.05.005.
    • (2007) Trends Microbiol. , vol.15 , pp. 326-333
    • Savery, N.J.1
  • 63
    • 0027905034 scopus 로고
    • Molecular mechanism of transcription-repair coupling
    • Selby CP, Sancar A. 1993. Molecular mechanism of transcription-repair coupling. Science 260:53-57. http://dx.doi.org/10.1126/science.8465200.
    • (1993) Science , vol.260 , pp. 53-57
    • Selby, C.P.1    Sancar, A.2
  • 64
    • 0028969976 scopus 로고
    • Structure and function of transcription-repair coupling factor
    • Selby CP, Sancar A. 1995. Structure and function of transcription-repair coupling factor. J. Biol. Chem. 270:4882-4889. http://dx.doi.org/10 .1074/jbc.270.9.4882.
    • (1995) J. Biol. Chem. , vol.270 , pp. 4882-4889
    • Selby, C.P.1    Sancar, A.2
  • 65
    • 0029939231 scopus 로고    scopus 로고
    • The Mfd protein of Bacillus subtilis 168 is involved in both transcription-coupled DNA repair and DNA recombination
    • Ayora S, Rojo F, Ogasawara N, Nakai S, Alonso JC. 1996. The Mfd protein of Bacillus subtilis 168 is involved in both transcription-coupled DNA repair and DNA recombination. J. Mol. Biol. 256:301-318. http: //dx.doi.org/10.1006/jmbi.1996.0087.
    • (1996) J. Mol. Biol. , vol.256 , pp. 301-318
    • Ayora, S.1    Rojo, F.2    Ogasawara, N.3    Nakai, S.4    Alonso, J.C.5
  • 66
    • 0037077154 scopus 로고    scopus 로고
    • E. coli transcription repair coupling factor (Mfd protein) rescues arrested complexes by promoting forward translocation
    • Park JS, Marr MT, Roberts JW. 2002. E. coli transcription repair coupling factor (Mfd protein) rescues arrested complexes by promoting forward translocation. Cell 109:757-767. http://dx.doi.org/10.1016/S0092-8674(02)00769-9.
    • (2002) Cell , vol.109 , pp. 757-767
    • Park, J.S.1    Marr, M.T.2    Roberts, J.W.3
  • 67
    • 22544464455 scopus 로고    scopus 로고
    • RNA polymerase modulator and DNA repair activities resolve conflicts between DNA replication and transcription
    • Trautinger BW, Jaktaji RP, Rusakova E, Lloyd RG. 2005. RNA polymerase modulator and DNA repair activities resolve conflicts between DNA replication and transcription. Cell 19:247-258. http://dx.doi.org /10.1016/j.molcel.2005.06.004.
    • (2005) Cell , vol.19 , pp. 247-258
    • Trautinger, B.W.1    Jaktaji, R.P.2    Rusakova, E.3    Lloyd, R.G.4
  • 68
    • 75749150810 scopus 로고    scopus 로고
    • Direct restart of a replication fork stalled by a head-on RNA polymerase
    • Pomerantz RT, O'Donnell M. 2010. Direct restart of a replication fork stalled by a head-on RNA polymerase. Science 327:590-592. http://dx .doi.org/10.1126/science.1179595.
    • (2010) Science , vol.327 , pp. 590-592
    • Pomerantz, R.T.1    O'Donnell, M.2
  • 69
    • 0031779321 scopus 로고    scopus 로고
    • Transcriptionrepair coupling factor is involved in carbon catabolite repression of the Bacillus subtilis hut and gnt operons
    • Zalieckas JM, Wray LV, Jr, Ferson AE, Fisher LH. 1998. Transcriptionrepair coupling factor is involved in carbon catabolite repression of the Bacillus subtilis hut and gnt operons. Mol. Microbiol. 27:1031-1038. http: //dx.doi.org/10.1046/j.1365-2958.1998.00751.x.
    • (1998) Mol. Microbiol. , vol.27 , pp. 1031-1038
    • Zalieckas, J.M.1    Wray, L.V.2    Ferson, A.E.3    Fisher, L.H.4
  • 70
    • 80051668431 scopus 로고    scopus 로고
    • Roadblock repression of transcription by Bacillus subtilis CodY
    • Belitsky BR, Sonenshein AL. 2011. Roadblock repression of transcription by Bacillus subtilis CodY. J. Mol. Biol. 411:729-743. http://dx.doi .org/10.1016/j.jmb.2011.06.012.
    • (2011) J. Mol. Biol. , vol.411 , pp. 729-743
    • Belitsky, B.R.1    Sonenshein, A.L.2
  • 71
    • 0035336771 scopus 로고    scopus 로고
    • Bacillus subtilis CodY represses early-stationary-phase genes by sensing GTP levels
    • Ratnayake-Lecamwasam M, Serror P, Wong KW, Sonenshein AL. 2001. Bacillus subtilis CodY represses early-stationary-phase genes by sensing GTP levels. Genes Dev. 15:1093-1103. http://dx.doi.org/10.1101 /gad.874201.
    • (2001) Genes Dev. , vol.15 , pp. 1093-1103
    • Ratnayake-Lecamwasam, M.1    Serror, P.2    Wong, K.W.3    Sonenshein, A.L.4
  • 72
    • 0037336206 scopus 로고    scopus 로고
    • Additional targets of the Bacillus subtilis global regulator CodY identified by chromatin immunoprecipitation and genome-wide transcript analysis
    • Molle V, Nakaura Y, Shivers RP, Yamaguchi H, Losick R, Fujita Y, Sonenshein A. 2003. Additional targets of the Bacillus subtilis global regulator CodY identified by chromatin immunoprecipitation and genome-wide transcript analysis. J. Bacteriol. 185:1911-1922. http://dx.doi .org/10.1128/JB.185.6.1911-1922.2003.
    • (2003) J. Bacteriol. , vol.185 , pp. 1911-1922
    • Molle, V.1    Nakaura, Y.2    Shivers, R.P.3    Yamaguchi, H.4    Losick, R.5    Fujita, Y.6    Sonenshein, A.7
  • 73
    • 3242880574 scopus 로고    scopus 로고
    • Activation of the Bacillus subtilis global regulator CodY by direct interaction with branched-chain amino acids
    • Shivers RP, Sonenshein AL. 2004. Activation of the Bacillus subtilis global regulator CodY by direct interaction with branched-chain amino acids. Mol. Microbiol. 53:599-611. http://dx.doi.org/10.1111/j.1365-2958.2004.04135.x.
    • (2004) Mol. Microbiol. , vol.53 , pp. 599-611
    • Shivers, R.P.1    Sonenshein, A.L.2
  • 74
    • 0028951976 scopus 로고
    • Convergent sensing pathways mediate response to two extracellular competence factors in Bacillus subtilis
    • Solomon JM, Magnuson R, Srivastava A, Grossman AD. 1995. Convergent sensing pathways mediate response to two extracellular competence factors in Bacillus subtilis. Genes Dev. 9:547-558. http://dx.doi.org /10.1101/gad.9.5.547.
    • (1995) Genes Dev. , vol.9 , pp. 547-558
    • Solomon, J.M.1    Magnuson, R.2    Srivastava, A.3    Grossman, A.D.4
  • 75
    • 0036134961 scopus 로고    scopus 로고
    • Characterization of comQ and comX, two genes required for production of ComX pheromone in Bacillus subtilis
    • Bacon Schneider K, Palmer TM, Grossman AD. 2002. Characterization of comQ and comX, two genes required for production of ComX pheromone in Bacillus subtilis. J. Bacteriol. 184:410-419. http://dx.doi.org/10 .1128/JB.184.2.410-419.2002.
    • (2002) J. Bacteriol. , vol.184 , pp. 410-419
    • Bacon Schneider, K.1    Palmer, T.M.2    Grossman, A.D.3
  • 76
    • 0028284877 scopus 로고
    • Biochemical and genetic characterization of a competence pheromone from B
    • Magnuson R, Solomon J, Grossman AD. 1994. Biochemical and genetic characterization of a competence pheromone from B. subtilis. Cell 77: 207-216. http://dx.doi.org/10.1016/0092-8674(94)90313-1.
    • (1994) subtilis. Cell , vol.77 , pp. 207-216
    • Magnuson, R.1    Solomon, J.2    Grossman, A.D.3
  • 78
    • 0025330201 scopus 로고
    • A Bacillus subtilis regulatory gene product for genetic competence and sporulation resembles sensor protein members of the bacterial twocomponent signal-transduction systems
    • Weinrauch Y, Penchev R, Dubnau E, Smith I, Dubnau D. 1990. A Bacillus subtilis regulatory gene product for genetic competence and sporulation resembles sensor protein members of the bacterial twocomponent signal-transduction systems. Genes Dev. 4:860-872. http: //dx.doi.org/10.1101/gad.4.5.860.
    • (1990) Genes Dev. , vol.4 , pp. 860-872
    • Weinrauch, Y.1    Penchev, R.2    Dubnau, E.3    Smith, I.4    Dubnau, D.5
  • 79
    • 0032791524 scopus 로고    scopus 로고
    • Mutational analysis and membrane topology of ComP, a quorum-sensing histidine kinase of Bacillus subtilis controlling competence development
    • Piazza F, Tortosa P, Dubnau D. 1999. Mutational analysis and membrane topology of ComP, a quorum-sensing histidine kinase of Bacillus subtilis controlling competence development. J. Bacteriol. 181:4540-4548.
    • (1999) J. Bacteriol , vol.181 , pp. 4540-4548
    • Piazza, F.1    Tortosa, P.2    Dubnau, D.3
  • 80
    • 0025164975 scopus 로고
    • Signal transduction pathway controlling synthesis of a class of degradative enzymes in Bacillus subtilis: expression of the regulatory genes and analysis of mutations in degS and degU
    • Msadek T, Kunst F, Henner D, Klier A, Rapoport G, Dedonder R. 1990. Signal transduction pathway controlling synthesis of a class of degradative enzymes in Bacillus subtilis: expression of the regulatory genes and analysis of mutations in degS and degU. J. Bacteriol. 172:824-834.
    • (1990) J. Bacteriol , vol.172 , pp. 824-834
    • Msadek, T.1    Kunst, F.2    Henner, D.3    Klier, A.4    Rapoport, G.5    Dedonder, R.6
  • 81
    • 0025909522 scopus 로고
    • Mutational analysis of the Bacillus subtilis DegU regulator and its phosphorylation by the DegS protein kinase
    • Dahl MK, Msadek T, Kunst F, Rapoport G. 1991. Mutational analysis of the Bacillus subtilis DegU regulator and its phosphorylation by the DegS protein kinase. J. Bacteriol. 173:2539-2547.
    • (1991) J. Bacteriol , vol.173 , pp. 2539-2547
    • Dahl, M.K.1    Msadek, T.2    Kunst, F.3    Rapoport, G.4
  • 82
    • 0026643498 scopus 로고
    • The phosphorylation state of the DegU response regulator acts as a molecular switch allowing either degradative enzyme synthesis of expression of genetic competence in Bacillus subtilis
    • Dahl MK, Msadek T, Kunst Rapoport FG. 1992. The phosphorylation state of the DegU response regulator acts as a molecular switch allowing either degradative enzyme synthesis of expression of genetic competence in Bacillus subtilis. J. Biol. Chem. 267:14509-14514.
    • (1992) J. Biol. Chem , vol.267 , pp. 14509-14514
    • Dahl, M.K.1    Msadek, T.2    Kunst Rapoport, F.G.3
  • 83
    • 0034255503 scopus 로고    scopus 로고
    • The pleiotropic response regulator DegU functions as a priming protein in competence development in Bacillus subtilis
    • Hamoen LW, Van Werkhoven AF, Venema G, Dubnau D. 2000. The pleiotropic response regulator DegU functions as a priming protein in competence development in Bacillus subtilis. Proc. Natl. Acad. Sci. U. S. A. 97:9246-9251. http://dx.doi.org/10.1073/pnas.160010597.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 9246-9251
    • Hamoen, L.W.1    Van Werkhoven, A.F.2    Venema, G.3    Dubnau, D.4
  • 84
    • 4444374929 scopus 로고    scopus 로고
    • DegU-P represses expression of the motility fla/che operon in Bacillus subtilis
    • Amati G, Bisicchia P, Galizzi A. 2004. DegU-P represses expression of the motility fla/che operon in Bacillus subtilis. J. Bacteriol. 186:6003-6014. http://dx.doi.org/10.1128/JB.186.18.6003-6014.2004.
    • (2004) J. Bacteriol. , vol.186 , pp. 6003-6014
    • Amati, G.1    Bisicchia, P.2    Galizzi, A.3
  • 85
    • 34748927064 scopus 로고    scopus 로고
    • Gradual activation of the response regulator DegU controls serial expression of genes for flagellum formation and biofilm formation in Bacillus subtilis
    • Kobayashi K. 2007. Gradual activation of the response regulator DegU controls serial expression of genes for flagellum formation and biofilm formation in Bacillus subtilis. Mol. Microbiol. 66:395-409. http://dx.doi .org/10.1111/j.1365-2958.2007.05923.x.
    • (2007) Mol. Microbiol. , vol.66 , pp. 395-409
    • Kobayashi, K.1
  • 86
    • 34447299099 scopus 로고    scopus 로고
    • DegU co-ordinates multicellular behaviour exhibited by Bacillus subtilis
    • Verhamme DT, Kiley TB, Stanley-Wall NR. 2007. DegU co-ordinates multicellular behaviour exhibited by Bacillus subtilis. Mol. Microbiol. 65:554-568. http://dx.doi.org/10.1111/j.1365-2958.2007.05810.x.
    • (2007) Mol. Microbiol. , vol.65 , pp. 554-568
    • Verhamme, D.T.1    Kiley, T.B.2    Stanley-Wall, N.R.3
  • 87
    • 70349671435 scopus 로고    scopus 로고
    • Bacillus subtilis response regulator DegU is a direct activator of pgsB transcription involved in γ-poly-glutamic acid synthesis
    • Ohsawa T, Tsukahara K, Ogura M. 2009. Bacillus subtilis response regulator DegU is a direct activator of pgsB transcription involved in γ-poly-glutamic acid synthesis. Biosci. Biotechnol. Biochem. 73:2096-2102. http://dx.doi.org/10.1271/bbb.90341.
    • (2009) Biosci. Biotechnol. Biochem. , vol.73 , pp. 2096-2102
    • Ohsawa, T.1    Tsukahara, K.2    Ogura, M.3
  • 88
    • 80051562783 scopus 로고    scopus 로고
    • DegU-phosphate activates expression of the antisigma factor FlgM in Bacillus subtilis
    • Hsueh YH, Cozy LM, Sham LT, Calvo RA, Gutu AD, Winkler ME, Kearns DB. 2011. DegU-phosphate activates expression of the antisigma factor FlgM in Bacillus subtilis. Mol. Microbiol. 81:1092-1108. http://dx.doi.org/10.1111/j.1365-2958.2011.07755.x.
    • (2011) Mol. Microbiol. , vol.81 , pp. 1092-1108
    • Hsueh, Y.H.1    Cozy, L.M.2    Sham, L.T.3    Calvo, R.A.4    Gutu, A.D.5    Winkler, M.E.6    Kearns, D.B.7
  • 89
    • 0025731021 scopus 로고
    • DegS-DegU and ComP-ComAmodulator-effector pairs control expression of the Bacillus subtilis pleiotropic regulatory gene degQ
    • Msadek T, Kunst F, Klier A, Rapoport G. 1991. DegS-DegU and ComP-ComAmodulator-effector pairs control expression of the Bacillus subtilis pleiotropic regulatory gene degQ. J. Bacteriol. 173:2366-2377.
    • (1991) J. Bacteriol , vol.173 , pp. 2366-2377
    • Msadek, T.1    Kunst, F.2    Klier, A.3    Rapoport, G.4
  • 90
    • 23744435412 scopus 로고    scopus 로고
    • Defining the genetic differences between wild and domestic strains of Bacillus subtilis that affect poly-γ-DLglutamic acid production and biofilm formation
    • Stanley NR, Lazazzera BA. 2005. Defining the genetic differences between wild and domestic strains of Bacillus subtilis that affect poly-γ-DLglutamic acid production and biofilm formation. Mol. Microbiol. 57: 1143-1158. http://dx.doi.org/10.1111/j.1365-2958.2005.04746.x.
    • (2005) Mol. Microbiol. , vol.57 , pp. 1143-1158
    • Stanley, N.R.1    Lazazzera, B.A.2
  • 91
    • 83255174926 scopus 로고    scopus 로고
    • Mutations suppressing the loss of DegQ function in Bacillus subtilis natto poly-γ-glutamate synthesis
    • Do TH, Suzuki Y, Abe N, Kaneko J, Itoh Y, Kimura K. 2011. Mutations suppressing the loss of DegQ function in Bacillus subtilis natto poly-γ-glutamate synthesis. Appl. Environ. Microbiol. 77:8249-8258. http://dx .doi.org/10.1128/AEM.05827-11.
    • (2011) Appl. Environ. Microbiol. , vol.77 , pp. 8249-8258
    • Do, T.H.1    Suzuki, Y.2    Abe, N.3    Kaneko, J.4    Itoh, Y.5    Kimura, K.6
  • 92
    • 33748926752 scopus 로고    scopus 로고
    • Stoichiometry and turnover in single functioning membrane protein complexes
    • Leake MC, Chandler JH, Wadhams GH, Bai F, Berry RM, Armitage JP. 2006. Stoichiometry and turnover in single functioning membrane protein complexes. Nature 443:355-358. http://dx.doi.org/10.1038 /nature05135.
    • (2006) Nature , vol.443 , pp. 355-358
    • Leake, M.C.1    Chandler, J.H.2    Wadhams, G.H.3    Bai, F.4    Berry, R.M.5    Armitage, J.P.6
  • 93
    • 29144501313 scopus 로고    scopus 로고
    • Cell population heterogeneity during growth of Bacillus subtilis
    • Kearns DB, Losick R. 2005. Cell population heterogeneity during growth of Bacillus subtilis. Genes Dev. 19:3083-3094. http://dx.doi.org /10.1101/gad.1373905.
    • (2005) Genes Dev. , vol.19 , pp. 3083-3094
    • Kearns, D.B.1    Losick, R.2
  • 95
    • 13244255402 scopus 로고    scopus 로고
    • Capsule synthesis by Bacillus anthracis is required for dissemination in murine inhalation anthrax
    • Drysdale M, Heninger S, Hutt J, Chen Y, Lyons CR, Koehler TM. 2005. Capsule synthesis by Bacillus anthracis is required for dissemination in murine inhalation anthrax. EMBO J. 24:221-227. http://dx.doi .org/10.1038/sj.emboj.7600495.
    • (2005) EMBO J. , vol.24 , pp. 221-227
    • Drysdale, M.1    Heninger, S.2    Hutt, J.3    Chen, Y.4    Lyons, C.R.5    Koehler, T.M.6
  • 96
    • 80053998875 scopus 로고    scopus 로고
    • CsrA-FliW interaction governs flagellin homeostasis and a checkpoint on flagellar morphogenesis in Bacillus subtilis
    • Mukherjee S, Yakhnin H, Kysela D, Sokoloski J, Babitzke P, Kearns DB. 2011. CsrA-FliW interaction governs flagellin homeostasis and a checkpoint on flagellar morphogenesis in Bacillus subtilis. Mol. Microbiol. 82:447-461. http://dx.doi.org/10.1111/j.1365-2958.2011.07822.x.
    • (2011) Mol. Microbiol. , vol.82 , pp. 447-461
    • Mukherjee, S.1    Yakhnin, H.2    Kysela, D.3    Sokoloski, J.4    Babitzke, P.5    Kearns, D.B.6
  • 97
    • 33748763844 scopus 로고    scopus 로고
    • FliT acts as an anti-FlhD2C2 factor in the transcriptional control of the flagellar regulon in Salmonella enterica serovar typhimurium
    • Yamamoto S, Kutsukake K. 2006. FliT acts as an anti-FlhD2C2 factor in the transcriptional control of the flagellar regulon in Salmonella enterica serovar typhimurium. J. Bacteriol. 188:6703-6708. http://dx.doi.org/10 .1128/JB.00799-06.
    • (2006) J. Bacteriol. , vol.188 , pp. 6703-6708
    • Yamamoto, S.1    Kutsukake, K.2
  • 98
    • 0029832102 scopus 로고    scopus 로고
    • FlgM is a primary regulator of σD activity, and its absence restores motility to a sinR mutant
    • Fredrick K, Helmann JD. 1996. FlgM is a primary regulator of σD activity, and its absence restores motility to a sinR mutant. J. Bacteriol. 178:7010-7013.
    • (1996) J. Bacteriol , vol.178 , pp. 7010-7013
    • Fredrick, K.1    Helmann, J.D.2
  • 99
    • 0022522793 scopus 로고
    • Regulation of lateral flagella gene transcription in Vibrio parahaemolyticus
    • Belas R, Simon M, Silverman M. 1986. Regulation of lateral flagella gene transcription in Vibrio parahaemolyticus. J. Bacteriol. 167:210-218.
    • (1986) J. Bacteriol , vol.167 , pp. 210-218
    • Belas, R.1    Simon, M.2    Silverman, M.3
  • 100
    • 0024299476 scopus 로고
    • Flagellar dynamometer controls swarmer cell differentiation of V
    • McCarter L, Hilman M, Silverman M. 1988. Flagellar dynamometer controls swarmer cell differentiation of V. parahaemolyticus. Cell 54:345-351.
    • (1988) parahaemolyticus Cell , vol.54 , pp. 345-351
    • McCarter, L.1    Hilman, M.2    Silverman, M.3
  • 101
    • 0029955266 scopus 로고    scopus 로고
    • The sodium-driven polar flagellar motor of marine Vibrio as the mechanosensor that regulates lateral flagellar expression
    • Kawagishi I, Imagawa M, Imae Y, McCarter L, Homma M. 1996. The sodium-driven polar flagellar motor of marine Vibrio as the mechanosensor that regulates lateral flagellar expression. Mol. Microbiol. 20:693-699. http://dx.doi.org/10.1111/j.1365-2958.1996.tb02509.x.
    • (1996) Mol. Microbiol. , vol.20 , pp. 693-699
    • Kawagishi, I.1    Imagawa, M.2    Imae, Y.3    McCarter, L.4    Homma, M.5
  • 102
    • 0033545947 scopus 로고    scopus 로고
    • Mutations conferring resistance to phenamil and amiloride, inhibitors of sodium-driven motility of Vibrio parahaemolyticus
    • Jaques S, Kim YK, McCarter LL. 1999. Mutations conferring resistance to phenamil and amiloride, inhibitors of sodium-driven motility of Vibrio parahaemolyticus. Proc. Natl. Acad. Sci. U. S. A. 96:5740-5745. http://dx.doi.org/10.1073/pnas.96.10.5740.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 5740-5745
    • Jaques, S.1    Kim, Y.K.2    McCarter, L.L.3
  • 103
    • 25144520842 scopus 로고    scopus 로고
    • The ability of Proteus mirabilis to sense surfaces and regulate virulence gene expression involves FliL, a flagellar basal body protein
    • Belas R, Suvanasuthi R. 2005. The ability of Proteus mirabilis to sense surfaces and regulate virulence gene expression involves FliL, a flagellar basal body protein. J. Bacteriol. 187:6789-6803. http://dx.doi.org/10 .1128/JB.187.19.6789-6803.2005.
    • (2005) J. Bacteriol. , vol.187 , pp. 6789-6803
    • Belas, R.1    Suvanasuthi, R.2
  • 104
    • 0028125086 scopus 로고
    • Caulobacter flagellar function, but not assembly, requires FliL, a non-polarly localized membrane protein present in all cell types
    • Jenal U, White J, Shapiro L. 1994. Caulobacter flagellar function, but not assembly, requires FliL, a non-polarly localized membrane protein present in all cell types. J. Mol. Biol. 243:227-244. http://dx.doi.org/10.1006 /jmbi.1994.1650.
    • (1994) J. Mol. Biol. , vol.243 , pp. 227-244
    • Jenal, U.1    White, J.2    Shapiro, L.3
  • 106
    • 84873539650 scopus 로고    scopus 로고
    • Activity of Proteus mirabilis FliL is viscosity dependent and requires extragenic DNA
    • Lee YY, Patellis J, Belas R. 2013. Activity of Proteus mirabilis FliL is viscosity dependent and requires extragenic DNA. J. Bacteriol. 195:823-832. http://dx.doi.org/10.1128/JB.02024-12.
    • (2013) J. Bacteriol. , vol.195 , pp. 823-832
    • Lee, Y.Y.1    Patellis, J.2    Belas, R.3
  • 107
    • 0032981401 scopus 로고    scopus 로고
    • Effects of changes in membrane sodium flux on virulence gene expression in Vibrio cholerae
    • Häse C, Mekalanos JJ. 1999. Effects of changes in membrane sodium flux on virulence gene expression in Vibrio cholerae. Proc. Natl. Acad. Sci. U. S. A. 96:3183-3187. http://dx.doi.org/10.1073/pnas.96.6.3183.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 3183-3187
    • Häse, C.1    Mekalanos, J.J.2
  • 108
    • 79953820763 scopus 로고    scopus 로고
    • Surface sensing in Vibrio parahaemolyticus triggers a programme of gene expression that promotes colonization and virulence
    • Gode-Potratz CJ, Kustusch RJ, Breheny PJ, Weiss DS, McCarter LL. 2011. Surface sensing in Vibrio parahaemolyticus triggers a programme of gene expression that promotes colonization and virulence. Mol. Microbiol. 79:240-263. http://dx.doi.org/10.1111/j.1365-2958.2010.07445.x.
    • (2011) Mol. Microbiol. , vol.79 , pp. 240-263
    • Gode-Potratz, C.J.1    Kustusch, R.J.2    Breheny, P.J.3    Weiss, D.S.4    McCarter, L.L.5
  • 109
    • 84155164758 scopus 로고    scopus 로고
    • Surface contact stimulates the just-in-time deployment of bacterial adhesins
    • Li G, Brown PJ, Tang JX, Xu J, Quardokus EM, Fuqua C, Brun YV. 2012. Surface contact stimulates the just-in-time deployment of bacterial adhesins. Mol. Microbiol. 83:41-51. http://dx.doi.org/10.1111/j.1365-2958.2011.07909.x.
    • (2012) Mol. Microbiol. , vol.83 , pp. 41-51
    • Li, G.1    Brown, P.J.2    Tang, J.X.3    Xu, J.4    Quardokus, E.M.5    Fuqua, C.6    Brun, Y.V.7
  • 110
    • 84880387422 scopus 로고    scopus 로고
    • Dynamics of mechanosensing in the bacterial flagellar motor
    • Lele PP, Hosu BG, Berg HC. 2013. Dynamics of mechanosensing in the bacterial flagellar motor. Proc. Natl. Acad. Sci. U. S. A. 110:11839-11844. http://dx.doi.org/10.1073/pnas.1305885110.
    • (2013) Proc. Natl. Acad. Sci. U. S. A. , vol.110 , pp. 11839-11844
    • Lele, P.P.1    Hosu, B.G.2    Berg, H.C.3
  • 111
    • 84883436048 scopus 로고    scopus 로고
    • Loaddependent assembly of the bacterial flagellar motor
    • Tipping MJ, Delalez NJ, Lim R, Berry RM, Armitage JP. 2013. Loaddependent assembly of the bacterial flagellar motor. mBio 4:e00551-13. http://dx.doi.org/10.1128/mBio.00551-13.
    • (2013) mBio , vol.4
    • Tipping, M.J.1    Delalez, N.J.2    Lim, R.3    Berry, R.M.4    Armitage, J.P.5
  • 112
    • 39449126798 scopus 로고    scopus 로고
    • Phylogeny of γ-polyglutamic acid-producing Bacillus strains isolated from fermented soybean foods manufactured in Asian countries
    • Meerak J, Iida H, Watanabe Y, Miyashita M, Sato H, Nakagawa Y, Tahara Y. 2007. Phylogeny of γ-polyglutamic acid-producing Bacillus strains isolated from fermented soybean foods manufactured in Asian countries. J. Gen. Appl. Microbiol. 53:315-323. http://dx.doi.org/10 .2323/jgam.53.315.
    • (2007) J. Gen. Appl. Microbiol. , vol.53 , pp. 315-323
    • Meerak, J.1    Iida, H.2    Watanabe, Y.3    Miyashita, M.4    Sato, H.5    Nakagawa, Y.6    Tahara, Y.7
  • 113
    • 33947216212 scopus 로고    scopus 로고
    • Microbial biosynthesis of polyglutamic acid biopolymer and applications in the biopharmaceutical, biomedical, and food industries
    • Buescher JM, Margaritis A. 2007. Microbial biosynthesis of polyglutamic acid biopolymer and applications in the biopharmaceutical, biomedical, and food industries. Crit. Rev. Biotechnol. 27:1-19. http://dx .doi.org/10.1080/07388550601166458.
    • (2007) Crit. Rev. Biotechnol. , vol.27 , pp. 1-19
    • Buescher, J.M.1    Margaritis, A.2
  • 114
    • 84856151373 scopus 로고    scopus 로고
    • Modified mariner transposons for random inducible-expression insertions and transcriptional reporter fusion insertions in Bacillus subtilis
    • Pozsgai ER, Blair KM, Kearns DB. 2012. Modified mariner transposons for random inducible-expression insertions and transcriptional reporter fusion insertions in Bacillus subtilis. Appl. Environ. Microbiol. 78:778-785. http://dx.doi.org/10.1128/AEM.07098-11.
    • (2012) Appl. Environ. Microbiol. , vol.78 , pp. 778-785
    • Pozsgai, E.R.1    Blair, K.M.2    Kearns, D.B.3
  • 115
    • 84883278830 scopus 로고    scopus 로고
    • Plasmid-encoded ComI inhibits competence in the ancestral 3610 strain of Bacillus subtilis
    • Konkol MA, Blair KM, Kearns DB. 2013. Plasmid-encoded ComI inhibits competence in the ancestral 3610 strain of Bacillus subtilis. J. Bacteriol. 195:4085-4093. http://dx.doi.org/10.1128/JB.00696-13.
    • (2013) J. Bacteriol. , vol.195 , pp. 4085-4093
    • Konkol, M.A.1    Blair, K.M.2    Kearns, D.B.3
  • 116
    • 84858293761 scopus 로고    scopus 로고
    • SlrA/SinR/SlrR inhibits motility gene expression upstream of a hypersensitive and hysteretic switch at the level of σD in Bacillus subtilis
    • Cozy LM, Phillips AM, Calvo RA, Bate AR, Hsueh Y-H, Bonneau R, Eichenberger P, Kearns DB. 2012. SlrA/SinR/SlrR inhibits motility gene expression upstream of a hypersensitive and hysteretic switch at the level of σD in Bacillus subtilis. Mol. Microbiol. 83:1210-1228. http://dx.doi .org/10.1111/j.1365-2958.2012.08003.x.
    • (2012) Mol. Microbiol. , vol.83 , pp. 1210-1228
    • Cozy, L.M.1    Phillips, A.M.2    Calvo, R.A.3    Bate, A.R.4    Hsueh, Y.-H.5    Bonneau, R.6    Eichenberger, P.7    Kearns, D.B.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.