메뉴 건너뛰기




Volumn 67, Issue 1, 2007, Pages 177-188

Acid-induced loss of functional properties of bacterial cell division protein FtsZ: Evidence for an alternative conformation at acidic pH

Author keywords

FtsZ assembly dynamics; GTP binding; GTP hydrolysis; Intermediate; Lifetime; Molten globule state; Productive aggregates; Unfolding of FtsZ

Indexed keywords

FTSZ PROTEIN; GUANOSINE TRIPHOSPHATASE; GUANOSINE TRIPHOSPHATE;

EID: 33847411950     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.21178     Document Type: Article
Times cited : (14)

References (55)
  • 1
    • 0026059127 scopus 로고
    • Fts Z ring structure associated with division in Escherichia coli
    • Bi EF, Lutkenhaus J. Fts Z ring structure associated with division in Escherichia coli. Nature 1991;354:161-164.
    • (1991) Nature , vol.354 , pp. 161-164
    • Bi, E.F.1    Lutkenhaus, J.2
  • 3
    • 0036019535 scopus 로고    scopus 로고
    • The tubulin ancestor, FtsZ, draughtsman, designer and driving force for bacterial cytokinesis
    • Addinall SG, Holland B. The tubulin ancestor, FtsZ, draughtsman, designer and driving force for bacterial cytokinesis. J Mol Biol 2002;318:219-236.
    • (2002) J Mol Biol , vol.318 , pp. 219-236
    • Addinall, S.G.1    Holland, B.2
  • 4
    • 0031466635 scopus 로고    scopus 로고
    • Bacterial cell division
    • Bramhill D. Bacterial cell division. Annu Rev Cell Dev Biol 1997;13:395-424.
    • (1997) Annu Rev Cell Dev Biol , vol.13 , pp. 395-424
    • Bramhill, D.1
  • 5
    • 0037022642 scopus 로고    scopus 로고
    • Rapid assembly dynamics of the Escherichia coli FtsZ-ring demonstrated by fluorescence recovery after photobleaching
    • Stricker J, Maddox P, Salmon ED, Erickson HP. Rapid assembly dynamics of the Escherichia coli FtsZ-ring demonstrated by fluorescence recovery after photobleaching. Proc Natl Acad Sci USA 2002;99:3171-3175.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 3171-3175
    • Stricker, J.1    Maddox, P.2    Salmon, E.D.3    Erickson, H.P.4
  • 6
    • 0030956145 scopus 로고    scopus 로고
    • Bacterial cell division and the Z ring
    • Lutkenhaus J, Addinall SG. Bacterial cell division and the Z ring. Annu Rev Biochem 1997;66:93-116.
    • (1997) Annu Rev Biochem , vol.66 , pp. 93-116
    • Lutkenhaus, J.1    Addinall, S.G.2
  • 8
    • 2642593025 scopus 로고    scopus 로고
    • Crystal structure of the bacterial cell-division protein FtsZ
    • Lowe J, Amos LA. Crystal structure of the bacterial cell-division protein FtsZ. Nature 1998;391:203-206.
    • (1998) Nature , vol.391 , pp. 203-206
    • Lowe, J.1    Amos, L.A.2
  • 9
    • 0032495513 scopus 로고    scopus 로고
    • Structure of the αβ tubulin dimer by electron crystallography
    • Nogales E, Wolf SG, Downing KH. Structure of the αβ tubulin dimer by electron crystallography. Nature 1998;391:199-203.
    • (1998) Nature , vol.391 , pp. 199-203
    • Nogales, E.1    Wolf, S.G.2    Downing, K.H.3
  • 11
    • 0031914188 scopus 로고    scopus 로고
    • Atomic structures of tubulin and FtsZ
    • Erickson HP. Atomic structures of tubulin and FtsZ. Trends Cell Biol 1998;8:133-137.
    • (1998) Trends Cell Biol , vol.8 , pp. 133-137
    • Erickson, H.P.1
  • 12
    • 0028290692 scopus 로고
    • GTP-dependent polymerization of Escherichia coli FtsZ protein to form tubules
    • Bramhill D, Thompson CM. GTP-dependent polymerization of Escherichia coli FtsZ protein to form tubules. Proc Natl Acad Sci USA 1994;91:5813-5817.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 5813-5817
    • Bramhill, D.1    Thompson, C.M.2
  • 13
    • 0032518656 scopus 로고    scopus 로고
    • Dynamic assembly of FtsZ regulated by GTP hydrolysis
    • Mukherjee A, Lutkenhaus J. Dynamic assembly of FtsZ regulated by GTP hydrolysis. EMBO J 1998;17:462-469.
    • (1998) EMBO J , vol.17 , pp. 462-469
    • Mukherjee, A.1    Lutkenhaus, J.2
  • 14
    • 0031968795 scopus 로고    scopus 로고
    • FtsZ from Escherichia coli, Azotobacter vinelandii, and Thermotoga maritima-quantitation, GTP hydrolysis, and assembly
    • Lu C, Stricker J, Erickson HP. FtsZ from Escherichia coli, Azotobacter vinelandii, and Thermotoga maritima-quantitation, GTP hydrolysis, and assembly. Cell Motil Cytoskeleton 1998;40:71-86.
    • (1998) Cell Motil Cytoskeleton , vol.40 , pp. 71-86
    • Lu, C.1    Stricker, J.2    Erickson, H.P.3
  • 16
    • 0019409829 scopus 로고
    • The effect of ruthenium red on the assembly and disassembly of microtubules and on rapid axonal transport
    • Deinum J, Wallin M, Kanje M, Lagercrantz C. The effect of ruthenium red on the assembly and disassembly of microtubules and on rapid axonal transport. Biochim Biophys Acta 1981;675:209-213.
    • (1981) Biochim Biophys Acta , vol.675 , pp. 209-213
    • Deinum, J.1    Wallin, M.2    Kanje, M.3    Lagercrantz, C.4
  • 17
    • 2942709709 scopus 로고    scopus 로고
    • Ruthenium red-induced bundling of bacterial cell division protein
    • Santra MK, Beuria TK, Banerjee A, Panda D. Ruthenium red-induced bundling of bacterial cell division protein. J Biol Chem 2004;279:25959-25965.
    • (2004) J Biol Chem , vol.279 , pp. 25959-25965
    • Santra, M.K.1    Beuria, T.K.2    Banerjee, A.3    Panda, D.4
  • 19
    • 0032916717 scopus 로고    scopus 로고
    • Analysis of FtsZ assembly by light scattering and determination of the role of divalent metal cations
    • Mukherjee A, Lutkenhaus J. Analysis of FtsZ assembly by light scattering and determination of the role of divalent metal cations. J Bacteriol 1999;181:823-832.
    • (1999) J Bacteriol , vol.181 , pp. 823-832
    • Mukherjee, A.1    Lutkenhaus, J.2
  • 20
    • 0030815131 scopus 로고    scopus 로고
    • 2+-mediated GTP-dependent dynamic assembly of bacterial cell division protein FtsZ into asters and polymer networks in vitro. EMBO J 1997;16:5455-5463.
    • 2+-mediated GTP-dependent dynamic assembly of bacterial cell division protein FtsZ into asters and polymer networks in vitro. EMBO J 1997;16:5455-5463.
  • 21
    • 0032562286 scopus 로고    scopus 로고
    • Inhibition of assembly of bacterial cell division protein FtsZ by the hydrophobic dye 5,5′-bis-(8-anilino-1- naphthalenesulfonate)
    • Yu XC, Margolin W. Inhibition of assembly of bacterial cell division protein FtsZ by the hydrophobic dye 5,5′-bis-(8-anilino-1- naphthalenesulfonate). J Biol Chem 1998;273:10216-10222.
    • (1998) J Biol Chem , vol.273 , pp. 10216-10222
    • Yu, X.C.1    Margolin, W.2
  • 22
    • 0030871206 scopus 로고    scopus 로고
    • Refolding of urea-denatured tubulin: Recovery of native like structure and colchicine binding activity from partly unfolded states
    • Guha S, Bhattacharyya B. Refolding of urea-denatured tubulin: recovery of native like structure and colchicine binding activity from partly unfolded states. Biochemistry 1997;36:13208-13213.
    • (1997) Biochemistry , vol.36 , pp. 13208-13213
    • Guha, S.1    Bhattacharyya, B.2
  • 23
    • 0029004398 scopus 로고
    • A partially folded intermediate during tubulin unfolding: Its detection and spectroscopic characterization
    • Guha S, Bhattacharyya B. A partially folded intermediate during tubulin unfolding: its detection and spectroscopic characterization. Biochemistry 1995;34:6925-6931.
    • (1995) Biochemistry , vol.34 , pp. 6925-6931
    • Guha, S.1    Bhattacharyya, B.2
  • 24
    • 0038691618 scopus 로고    scopus 로고
    • Detection of an intermediate during unfolding of bacterial cell division protein FtsZ: Loss of functional properties precedes the global unfolding of FtsZ
    • Santra MK, Panda D. Detection of an intermediate during unfolding of bacterial cell division protein FtsZ: loss of functional properties precedes the global unfolding of FtsZ. J Biol Chem 2003;278:21336-21343.
    • (2003) J Biol Chem , vol.278 , pp. 21336-21343
    • Santra, M.K.1    Panda, D.2
  • 26
    • 0025195499 scopus 로고
    • Mechanism of acid-induced folding of proteins
    • Goto Y, Takahashi N, Fink AL. Mechanism of acid-induced folding of proteins. Biochemistry 1990;29:3480-3488.
    • (1990) Biochemistry , vol.29 , pp. 3480-3488
    • Goto, Y.1    Takahashi, N.2    Fink, A.L.3
  • 27
    • 0028053016 scopus 로고
    • Equilibrium unfolding studies of barstar: Evidence for an alternative conformation which resembles a molten globule
    • Khurana R, Udgaonkar JB. Equilibrium unfolding studies of barstar: evidence for an alternative conformation which resembles a molten globule. Biochemistry 1994;33:106-115.
    • (1994) Biochemistry , vol.33 , pp. 106-115
    • Khurana, R.1    Udgaonkar, J.B.2
  • 28
    • 0025186451 scopus 로고
    • Structural characterization of a partly folded apomyoglobin intermediate
    • Hughson FM, Wright PE, Baldwin RL. Structural characterization of a partly folded apomyoglobin intermediate. Science 1990;249:1544-1548.
    • (1990) Science , vol.249 , pp. 1544-1548
    • Hughson, F.M.1    Wright, P.E.2    Baldwin, R.L.3
  • 29
    • 0029124248 scopus 로고
    • Molten globule and protein folding
    • Ptitsyn OB. Molten globule and protein folding. Adv Protein Chem 1995;47:83-229.
    • (1995) Adv Protein Chem , vol.47 , pp. 83-229
    • Ptitsyn, O.B.1
  • 30
    • 4344596240 scopus 로고    scopus 로고
    • Nonspecific hydrophobic interactions stabilize an equilibrium intermediate of apomyoglobin at a key position within the AGH region
    • Bertagna AM, Barrick D. Nonspecific hydrophobic interactions stabilize an equilibrium intermediate of apomyoglobin at a key position within the AGH region. Proc Natl Acad Sci USA 2004;101:12514-12519.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 12514-12519
    • Bertagna, A.M.1    Barrick, D.2
  • 31
    • 0035035812 scopus 로고    scopus 로고
    • A glutamate decarboxylase system protects Listeria monocytogenes in gastric fluid
    • Cotter PD, Gahan CG, Hill C. A glutamate decarboxylase system protects Listeria monocytogenes in gastric fluid. Mol Microbiol 2001;40:465-475.
    • (2001) Mol Microbiol , vol.40 , pp. 465-475
    • Cotter, P.D.1    Gahan, C.G.2    Hill, C.3
  • 32
    • 0029073161 scopus 로고
    • Comparative analysis of extreme acid survival in Salmonella typhimurium, Shigella flexneri, and Escherichia coli
    • Lin J, Lee IS, Frey J, Slonczewski JL, Foster JW. Comparative analysis of extreme acid survival in Salmonella typhimurium, Shigella flexneri, and Escherichia coli. J Bacteriol 1995;177:4097-4104.
    • (1995) J Bacteriol , vol.177 , pp. 4097-4104
    • Lin, J.1    Lee, I.S.2    Frey, J.3    Slonczewski, J.L.4    Foster, J.W.5
  • 34
    • 4444226939 scopus 로고    scopus 로고
    • Escherichia coli glutamate- and arginine-dependent acid resistance systems increase internal pH and reverse transmembrane potential
    • Richard H, Foster JW. Escherichia coli glutamate- and arginine-dependent acid resistance systems increase internal pH and reverse transmembrane potential. J Bacteriol 2004;186:6032-6041.
    • (2004) J Bacteriol , vol.186 , pp. 6032-6041
    • Richard, H.1    Foster, J.W.2
  • 35
    • 0038107561 scopus 로고    scopus 로고
    • The role of gastric acid in preventing food borne disease and how bacteria overcome acid conditions
    • Smith JL. The role of gastric acid in preventing food borne disease and how bacteria overcome acid conditions. J Food Prot 2003;66:1292-1303.
    • (2003) J Food Prot , vol.66 , pp. 1292-1303
    • Smith, J.L.1
  • 36
    • 0345687928 scopus 로고    scopus 로고
    • pH-Dependent modulation of cyclic AMP levels and GadW-dependent repression of RpoS affect synthesis of the GadX regulator and Escherichia coli acid resistance
    • Ma Z, Richard H, Foster JW. pH-Dependent modulation of cyclic AMP levels and GadW-dependent repression of RpoS affect synthesis of the GadX regulator and Escherichia coli acid resistance. J Bacteriol 2003;185:6852-6859.
    • (2003) J Bacteriol , vol.185 , pp. 6852-6859
    • Ma, Z.1    Richard, H.2    Foster, J.W.3
  • 37
    • 28644447479 scopus 로고    scopus 로고
    • Deuterium oxide promotes assembly and bundling of FtsZ protofilaments
    • Santra MK, Dasgupta D, Panda D. Deuterium oxide promotes assembly and bundling of FtsZ protofilaments. Proteins 2005;61:1101-1110.
    • (2005) Proteins , vol.61 , pp. 1101-1110
    • Santra, M.K.1    Dasgupta, D.2    Panda, D.3
  • 38
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 1976;72:248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 39
    • 0028100451 scopus 로고
    • Acid-induced reversible unfolding of mitochondrial aspartate aminotransferase
    • Artigues A, Iriarte A, Martinez-Carrion M. Acid-induced reversible unfolding of mitochondrial aspartate aminotransferase. J Biol Chem 1994;269:21990-21999.
    • (1994) J Biol Chem , vol.269 , pp. 21990-21999
    • Artigues, A.1    Iriarte, A.2    Martinez-Carrion, M.3
  • 40
    • 0032568639 scopus 로고    scopus 로고
    • Alternative models for describing the acid unfolding of the apomyoglobin folding intermediate
    • Kay MS, Baldwin RL. Alternative models for describing the acid unfolding of the apomyoglobin folding intermediate. Biochemistry 1998;37:7859-7868.
    • (1998) Biochemistry , vol.37 , pp. 7859-7868
    • Kay, M.S.1    Baldwin, R.L.2
  • 41
    • 0027245421 scopus 로고
    • Three-state analysis of sperm whale apomyoglobin folding
    • Barrick D, Baldwin RL. Three-state analysis of sperm whale apomyoglobin folding. Biochemistry 1993;32:3790-3796.
    • (1993) Biochemistry , vol.32 , pp. 3790-3796
    • Barrick, D.1    Baldwin, R.L.2
  • 42
    • 2342588126 scopus 로고    scopus 로고
    • Multiple-probe analysis of folding and unfolding pathways of human serum albumin. Evidence for a framework mechanism of folding
    • Santra MK, Banerjee A, Krishnakumar SS, Rahaman O, Panda D. Multiple-probe analysis of folding and unfolding pathways of human serum albumin. Evidence for a framework mechanism of folding. Eur J Biochem 2004;271:1789-1797.
    • (2004) Eur J Biochem , vol.271 , pp. 1789-1797
    • Santra, M.K.1    Banerjee, A.2    Krishnakumar, S.S.3    Rahaman, O.4    Panda, D.5
  • 43
    • 33847340554 scopus 로고    scopus 로고
    • Ligand-receptor energetics
    • 19pp
    • KoltZ IM. Ligand-receptor energetics. New York: Wiley; 1997. 19pp.
    • (1997) New York: Wiley
    • KoltZ, I.M.1
  • 45
    • 0022555885 scopus 로고
    • Determination and analysis of urea and guanidine hydrochloride denaturation curves
    • Pace CN. Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods Enzymol 1986;131:266-280.
    • (1986) Methods Enzymol , vol.131 , pp. 266-280
    • Pace, C.N.1
  • 46
    • 0027155577 scopus 로고
    • Engineered disulfide bonds as probes of the folding pathway of barnase: Increasing the stability of proteins against the rate of denaturation
    • Clarke J, Fersht AR. Engineered disulfide bonds as probes of the folding pathway of barnase: increasing the stability of proteins against the rate of denaturation. Biochemistry 1993;32:4322-4329.
    • (1993) Biochemistry , vol.32 , pp. 4322-4329
    • Clarke, J.1    Fersht, A.R.2
  • 47
    • 20444474170 scopus 로고    scopus 로고
    • A natural osmolyte trimethylamine N-oxide promotes assembly and bundling of the bacterial cell division protein, FtsZ and counteracts the denaturing effects of urea
    • Mukherjee A, Santra MK, Beuria TK, Panda D. A natural osmolyte trimethylamine N-oxide promotes assembly and bundling of the bacterial cell division protein, FtsZ and counteracts the denaturing effects of urea. FEBS J 2005;272:2760-2772.
    • (2005) FEBS J , vol.272 , pp. 2760-2772
    • Mukherjee, A.1    Santra, M.K.2    Beuria, T.K.3    Panda, D.4
  • 48
    • 0034614370 scopus 로고    scopus 로고
    • Productive and nonproductive intermediates in the folding of denatured rhodanese
    • Panda M, Gorovits BM, Horowitz PM. Productive and nonproductive intermediates in the folding of denatured rhodanese. J Biol Chem 2000;275:63-70.
    • (2000) J Biol Chem , vol.275 , pp. 63-70
    • Panda, M.1    Gorovits, B.M.2    Horowitz, P.M.3
  • 49
    • 0030347877 scopus 로고
    • On-pathway versus off-pathway folding intermediates
    • Baldwin RL. On-pathway versus off-pathway folding intermediates. Fold Des 1995;1:R1-R8.
    • (1995) Fold Des , vol.1
    • Baldwin, R.L.1
  • 51
    • 0031705420 scopus 로고    scopus 로고
    • Purification, assembly, and localization of FtsZ
    • Mukherjee A, Lutkenhaus J. Purification, assembly, and localization of FtsZ. Methods Enzymol 1998;298:296-305.
    • (1998) Methods Enzymol , vol.298 , pp. 296-305
    • Mukherjee, A.1    Lutkenhaus, J.2
  • 52
    • 19044391883 scopus 로고    scopus 로고
    • Site-specific mutations of FtsZ-effects on GTPase and in vitro assembly
    • Lu C, Stricker J, Erickson HP. Site-specific mutations of FtsZ-effects on GTPase and in vitro assembly. BMC Microbiol 2001;1:7-18.
    • (2001) BMC Microbiol , vol.1 , pp. 7-18
    • Lu, C.1    Stricker, J.2    Erickson, H.P.3
  • 53
    • 0043062671 scopus 로고    scopus 로고
    • In vivo characterization of Escherichia coli ftsZ mutants: Effects on Z-ring structure and function
    • Stricker J, Erickson HP. In vivo characterization of Escherichia coli ftsZ mutants: effects on Z-ring structure and function. J Bacteriol 2003;185:4796-4805.
    • (2003) J Bacteriol , vol.185 , pp. 4796-4805
    • Stricker, J.1    Erickson, H.P.2
  • 54
    • 0037080162 scopus 로고    scopus 로고
    • GTP hydrolysis of cell division protein FtsZ: Evidence that the active site is formed by the association of monomers
    • Scheffers DJ, de Wit JG, den Blaauwen T, Driessen AJ. GTP hydrolysis of cell division protein FtsZ: evidence that the active site is formed by the association of monomers. Biochemistry 2002;41:521-529.
    • (2002) Biochemistry , vol.41 , pp. 521-529
    • Scheffers, D.J.1    de Wit, J.G.2    den Blaauwen, T.3    Driessen, A.J.4
  • 55
    • 16844382689 scopus 로고    scopus 로고
    • Mutants of FtsZ targeting the protofilament interface: Effects on cell division and GTPase activity
    • Redick SD, Stricker J, Briscoe G, Erickson HP. Mutants of FtsZ targeting the protofilament interface: effects on cell division and GTPase activity. J Bacteriol 2005;187:2727-2736.
    • (2005) J Bacteriol , vol.187 , pp. 2727-2736
    • Redick, S.D.1    Stricker, J.2    Briscoe, G.3    Erickson, H.P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.