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Volumn 9, Issue 4, 2014, Pages

Location of dual sites in E. coli FtsZ important for degradation by ClpXP; one at the C-terminus and one in the disordered linker

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE DEPENDENT PROTEINASE; BACTERIAL PROTEIN; CLPXP PROTEIN; FTSZ PROTEIN; GUANOSINE TRIPHOSPHATASE; MINC PROTEIN; UNCLASSIFIED DRUG; ZIPA PROTEIN; CLPXP PROTEASE, E COLI; CYTOSKELETON PROTEIN; ENDOPEPTIDASE CLP; ESCHERICHIA COLI PROTEIN; FTSZ PROTEIN, BACTERIA; PROTEIN BINDING;

EID: 84899503736     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0094964     Document Type: Article
Times cited : (28)

References (48)
  • 1
    • 79959389010 scopus 로고    scopus 로고
    • AAA+ proteases: ATP-fueled machines of protein destruction
    • Sauer RT, Baker TA (2011) AAA+ proteases: ATP-fueled machines of protein destruction. Annu. Rev. Biochem. 80: 587-612.
    • (2011) Annu. Rev. Biochem. , vol.80 , pp. 587-612
    • Sauer, R.T.1    Baker, T.A.2
  • 2
    • 0345687188 scopus 로고    scopus 로고
    • Distinct peptide signals in the UmuD and UmuD' subunits of UmuD/D' mediate tethering and substrate processing by the ClpXP protease
    • DOI 10.1073/pnas.2235804100
    • Neher SB, Sauer RT, Baker TA (2003) Distinct peptide signals in the UmuD and UmuD' subunits of UmuD/D' mediate tethering and substrate processing by the ClpXP protease. Proc. Natl. Acad. Sci. U S A 100: 13219-13224. (Pubitemid 37444722)
    • (2003) Proceedings of the National Academy of Sciences of the United States of America , vol.100 , Issue.23 , pp. 13219-13224
    • Neher, S.B.1    Sauer, R.T.2    Baker, T.A.3
  • 3
    • 84862272387 scopus 로고    scopus 로고
    • Role of the N-terminal domain of the chaperone ClpX in the recognition and degradation of lambda phage protein O
    • Thibault G, Houry WA (2012) Role of the N-terminal domain of the chaperone ClpX in the recognition and degradation of lambda phage protein O. J. Phys. Chem. B. 116: 6717-6724.
    • (2012) J. Phys. Chem. B. , vol.116 , pp. 6717-6724
    • Thibault, G.1    Houry, W.A.2
  • 4
    • 41549163391 scopus 로고    scopus 로고
    • Unique Contacts Direct High-Priority Recognition of the Tetrameric Mu Transposase-DNA Complex by the AAA+ Unfoldase ClpX
    • DOI 10.1016/j.molcel.2008.02.013, PII S1097276508001329
    • Abdelhakim AH, Oakes EC, Sauer RT, Baker TA (2008) Unique contacts direct high-priority recognition of the tetrameric Mu transposase-DNA complex by the AAA+ unfoldase ClpX. Mol. Cell 30: 39-50. (Pubitemid 351470146)
    • (2008) Molecular Cell , vol.30 , Issue.1 , pp. 39-50
    • Abdelhakim, A.H.1    Oakes, E.C.2    Sauer, R.T.3    Baker, T.A.4
  • 5
    • 67651208925 scopus 로고    scopus 로고
    • Adapting the machine: Adaptor proteins for Hsp100/Clp and AAA+ proteases
    • Kirstein J, Moliere N, Dougan DA, Turgay K (2009) Adapting the machine: adaptor proteins for Hsp100/Clp and AAA+ proteases. Nat. Rev. Microbiols. 7: 589-599.
    • (2009) Nat. Rev. Microbiols. , vol.7 , pp. 589-599
    • Kirstein, J.1    Moliere, N.2    Dougan, D.A.3    Turgay, K.4
  • 6
    • 0141957392 scopus 로고    scopus 로고
    • Targeted delivery of an ssrA-tagged substrate by the adaptor protein SspB to its cognate AAA+ protein ClpX
    • DOI 10.1016/j.molcel.2003.08.012
    • Dougan DA, Weber-Ban E, Bukau B (2003) Targeted delivery of an ssrA-tagged substrate by the adaptor protein SspB to its cognate AAA+ protein ClpX. Mol. Cell 12: 373-380. (Pubitemid 37238924)
    • (2003) Molecular Cell , vol.12 , Issue.2 , pp. 373-380
    • Dougan, D.A.1    Weber-Ban, E.2    Bukau, B.3
  • 7
    • 67649811066 scopus 로고    scopus 로고
    • ClpXP protease degrades the cytoskeletal protein, FtsZ, and modulates FtsZ polymer dynamics
    • Camberg JL, Hoskins JR, Wickner S (2009) ClpXP protease degrades the cytoskeletal protein, FtsZ, and modulates FtsZ polymer dynamics. Proc. Natl. Acad. Sci. U S A 106: 10614-10619.
    • (2009) Proc. Natl. Acad. Sci. U S A , vol.106 , pp. 10614-10619
    • Camberg, J.L.1    Hoskins, J.R.2    Wickner, S.3
  • 8
    • 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.
    • (2009) Nat. Rev. Microbiol. , vol.7 , pp. 642-653
    • Adams, D.W.1    Errington, J.2
  • 9
    • 33746358181 scopus 로고    scopus 로고
    • Dynamic filaments of the bacterial cytoskeleton
    • DOI 10.1146/annurev.biochem.75.103004.142452
    • Michie KA, Lowe J (2006) Dynamic filaments of the bacterial cytoskeleton. Annu. Rev. Biochem. 75: 467-492. (Pubitemid 44118040)
    • (2006) Annual Review of Biochemistry , vol.75 , pp. 467-492
    • Michie, K.A.1    Lowe, J.2
  • 10
    • 79952403634 scopus 로고    scopus 로고
    • Identification and characterization of ZapC, a stabilizer of the FtsZ ring in Escherichia coli
    • Durand-Heredia JM, Yu HH, De Carlo S, Lesser CF, Janakiraman A (2011) Identification and characterization of ZapC, a stabilizer of the FtsZ ring in Escherichia coli. J. Bacteriol. 193: 1405-1413.
    • (2011) J. Bacteriol. , vol.193 , pp. 1405-1413
    • Durand-Heredia, J.M.1    Yu, H.H.2    De Carlo, S.3    Lesser, C.F.4    Janakiraman, A.5
  • 11
    • 79952401787 scopus 로고    scopus 로고
    • Identification of Escherichia coli ZapC (YcbW) as a component of the division apparatus that binds and bundles FtsZ polymers
    • Hale CA, Shiomi D, Liu B, Bernhardt TG, Margolin W, et al. (2011) Identification of Escherichia coli ZapC (YcbW) as a component of the division apparatus that binds and bundles FtsZ polymers. J. Bacteriol. 193: 1393-1404.
    • (2011) J. Bacteriol. , vol.193 , pp. 1393-1404
    • Hale, C.A.1    Shiomi, D.2    Liu, B.3    Bernhardt, T.G.4    Margolin, W.5
  • 12
    • 34548630230 scopus 로고    scopus 로고
    • Assembly dynamics of the bacterial MinCDE system and spatial regulation of the Z ring
    • Lutkenhaus J (2007) Assembly dynamics of the bacterial MinCDE system and spatial regulation of the Z ring. Annu. Rev. Biochem. 76: 539-562.
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 539-562
    • Lutkenhaus, J.1
  • 13
    • 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.
    • (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
  • 14
    • 78650910561 scopus 로고    scopus 로고
    • Molecular mechanism by which the nucleoid occlusion factor, SlmA, keeps cytokinesis in check
    • Tonthat NK, Arold ST, Pickering BF, Van Dyke MW, Liang S, et al. (2011) Molecular mechanism by which the nucleoid occlusion factor, SlmA, keeps cytokinesis in check. EMBO J. 30: 154-164.
    • (2011) EMBO J. , vol.30 , pp. 154-164
    • Tonthat, N.K.1    Arold, S.T.2    Pickering, B.F.3    Van Dyke, M.W.4    Liang, S.5
  • 15
    • 64149089661 scopus 로고    scopus 로고
    • The conserved C-terminal tail of FtsZ is required for the septal localization and division inhibitory activity of MinC(C)/MinD
    • Shen B, Lutkenhaus J (2009) The conserved C-terminal tail of FtsZ is required for the septal localization and division inhibitory activity of MinC(C)/MinD. Mol. Microbiol. 72: 410-424.
    • (2009) Mol. Microbiol. , vol.72 , pp. 410-424
    • Shen, B.1    Lutkenhaus, J.2
  • 16
    • 0032786248 scopus 로고    scopus 로고
    • Genetic and functional analyses of the conserved C-terminal core domain of Escherichia coli FtsZ
    • Ma X, Margolin W (1999) Genetic and functional analyses of the conserved C-terminal core domain of Escherichia coli FtsZ. J. Bacteriol. 181: 7531-7544.
    • (1999) J. Bacteriol. , vol.181 , pp. 7531-7544
    • Ma, X.1    Margolin, W.2
  • 17
    • 77349085366 scopus 로고    scopus 로고
    • Examination of the interaction between FtsZ and MinCN in E. coli suggests how MinC disrupts Z rings
    • Shen B, Lutkenhaus J (2010) Examination of the interaction between FtsZ and MinCN in E. coli suggests how MinC disrupts Z rings. Mol. Microbiol. 75: 1285-1298.
    • (2010) Mol. Microbiol. , vol.75 , pp. 1285-1298
    • Shen, B.1    Lutkenhaus, J.2
  • 18
    • 39249085850 scopus 로고    scopus 로고
    • MinC spatially controls bacterial cytokinesis by antagonizing the scaffolding function of FtsZ
    • Dajkovic A, Lan G, Sun SX, Wirtz D, Lutkenhaus J (2008) MinC spatially controls bacterial cytokinesis by antagonizing the scaffolding function of FtsZ. Curr. Biol. 18: 235-244.
    • (2008) Curr. Biol. , vol.18 , pp. 235-244
    • Dajkovic, A.1    Lan, G.2    Sun, S.X.3    Wirtz, D.4    Lutkenhaus, J.5
  • 19
    • 0027364289 scopus 로고
    • ClpX, an alternative subunit for the ATP-dependent Clp protease of Escherichia coli. Sequence and in vivo activities
    • Gottesman S, Clark WP, de Crecy-Lagard V, Maurizi MR (1993) ClpX, an alternative subunit for the ATP-dependent Clp protease of Escherichia coli. Sequence and in vivo activities. J. Biol. Chem. 268: 22618-22626. (Pubitemid 23318317)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.30 , pp. 22618-22626
    • Gottesman, S.1    Clark, W.P.2    De Crecy-Lagard, V.3    Maurizi, M.R.4
  • 20
    • 84872856522 scopus 로고    scopus 로고
    • The physiology of bacterial cell division
    • Egan AJ, Vollmer W (2013) The physiology of bacterial cell division. Annals N. Y. Acad. Sci. 1277: 8-28.
    • (2013) Annals N. Y. Acad. Sci. , vol.1277 , pp. 8-28
    • Egan, A.J.1    Vollmer, W.2
  • 21
    • 0037351068 scopus 로고    scopus 로고
    • Proteomic discovery of cellular substrates of the ClpXP protease reveals five classes of ClpX-recognition signals
    • DOI 10.1016/S1097-2765(03)00060-1
    • Flynn JM, Neher SB, Kim YI, Sauer RT, Baker TA (2003) Proteomic discovery of cellular substrates of the ClpXP protease reveals five classes of ClpX-recognition signals. Mol. Cell 11: 671-683. (Pubitemid 36388762)
    • (2003) Molecular Cell , vol.11 , Issue.3 , pp. 671-683
    • Flynn, J.M.1    Neher, S.B.2    Kim, Y.-I.3    Sauer, R.T.4    Baker, T.A.5
  • 22
    • 0035216867 scopus 로고    scopus 로고
    • BAD promoter in Escherichia coli by constitutive expression of the low-affinity high-capacity araE transporter
    • Khlebnikov A, Datsenko KA, Skaug T, Wanner BL, Keasling JD (2001) Homogeneous expression of the P(BAD) promoter in Escherichia coli by constitutive expression of the low-affinity high-capacity AraE transporter. Microbiology 147: 3241-3247. (Pubitemid 33150330)
    • (2001) Microbiology , vol.147 , Issue.12 , pp. 3241-3247
    • Khlebnikov, A.1    Datsenko, K.A.2    Skaug, T.3    Wanner, B.L.4    Keasling, J.D.5
  • 24
    • 0029018327 scopus 로고
    • Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter
    • Guzman LM, Belin D, Carson MJ, Beckwith J (1995) Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter. J. Bacteriol. 177: 4121-4130.
    • (1995) J. Bacteriol. , vol.177 , pp. 4121-4130
    • Guzman, L.M.1    Belin, D.2    Carson, M.J.3    Beckwith, J.4
  • 25
    • 79955460424 scopus 로고    scopus 로고
    • The interplay of ClpXP with the cell division machinery in Escherichia coli
    • Camberg JL, Hoskins JR, Wickner S (2011) The interplay of ClpXP with the cell division machinery in Escherichia coli. J. Bacteriol. 193: 1911-1918.
    • (2011) J. Bacteriol. , vol.193 , pp. 1911-1918
    • Camberg, J.L.1    Hoskins, J.R.2    Wickner, S.3
  • 26
    • 0032524297 scopus 로고    scopus 로고
    • Enzymatic and structural similarities between the Escherichia coli ATP- dependent proteases, ClpXP and ClpAP
    • DOI 10.1074/jbc.273.20.12476
    • Grimaud R, Kessel M, Beuron F, Steven AC, Maurizi MR (1998) Enzymatic and structural similarities between the Escherichia coli ATP- dependent proteases, ClpXP and ClpAP. J. Biol. Chem. 273: 12476-12481. (Pubitemid 28240621)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.20 , pp. 12476-12481
    • Grimaud, R.1    Kessel, M.2    Beuron, F.3    Steven, A.C.4    Maurizi, M.R.5
  • 27
    • 0028674499 scopus 로고
    • Endopeptidase Clp: ATP-dependent Clp protease from Escherichia coli
    • Maurizi MR, Thompson MW, Singh SK, Kim SH (1994) Endopeptidase Clp: ATP-dependent Clp protease from Escherichia coli. Methods Enzymol. 244: 314-331.
    • (1994) Methods Enzymol. , vol.244 , pp. 314-331
    • Maurizi, M.R.1    Thompson, M.W.2    Singh, S.K.3    Kim, S.H.4
  • 29
    • 0242584670 scopus 로고    scopus 로고
    • Essential cell division protein FtsZ assembles into one monomer-thick ribbons under conditions resembling the crowded intracellular environment
    • DOI 10.1074/jbc.M305230200
    • Gonzalez JM, Jimenez M, Velez M, Mingorance J, Andreu JM, et al. (2003) Essential cell division protein FtsZ assembles into one monomer-thick ribbons under conditions resembling the crowded intracellular environment. J. Biol. Chem. 278: 37664-37671. (Pubitemid 37175290)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.39 , pp. 37664-37671
    • Gonzalez, J.M.1    Jimenez, M.2    Velez, M.3    Mingorance, J.4    Andreu, J.M.5    Vicente, M.6    Rivas, G.7
  • 30
    • 0030815131 scopus 로고    scopus 로고
    • Ca2+-mediated GTP-dependent dynamic assembly of bacterial cell division protein FtsZ into asters and polymer networks in vitro
    • Yu XC, Margolin W (1997) Ca2+-mediated GTP-dependent dynamic assembly of bacterial cell division protein FtsZ into asters and polymer networks in vitro. EMBO J. 16: 5455-5463.
    • (1997) EMBO J. , vol.16 , pp. 5455-5463
    • Yu, X.C.1    Margolin, W.2
  • 31
    • 84859484529 scopus 로고    scopus 로고
    • Extreme C terminus of bacterial cytoskeletal protein FtsZ plays fundamental role in assembly independent of modulatory proteins
    • Buske PJ, Levin PA (2012) Extreme C terminus of bacterial cytoskeletal protein FtsZ plays fundamental role in assembly independent of modulatory proteins. J. Biol. Chem. 287: 10945-10957.
    • (2012) J. Biol. Chem. , vol.287 , pp. 10945-10957
    • Buske, P.J.1    Levin, P.A.2
  • 32
    • 0034600952 scopus 로고    scopus 로고
    • The bacterial cell-division protein ZipA and its interaction with an FtsZ fragment revealed by X-ray crystallography
    • Mosyak L, Zhang Y, Glasfeld E, Haney S, Stahl M, et al. (2000) The bacterial cell-division protein ZipA and its interaction with an FtsZ fragment revealed by X-ray crystallography. EMBO J. 19: 3179-3191. (Pubitemid 30428197)
    • (2000) EMBO Journal , vol.19 , Issue.13 , pp. 3179-3191
    • Mosyak, L.1    Zhang, Y.2    Glasfeld, E.3    Haney, S.4    Stahl, M.5    Seehra, J.6    Somers, W.S.7
  • 34
    • 84880136225 scopus 로고    scopus 로고
    • The C-terminal linker of Escherichia coli FtsZ functions as an intrinsically disordered peptide
    • Gardner KA, Moore DA, Erickson HP (2013) The C-terminal linker of Escherichia coli FtsZ functions as an intrinsically disordered peptide. Mol. Microbiol. 89: 264-275.
    • (2013) Mol. Microbiol. , vol.89 , pp. 264-275
    • Gardner, K.A.1    Moore, D.A.2    Erickson, H.P.3
  • 36
    • 33847108004 scopus 로고    scopus 로고
    • Structural Basis of SspB-tail Recognition by the Zinc Binding Domain of ClpX
    • DOI 10.1016/j.jmb.2007.01.003, PII S0022283607000046
    • Park EY, Lee BG, Hong SB, Kim HW, Jeon H, et al. (2007) Structural basis of SspB-tail recognition by the zinc binding domain of ClpX. J. Mol. Biol. 367: 514-526. (Pubitemid 46295430)
    • (2007) Journal of Molecular Biology , vol.367 , Issue.2 , pp. 514-526
    • Park, E.Y.1    Lee, B.-G.2    Hong, S.-B.3    Kim, H.-W.4    Jeon, H.5    Song, H.K.6
  • 37
    • 0141888401 scopus 로고    scopus 로고
    • Flexible linkers leash the substrate binding domain of SspB to a peptide module that stabilizes delivery complexes with the AAA+ ClpXP protease
    • DOI 10.1016/S1097-2765(03)00272-7
    • Wah DA, Levchenko I, Rieckhof GE, Bolon DN, Baker TA, et al. (2003) Flexible linkers leash the substrate binding domain of SspB to a peptide module that stabilizes delivery complexes with the AAA+ ClpXP protease. Mol. Cell 12: 355-363. (Pubitemid 37238922)
    • (2003) Molecular Cell , vol.12 , Issue.2 , pp. 355-363
    • Wah, D.A.1    Levchenko, I.2    Rieckhof, G.E.3    Bolon, D.N.4    Baker, T.A.5    Sauer, R.T.6
  • 38
    • 21244482459 scopus 로고    scopus 로고
    • 6 unfoldase: Allosteric control of a protein machine
    • DOI 10.1016/j.cell.2005.05.024, PII S0092867405005039
    • Hersch GL, Burton RE, Bolon DN, Baker TA, Sauer RT (2005) Asymmetric interactions of ATP with the AAA + ClpX6 unfoldase: allosteric control of a protein machine. Cell 121: 1017-1027. (Pubitemid 40884394)
    • (2005) Cell , vol.121 , Issue.7 , pp. 1017-1027
    • Hersch, G.L.1    Burton, R.E.2    Bolon, D.N.3    Baker, T.A.4    Sauer, R.T.5
  • 39
    • 0034751570 scopus 로고    scopus 로고
    • The dimerization function of MinC resides in a structurally autonomous C-terminal domain
    • DOI 10.1128/JB.183.22.6684-6687.2001
    • Szeto TH, Rowland SL, King GF (2001) The dimerization function of MinC resides in a structurally autonomous C-terminal domain. J. Bacteriol. 183: 6684-6687. (Pubitemid 33026761)
    • (2001) Journal of Bacteriology , vol.183 , Issue.22 , pp. 6684-6687
    • Szeto, T.H.1    Rowland, S.L.2    King, G.F.3
  • 40
    • 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.
    • (2010) Microbiol. Mol. Biol. Rev. , vol.74 , pp. 504-528
    • Erickson, H.P.1    Anderson, D.E.2    Osawa, M.3
  • 41
    • 0027167446 scopus 로고
    • Cloning and characterization of ftsN, an essential cell division gene in Escherichia coli isolated as a multicopy suppressor of ftsA12(Ts)
    • Dai K, Xu Y, Lutkenhaus J (1993) Cloning and characterization of ftsN, an essential cell division gene in Escherichia coli isolated as a multicopy suppressor of ftsA12(Ts). J. Bacteriol. 175: 3790-3797. (Pubitemid 23173341)
    • (1993) Journal of Bacteriology , vol.175 , Issue.12 , pp. 3790-3797
    • Dai, K.1    Xu, Y.2    Lutkenhaus, J.3
  • 43
    • 77949908054 scopus 로고    scopus 로고
    • AAA+ chaperone ClpX regulates dynamics of prokaryotic cytoskeletal protein FtsZ
    • Sugimoto S, Yamanaka K, Nishikori S, Miyagi A, Ando T, et al. (2010) AAA+ chaperone ClpX regulates dynamics of prokaryotic cytoskeletal protein FtsZ. J. Biol. Chem. 285: 6648-6657.
    • (2010) J. Biol. Chem. , vol.285 , pp. 6648-6657
    • Sugimoto, S.1    Yamanaka, K.2    Nishikori, S.3    Miyagi, A.4    Ando, T.5
  • 44
    • 84873286335 scopus 로고    scopus 로고
    • A specific role for the ZipA protein in cell division: Stabilization of the FtsZ protein
    • Pazos M, Natale P, Vicente M (2012) A specific role for the ZipA protein in cell division: stabilization of the FtsZ protein. J. Biol. Chem. 288: 3219-3226.
    • (2012) J. Biol. Chem. , vol.288 , pp. 3219-3226
    • Pazos, M.1    Natale, P.2    Vicente, M.3
  • 45
    • 84873401017 scopus 로고    scopus 로고
    • Trapping and Proteomic Identification of Cellular Substrates of the ClpP Protease in Staphylococcus aureus
    • Feng J, Michalik S, Varming AN, Andersen JH, Albrecht D, et al. (2013) Trapping and Proteomic Identification of Cellular Substrates of the ClpP Protease in Staphylococcus aureus. J. Proteome. Res. 12: 547-558.
    • (2013) J. Proteome. Res. , vol.12 , pp. 547-558
    • Feng, J.1    Michalik, S.2    Varming, A.N.3    Andersen, J.H.4    Albrecht, D.5
  • 46
    • 63049127158 scopus 로고    scopus 로고
    • ClpX inhibits FtsZ assembly in a manner that does not require its ATP hydrolysis-dependent chaperone activity
    • Haeusser DP, Lee AH, Weart RB, Levin PA (2009) ClpX inhibits FtsZ assembly in a manner that does not require its ATP hydrolysis-dependent chaperone activity. J. Bacteriol. 191: 1986-1991.
    • (2009) J. Bacteriol. , vol.191 , pp. 1986-1991
    • Haeusser, D.P.1    Lee, A.H.2    Weart, R.B.3    Levin, P.A.4
  • 47
    • 77955374003 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis ClpX Interacts with FtsZ and Interferes with FtsZ Assembly
    • Dziedzic R, Kiran M, Plocinski P, Ziolkiewicz M, Brzostek A, et al. (2010) Mycobacterium tuberculosis ClpX Interacts with FtsZ and Interferes with FtsZ Assembly. PloS one 5: e11058.
    • (2010) PloS One , vol.5
    • Dziedzic, R.1    Kiran, M.2    Plocinski, P.3    Ziolkiewicz, M.4    Brzostek, A.5
  • 48
    • 0032518656 scopus 로고    scopus 로고
    • Dynamic assembly of FtsZ regulated by GTP hydrolysis
    • DOI 10.1093/emboj/17.2.462
    • Mukherjee A, Lutkenhaus J (1998) Dynamic assembly of FtsZ regulated by GTP hydrolysis. EMBO J. 17: 462-469. (Pubitemid 28045487)
    • (1998) EMBO Journal , vol.17 , Issue.2 , pp. 462-469
    • Mukherjee, A.1    Lutkenhaus, J.2


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