메뉴 건너뛰기




Volumn 192, Issue 19, 2010, Pages 4847-4858

The Caulobacter Tol-Pal complex is essential for outer membrane integrity and the positioning of a polar localization factor

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; FTSZ PROTEIN; MEMBRANE PROTEIN; PEPTIDOGLYCAN; PROTEIN HISTIDINE KINASE; PROTEIN PAL; PROTEIN PLEC; PROTEIN TIPN; PROTEIN TOLA; PROTEIN TOLB; UNCLASSIFIED DRUG;

EID: 77956850709     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.00607-10     Document Type: Article
Times cited : (92)

References (50)
  • 1
    • 0030856502 scopus 로고    scopus 로고
    • FtsN, a late recruit to the septum in Escherichia coli
    • Addinall, S. G., C. Cao, and J. Lutkenhaus. 1997. FtsN, a late recruit to the septum in Escherichia coli. Mol. Microbiol. 25:303-309.
    • (1997) Mol. Microbiol. , vol.25 , pp. 303-309
    • Addinall, S.G.1    Cao, C.2    Lutkenhaus, J.3
  • 4
    • 0344631755 scopus 로고    scopus 로고
    • In vitro characterization of peptidoglycan-associated lipoprotein (PAL)-peptidoglycan and PAL-TolB interactions
    • Bouveret, E., H. Benedetti, A. Rigal, E. Loret, and C. Lazdunski. 1999. In vitro characterization of peptidoglycan-associated lipoprotein (PAL)-peptidoglycan and PAL-TolB interactions. J. Bacteriol. 181:6306-6311.
    • (1999) J. Bacteriol. , vol.181 , pp. 6306-6311
    • Bouveret, E.1    Benedetti, H.2    Rigal, A.3    Loret, E.4    Lazdunski, C.5
  • 5
    • 0029045244 scopus 로고
    • Peptidoglycan-associated lipoprotein-TolB interaction. A possible key to explaining the formation of contact sites between the inner and outer membranes of Escherichia coli
    • Bouveret, E., R. Derouiche, A. Rigal, R. Lloubes, C. Lazdunski, and H. Benedetti. 1995. Peptidoglycan-associated lipoprotein-TolB interaction. A possible key to explaining the formation of contact sites between the inner and outer membranes of Escherichia coli. J. Biol. Chem. 270:11071-11077.
    • (1995) J. Biol. Chem. , vol.270 , pp. 11071-11077
    • Bouveret, E.1    Derouiche, R.2    Rigal, A.3    Lloubes, R.4    Lazdunski, C.5    Benedetti, H.6
  • 7
    • 0036180995 scopus 로고    scopus 로고
    • Pal lipoprotein of Escherichia coli plays a major role in outer membrane integrity
    • Cascales, E., A. Bernadac, M. Gavioli, J. C. Lazzaroni, and R. Lloubes. 2002. Pal lipoprotein of Escherichia coli plays a major role in outer membrane integrity. J. Bacteriol. 184:754-759.
    • (2002) J. Bacteriol. , vol.184 , pp. 754-759
    • Cascales, E.1    Bernadac, A.2    Gavioli, M.3    Lazzaroni, J.C.4    Lloubes, R.5
  • 8
    • 0035163972 scopus 로고    scopus 로고
    • The TolQ-TolR proteins energize TolA and share homologies with the flagellar motor proteins MotAMotB
    • Cascales, E., R. Lloubes, and J. N. Sturgis. 2001. The TolQ-TolR proteins energize TolA and share homologies with the flagellar motor proteins MotAMotB. Mol. Microbiol. 42:795-807.
    • (2001) Mol. Microbiol. , vol.42 , pp. 795-807
    • Cascales, E.1    Lloubes, R.2    Sturgis, J.N.3
  • 10
    • 0031848939 scopus 로고    scopus 로고
    • TolB protein of Escherichia coli K-12 interacts with the outer membrane peptidoglycan-associated proteins Pal, Lpp and OmpA
    • Clavel, T., P. Germon, A. Vianney, R. Portalier, and J. C. Lazzaroni. 1998. TolB protein of Escherichia coli K-12 interacts with the outer membrane peptidoglycan-associated proteins Pal, Lpp and OmpA. Mol. Microbiol. 29:359-367.
    • (1998) Mol. Microbiol. , vol.29 , pp. 359-367
    • Clavel, T.1    Germon, P.2    Vianney, A.3    Portalier, R.4    Lazzaroni, J.C.5
  • 11
    • 0030026642 scopus 로고    scopus 로고
    • Expression of the tolQRA genes of Escherichia coli K-12 is controlled by the RcsC sensor protein involved in capsule synthesis
    • Clavel, T., J. C. Lazzaroni, A. Vianney, and R. Portalier. 1996. Expression of the tolQRA genes of Escherichia coli K-12 is controlled by the RcsC sensor protein involved in capsule synthesis. Mol. Microbiol. 19:19-25.
    • (1996) Mol. Microbiol. , vol.19 , pp. 19-25
    • Clavel, T.1    Lazzaroni, J.C.2    Vianney, A.3    Portalier, R.4
  • 12
    • 0030801376 scopus 로고    scopus 로고
    • Filamentous phage infection: Required interactions with the TolA protein
    • Click, E. M., and R. E. Webster. 1997. Filamentous phage infection: required interactions with the TolA protein. J. Bacteriol. 179:6464-6471.
    • (1997) J. Bacteriol. , vol.179 , pp. 6464-6471
    • Click, E.M.1    Webster, R.E.2
  • 13
    • 0016524407 scopus 로고
    • Genetics of resistance to colicins in Escherichia coli K-12: Cross-resistance among colicins of group a
    • Davies, J. K., and P. Reeves. 1975. Genetics of resistance to colicins in Escherichia coli K-12: cross-resistance among colicins of group A. J. Bacteriol. 123:102-117.
    • (1975) J. Bacteriol. , vol.123 , pp. 102-117
    • Davies, J.K.1    Reeves, P.2
  • 14
    • 0029055749 scopus 로고
    • Protein complex within Escherichia coli inner membrane. TolA Nterminal domain interacts with TolQ and TolR proteins
    • Derouiche, R., H. Benedetti, J. C. Lazzaroni, C. Lazdunski, and R. Lloubes. 1995. Protein complex within Escherichia coli inner membrane. TolA Nterminal domain interacts with TolQ and TolR proteins. J. Biol. Chem. 270:11078-11084.
    • (1995) J. Biol. Chem. , vol.270 , pp. 11078-11084
    • Derouiche, R.1    Benedetti, H.2    Lazzaroni, J.C.3    Lazdunski, C.4    Lloubes, R.5
  • 15
    • 0036330840 scopus 로고    scopus 로고
    • Mutational analysis of the TolA C-terminal domain of Escherichia coli and genetic evidence for an interaction between TolA and TolB
    • Dubuisson, J. F., A. Vianney, and J. C. Lazzaroni. 2002. Mutational analysis of the TolA C-terminal domain of Escherichia coli and genetic evidence for an interaction between TolA and TolB. J. Bacteriol. 184:4620-4625.
    • (2002) J. Bacteriol. , vol.184 , pp. 4620-4625
    • Dubuisson, J.F.1    Vianney, A.2    Lazzaroni, J.C.3
  • 16
    • 51549102573 scopus 로고    scopus 로고
    • A self-associating protein critical for chromosome attachment, division, and polar organization in Caulobacter
    • Ebersbach, G., A. Briegel, G. J. Jensen, and C. Jacobs-Wagner. 2008. A self-associating protein critical for chromosome attachment, division, and polar organization in Caulobacter. Cell 134:956-968.
    • (2008) Cell , vol.134 , pp. 956-968
    • Ebersbach, G.1    Briegel, A.2    Jensen, G.J.3    Jacobs-Wagner, C.4
  • 17
    • 48149089820 scopus 로고    scopus 로고
    • NagA-dependent uptake of N-acetyl-glucosamine and N-acetyl-chitin oligosaccharides across the outer membrane of Caulobacter crescentus
    • Eisenbeis, S., S. Lohmiller, M. Valdebenito, S. Leicht, and V. Braun. 2008. NagA-dependent uptake of N-acetyl-glucosamine and N-acetyl-chitin oligosaccharides across the outer membrane of Caulobacter crescentus. J. Bacteriol. 190:5230-5238.
    • (2008) J. Bacteriol. , vol.190 , pp. 5230-5238
    • Eisenbeis, S.1    Lohmiller, S.2    Valdebenito, M.3    Leicht, S.4    Braun, V.5
  • 18
    • 0033744772 scopus 로고    scopus 로고
    • Surface expression of O-specific lipopolysaccharide in Escherichia coli requires the function of the TolA protein
    • Gaspar, J. A., J. A. Thomas, C. L. Marolda, and M. A. Valvano. 2000. Surface expression of O-specific lipopolysaccharide in Escherichia coli requires the function of the TolA protein. Mol. Microbiol. 38:262-275.
    • (2000) Mol. Microbiol. , vol.38 , pp. 262-275
    • Gaspar, J.A.1    Thomas, J.A.2    Marolda, C.L.3    Valvano, M.A.4
  • 19
    • 33846650968 scopus 로고    scopus 로고
    • The trans-envelope Tol-Pal complex is part of the cell division machinery and required for proper outer-membrane invagination during cell constriction in E. coli
    • Gerding, M. A., Y. Ogata, N. D. Pecora, H. Niki, and P. A. de Boer. 2007. The trans-envelope Tol-Pal complex is part of the cell division machinery and required for proper outer-membrane invagination during cell constriction in E. coli. Mol. Microbiol. 63:1008-1025.
    • (2007) Mol. Microbiol. , vol.63 , pp. 1008-1025
    • Gerding, M.A.1    Ogata, Y.2    Pecora, N.D.3    Niki, H.4    De Boer, P.A.5
  • 20
    • 0032417321 scopus 로고    scopus 로고
    • Mutational analysis of the Escherichia coli K-12 TolA N-terminal region and characterization of its TolQ-interacting domain by genetic suppression
    • Germon, P., T. Clavel, A. Vianney, R. Portalier, and J. C. Lazzaroni. 1998. Mutational analysis of the Escherichia coli K-12 TolA N-terminal region and characterization of its TolQ-interacting domain by genetic suppression. J. Bacteriol. 180:6433-6439.
    • (1998) J. Bacteriol. , vol.180 , pp. 6433-6439
    • Germon, P.1    Clavel, T.2    Vianney, A.3    Portalier, R.4    Lazzaroni, J.C.5
  • 21
    • 0034970708 scopus 로고    scopus 로고
    • Energy-dependent conformational change in the TolA protein of Escherichia coli involves its N-terminal domain, TolQ, and TolR
    • Germon, P., M. C. Ray, A. Vianney, and J. C. Lazzaroni. 2001. Energy-dependent conformational change in the TolA protein of Escherichia coli involves its N-terminal domain, TolQ, and TolR. J. Bacteriol. 183:4110-4114.
    • (2001) J. Bacteriol. , vol.183 , pp. 4110-4114
    • Germon, P.1    Ray, M.C.2    Vianney, A.3    Lazzaroni, J.C.4
  • 22
    • 21844441637 scopus 로고    scopus 로고
    • Diverse paths to midcell: Assembly of the bacterial cell division machinery
    • Goehring, N. W., and J. Beckwith. 2005. Diverse paths to midcell: assembly of the bacterial cell division machinery. Curr. Biol. 15:R514-R526.
    • (2005) Curr. Biol. , vol.15
    • Goehring, N.W.1    Beckwith, J.2
  • 23
    • 77953995341 scopus 로고    scopus 로고
    • DipM links peptidoglycan remodeling to outer membrane organization in Caulobacter
    • Goley, E. E., L. R. Comolli, M. J. Fero, K. H. Downing, and L. Shapiro. 2010. DipM links peptidoglycan remodeling to outer membrane organization in Caulobacter. Mol. Microbiol. 77:56-73.
    • (2010) Mol. Microbiol. , vol.77 , pp. 56-73
    • Goley, E.E.1    Comolli, L.R.2    Fero, M.J.3    Downing, K.H.4    Shapiro, L.5
  • 24
    • 0033988998 scopus 로고    scopus 로고
    • Regulation of stalk elongation by phosphate in Caulobacter crescentus
    • Gonin, M., E. M. Quardokus, D. O'Donnol, J. Maddock, and Y. V. Brun. 2000. Regulation of stalk elongation by phosphate in Caulobacter crescentus. J. Bacteriol. 182:337-347.
    • (2000) J. Bacteriol. , vol.182 , pp. 337-347
    • Gonin, M.1    Quardokus, E.M.2    O'Donnol, D.3    Maddock, J.4    Brun, Y.V.5
  • 26
    • 33746610535 scopus 로고    scopus 로고
    • A phospho-signaling pathway controls the localization and activity of a protease complex critical for bacterial cell cycle progression
    • Iniesta, A. A., P. T. McGrath, A. Reisenauer, H. H. McAdams, and L. Shapiro. 2006. A phospho-signaling pathway controls the localization and activity of a protease complex critical for bacterial cell cycle progression. Proc. Natl. Acad. Sci. U. S. A. 103:10935-10940.
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 10935-10940
    • Iniesta, A.A.1    McGrath, P.T.2    Reisenauer, A.3    McAdams, H.H.4    Shapiro, L.5
  • 27
    • 26444490066 scopus 로고    scopus 로고
    • Distinct constrictive processes, separated in time and space, divide Caulobacter inner and outer membranes
    • Judd, E. M., L. R. Comolli, J. C. Chen, K. H. Downing, W. E. Moerner, and H. H. McAdams. 2005. Distinct constrictive processes, separated in time and space, divide Caulobacter inner and outer membranes. J. Bacteriol. 187:6874-6882.
    • (2005) J. Bacteriol. , vol.187 , pp. 6874-6882
    • Judd, E.M.1    Comolli, L.R.2    Chen, J.C.3    Downing, K.H.4    Moerner, W.E.5    McAdams, H.H.6
  • 28
    • 0029092472 scopus 로고
    • Proposal for a peptidoglycan-associating alpha-helical motif in the C-terminal regions of some bacterial cell-surface proteins
    • Koebnik, R. 1995. Proposal for a peptidoglycan-associating alpha-helical motif in the C-terminal regions of some bacterial cell-surface proteins. Mol. Microbiol. 16:1269-1270.
    • (1995) Mol. Microbiol. , vol.16 , pp. 1269-1270
    • Koebnik, R.1
  • 29
    • 33644753905 scopus 로고    scopus 로고
    • A landmark protein essential for establishing and perpetuating the polarity of a bacterial cell
    • Lam, H., W. B. Schofield, and C. Jacobs-Wagner. 2006. A landmark protein essential for establishing and perpetuating the polarity of a bacterial cell. Cell 124:1011-1023.
    • (2006) Cell , vol.124 , pp. 1011-1023
    • Lam, H.1    Schofield, W.B.2    Jacobs-Wagner, C.3
  • 30
    • 0026621146 scopus 로고
    • Interactions of Escherichia coli membrane lipoproteins with the murein sacculus
    • Leduc, M., K. Ishidate, N. Shakibai, and L. Rothfield. 1992. Interactions of Escherichia coli membrane lipoproteins with the murein sacculus. J. Bacteriol. 174:7982-7988.
    • (1992) J. Bacteriol. , vol.174 , pp. 7982-7988
    • Leduc, M.1    Ishidate, K.2    Shakibai, N.3    Rothfield, L.4
  • 31
    • 0025912823 scopus 로고
    • TolA: A membrane protein involved in colicin uptake contains an extended helical region
    • Levengood, S. K., W. F. Beyer, Jr., and R. E. Webster. 1991. TolA: a membrane protein involved in colicin uptake contains an extended helical region. Proc. Natl. Acad. Sci. U. S. A. 88:5939-5943.
    • (1991) Proc. Natl. Acad. Sci. U. S. A. , vol.88 , pp. 5939-5943
    • Levengood, S.K.1    Beyer Jr., W.F.2    Webster, R.E.3
  • 32
    • 36248938686 scopus 로고    scopus 로고
    • The structure of FtsZ filaments in vivo suggests a force-generating role in cell division
    • Li, Z., M. J. Trimble, Y. V. Brun, and G. J. Jensen. 2007. The structure of FtsZ filaments in vivo suggests a force-generating role in cell division. EMBO J. 26:4694-4708.
    • (2007) EMBO J. , vol.26 , pp. 4694-4708
    • Li, Z.1    Trimble, M.J.2    Brun, Y.V.3    Jensen, G.J.4
  • 33
    • 0037214420 scopus 로고    scopus 로고
    • Transcriptional organization of the Pseudomonas putida tol-oprL genes
    • Llamas, M. A., J. L. Ramos, and J. J. Rodriguez-Herva. 2003. Transcriptional organization of the Pseudomonas putida tol-oprL genes. J. Bacteriol. 185:184-195.
    • (2003) J. Bacteriol. , vol.185 , pp. 184-195
    • Llamas, M.A.1    Ramos, J.L.2    Rodriguez-Herva, J.J.3
  • 34
    • 0043062733 scopus 로고    scopus 로고
    • Role of Pseudomonas putida tol-oprL gene products in uptake of solutes through the cytoplasmic membrane
    • Llamas, M. A., J. J. Rodriguez-Herva, R. E. Hancock, W. Bitter, J. Tommassen, and J. L. Ramos. 2003. Role of Pseudomonas putida tol-oprL gene products in uptake of solutes through the cytoplasmic membrane. J. Bacteriol. 185:4707-4716.
    • (2003) J. Bacteriol. , vol.185 , pp. 4707-4716
    • Llamas, M.A.1    Rodriguez-Herva, J.J.2    Hancock, R.E.3    Bitter, W.4    Tommassen, J.5    Ramos, J.L.6
  • 35
    • 0034944420 scopus 로고    scopus 로고
    • The Tol-Pal proteins of the Escherichia coli cell envelope: An energized system required for outer membrane integrity?
    • Lloubes, R., E. Cascales, A. Walburger, E. Bouveret, C. Lazdunski, A. Bernadac, and L. Journet. 2001. The Tol-Pal proteins of the Escherichia coli cell envelope: an energized system required for outer membrane integrity? Res. Microbiol. 152:523-529.
    • (2001) Res. Microbiol. , vol.152 , pp. 523-529
    • Lloubes, R.1    Cascales, E.2    Walburger, A.3    Bouveret, E.4    Lazdunski, C.5    Bernadac, A.6    Journet, L.7
  • 37
    • 0035164022 scopus 로고    scopus 로고
    • The chromosome partitioning protein, ParB, is required for cytokinesis in Caulobacter crescentus
    • Mohl, D. A., J. Easter, Jr., and J. W. Gober. 2001. The chromosome partitioning protein, ParB, is required for cytokinesis in Caulobacter crescentus. Mol. Microbiol. 42:741-755.
    • (2001) Mol. Microbiol. , vol.42 , pp. 741-755
    • Mohl, D.A.1    Easter Jr., J.2    Gober, J.W.3
  • 38
    • 77953996215 scopus 로고    scopus 로고
    • DipM, a new factor required for peptidoglycan remodelling during cell division in Caulobacter crescentus
    • Moll, A., S. Schlimpert, A. Briegel, G. J. Jensen, and M. Thanbichler. 2010. DipM, a new factor required for peptidoglycan remodelling during cell division in Caulobacter crescentus. Mol. Microbiol. 77:90-107.
    • (2010) Mol. Microbiol. , vol.77 , pp. 90-107
    • Moll, A.1    Schlimpert, S.2    Briegel, A.3    Jensen, G.J.4    Thanbichler, M.5
  • 40
    • 70450224670 scopus 로고    scopus 로고
    • Curved FtsZ protofilaments generate bending forces on liposome membranes
    • Osawa, M., D. E. Anderson, and H. P. Erickson. 2009. Curved FtsZ protofilaments generate bending forces on liposome membranes. EMBO J. 28:3476-3484.
    • (2009) EMBO J. , vol.28 , pp. 3476-3484
    • Osawa, M.1    Anderson, D.E.2    Erickson, H.P.3
  • 41
    • 77953977302 scopus 로고    scopus 로고
    • A protein critical for cell constriction in the Gram-negative bacterium Caulobacter crescentus localizes at the division site through its peptidoglycan-binding LysM domains
    • Poggio, S., C. N. Takacs, W. Vollmer, and C. Jacobs-Wagner. 2010. A protein critical for cell constriction in the Gram-negative bacterium Caulobacter crescentus localizes at the division site through its peptidoglycan-binding LysM domains. Mol. Microbiol. 77:74-89.
    • (2010) Mol. Microbiol. , vol.77 , pp. 74-89
    • Poggio, S.1    Takacs, C.N.2    Vollmer, W.3    Jacobs-Wagner, C.4
  • 42
    • 0030011228 scopus 로고    scopus 로고
    • Cell cycle regulation and cell type-specific localization of the FtsZ division initiation protein in Caulobacter
    • Quardokus, E., N. Din, and Y. V. Brun. 1996. Cell cycle regulation and cell type-specific localization of the FtsZ division initiation protein in Caulobacter. Proc. Natl. Acad. Sci. U. S. A. 93:6314-6319.
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 6314-6319
    • Quardokus, E.1    Din, N.2    Brun, Y.V.3
  • 43
    • 0033966170 scopus 로고    scopus 로고
    • Identification by genetic suppression of Escherichia coli TolB residues important for TolB-Pal interaction
    • Ray, M. C., P. Germon, A. Vianney, R. Portalier, and J. C. Lazzaroni. 2000. Identification by genetic suppression of Escherichia coli TolB residues important for TolB-Pal interaction. J. Bacteriol. 182:821-824.
    • (2000) J. Bacteriol. , vol.182 , pp. 821-824
    • Ray, M.C.1    Germon, P.2    Vianney, A.3    Portalier, R.4    Lazzaroni, J.C.5
  • 44
    • 0035155704 scopus 로고    scopus 로고
    • Organisation and evolution of the tol-pal gene cluster
    • Sturgis, J. N. 2001. Organisation and evolution of the tol-pal gene cluster. J. Mol. Microbiol. Biotechnol. 3:113-122.
    • (2001) J. Mol. Microbiol. Biotechnol. , vol.3 , pp. 113-122
    • Sturgis, J.N.1
  • 45
    • 33745699284 scopus 로고    scopus 로고
    • MipZ, a spatial regulator coordinating chromosome segregation with cell division in Caulobacter
    • Thanbichler, M., and L. Shapiro. 2006. MipZ, a spatial regulator coordinating chromosome segregation with cell division in Caulobacter. Cell 126:147-162.
    • (2006) Cell , vol.126 , pp. 147-162
    • Thanbichler, M.1    Shapiro, L.2
  • 46
    • 0028009448 scopus 로고
    • Membrane topology and mutational analysis of the TolQ protein of Escherichia coli required for the uptake of macromolecules and cell envelope integrity
    • Vianney, A., T. M. Lewin, W. F. Beyer, Jr., J. C. Lazzaroni, R. Portalier, and R. E. Webster. 1994. Membrane topology and mutational analysis of the TolQ protein of Escherichia coli required for the uptake of macromolecules and cell envelope integrity. J. Bacteriol. 176:822-829.
    • (1994) J. Bacteriol. , vol.176 , pp. 822-829
    • Vianney, A.1    Lewin, T.M.2    Beyer Jr., W.F.3    Lazzaroni, J.C.4    Portalier, R.5    Webster, R.E.6
  • 48
    • 0036093944 scopus 로고    scopus 로고
    • The Tol/Pal system function requires an interaction between the C-terminal domain of TolA and the N-terminal domain of TolB
    • Walburger, A., C. Lazdunski, and Y. Corda. 2002. The Tol/Pal system function requires an interaction between the C-terminal domain of TolA and the N-terminal domain of TolB. Mol. Microbiol. 44:695-708.
    • (2002) Mol. Microbiol. , vol.44 , pp. 695-708
    • Walburger, A.1    Lazdunski, C.2    Corda, Y.3
  • 49
    • 0017140367 scopus 로고
    • Morphogenesis of the bacterial division septum: A new class of septation-defective mutants
    • Weigand, R. A., K. D. Vinci, and L. I. Rothfield. 1976. Morphogenesis of the bacterial division septum: a new class of septation-defective mutants. Proc. Natl. Acad. Sci. U. S. A. 73:1882-1886.
    • (1976) Proc. Natl. Acad. Sci. U. S. A. , vol.73 , pp. 1882-1886
    • Weigand, R.A.1    Vinci, K.D.2    Rothfield, L.I.3
  • 50
    • 0033231550 scopus 로고    scopus 로고
    • Differential localization of two histidine kinases controlling bacterial cell differentiation
    • Wheeler, R. T., and L. Shapiro. 1999. Differential localization of two histidine kinases controlling bacterial cell differentiation. Mol. Cell 4:683-694.
    • (1999) Mol. Cell , vol.4 , pp. 683-694
    • Wheeler, R.T.1    Shapiro, L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.