메뉴 건너뛰기




Volumn 19, Issue 8, 2010, Pages 1445-1460

A cytochrome c fusion protein domain for convenient detection, quantification, and enhanced production of membrane proteins in Escherichia coli - Expression and characterization of cytochrome-tagged complex I subunits

Author keywords

Bacillus subtilis; Covalently bound heme; Cytochrome c; Escherichia coli; Fusion proteins; MrpA; MrpD; NADH:quinone oxidoreductase; NuoH; NuoL; NuoM; NuoN

Indexed keywords

CYTOCHROME C; ESCHERICHIA COLI PROTEIN; HEME; MRPA PROTEIN CYTOCHROME C FUSION PROTEIN; MRPD PROTEIN CYTOCHROME C FUSION PROTEIN; NUOH PROTEIN; NUOH PROTEIN CYTOCHROME C FUSION PROTEIN; NUOL PROTEIN; NUOL PROTEIN CYTOCHROME C FUSION PROTEIN; NUOM PROTEIN; NUOM PROTEIN CYTOCHROME C FUSION PROTEIN; NUON PROTEIN; NUON PROTEIN CYTOCHROME C FUSION PROTEIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); UNCLASSIFIED DRUG;

EID: 77955105850     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.424     Document Type: Article
Times cited : (12)

References (47)
  • 1
    • 0037450574 scopus 로고    scopus 로고
    • Practical aspects of overexpressing bacterial secondary membrane transporters for structural studies
    • Wang DN, Safferling M, Lemieux MJ, Griffith H, Chen Y, Li XD (2003) Practical aspects of overexpressing bacterial secondary membrane transporters for structural studies. Biochim Biophys Acta 1610:23-36.
    • (2003) Biochim Biophys Acta , vol.1610 , pp. 23-36
    • Wang, D.N.1    Safferling, M.2    Lemieux, M.J.3    Griffith, H.4    Chen, Y.5    Li, X.D.6
  • 2
    • 0033943049 scopus 로고    scopus 로고
    • Escherichia coli translocase: The unravelling of a molecular machine
    • DOI 10.1046/j.1365-2958.2000.01980.x
    • Manting EH, Driessen AJM (2000) Escherichia coli translocase: the unravelling of a molecular machine. Mol Microbiol 37:226-238. (Pubitemid 30481008)
    • (2000) Molecular Microbiology , vol.37 , Issue.2 , pp. 226-238
    • Manting, E.H.1    Driessen, A.J.M.2
  • 3
    • 3843095033 scopus 로고    scopus 로고
    • Targeting and translocation of two lipoproteins in Escherichia coli via the SRP/Sec/YidC pathway
    • DOI 10.1074/jbc.M403229200
    • Fröderberg L, Houben ENG, Baars L, Luirink J, de Gier JW (2004) Targeting and translocation of two lipoproteins in Escherichia coli via the SRP/Sec/YidC pathway. J Biol Chem 279:31026-31032. (Pubitemid 39037762)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.30 , pp. 31026-31032
    • Froderberg, L.1    Houben, E.N.G.2    Baars, L.3    Luirink, J.4    De Gier, J.-W.5
  • 4
    • 33644872938 scopus 로고    scopus 로고
    • Structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus
    • DOI 10.1126/science.1123809
    • Sazanov LA, Hinchliffe P (2006) Structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus. Science 311:1430-1436. (Pubitemid 43376691)
    • (2006) Science , vol.311 , Issue.5766 , pp. 1430-1436
    • Sazanov, L.A.1    Hinchliffe, P.2
  • 5
    • 33847687662 scopus 로고    scopus 로고
    • Respiratory complex I: Mechanistic and structural insights provided by the crystal structure of the hydrophilic domain
    • Sazanov LA (2007) Respiratory complex I: mechanistic and structural insights provided by the crystal structure of the hydrophilic domain. Biochemistry 46: 2275-2288.
    • (2007) Biochemistry , vol.46 , pp. 2275-2288
    • Sazanov, L.A.1
  • 6
    • 33846270288 scopus 로고    scopus 로고
    • Projection structure of the membrane domain of Escherichia coli respiratory complex I at 8 angstrom resolution
    • Baranova EA, Holt PJ, Sazanov LA (2007) Projection structure of the membrane domain of Escherichia coli respiratory complex I at 8 angstrom resolution. J Mol Biol 366:140-154.
    • (2007) J Mol Biol , vol.366 , pp. 140-154
    • Baranova, E.A.1    Holt, P.J.2    Sazanov, L.A.3
  • 7
    • 0035795161 scopus 로고    scopus 로고
    • Transmembrane orientation and topology of the NADH: Quinone oxidoreductase putative quinone binding subunit NuoH
    • Roth R, Hägerhäll C (2001) Transmembrane orientation and topology of the NADH: quinone oxidoreductase putative quinone binding subunit NuoH. Biochim Biophys Acta 1504:352-362.
    • (2001) Biochim Biophys Acta , vol.1504 , pp. 352-362
    • Roth, R.1    Hägerhäll, C.2
  • 8
    • 0037010862 scopus 로고    scopus 로고
    • Transmembrane topology of the NuoL, M and N subunits of NADH: Quinone oxidoreductase and their homologues among membrane-bound hydrogenases and bona fide antiporters
    • Mathiesen C, Hägerhäll C (2002) Transmembrane topology of the NuoL, M and N subunits of NADH: quinone oxidoreductase and their homologues among membrane-bound hydrogenases and bona fide antiporters. Biochim Biophys Acta 1556:121-132.
    • (2002) Biochim Biophys Acta , vol.1556 , pp. 121-132
    • Mathiesen, C.1    Hägerhäll, C.2
  • 9
    • 0037006973 scopus 로고    scopus 로고
    • Characterization of the membrane domain Nqo11 subunit of the proton-translocating NADH-quinone oxidoreductase of Paracoccus denitrificans
    • DOI 10.1021/bi025525d
    • Kao MC, Di Bernardo S, Matsuno-Yagi A, Yagi T (2002) Characterization of the membrane domain Nqo11 subunit of the proton-translocating NADH-quinone oxidoreductase of Paracoccus denitrificans. Biochemistry 41:4377-4384. (Pubitemid 34259881)
    • (2002) Biochemistry , vol.41 , Issue.13 , pp. 4377-4384
    • Kao, M.-C.1    Di Bernardo, S.2    Matsuno-Yagi, A.3    Yagi, T.4
  • 10
    • 0037461290 scopus 로고    scopus 로고
    • Characterization and topology of the membrane domain Nqo10 subunit of the proton-translocating NADH-quinone oxidoreductase of Paracoccus denitrificanst
    • DOI 10.1021/bi034166z
    • Kao MC, Di Bernardo S, Matsuno-Yagi A, Yagi T (2003) Characterization and topology of the membrane domain Nqo10 subunit of the proton-translocating NADH-quinone oxidoreductase of Paracoccus denitrificans. Biochemistry 42:4534-4543. (Pubitemid 36457622)
    • (2003) Biochemistry , vol.42 , Issue.15 , pp. 4534-4543
    • Kao, M.-C.1    Di Bernardo, S.2    Matsuno-Yagi, A.3    Yagi, T.4
  • 11
  • 12
    • 0242322000 scopus 로고    scopus 로고
    • The location of NuoL and NuoM subunits in the membrane domain of the Escherichia coli complex I - Implications for the mechanism of proton pumping
    • Holt PJ, Morgan DJ, Sazanov LA (2003) The location of NuoL and NuoM subunits in the membrane domain of the Escherichia coli complex I - implications for the mechanism of proton pumping. J Biol Chem 278: 43114-43120.
    • (2003) J Biol Chem , vol.278 , pp. 43114-43120
    • Holt, P.J.1    Morgan, D.J.2    Sazanov, L.A.3
  • 13
    • 34547096741 scopus 로고    scopus 로고
    • Single particle analysis confirms distal location of subunits NuoL and NuoM in Escherichia coli complex I
    • Baranova EA, Morgan DJ, Sazanov LA (2007) Single particle analysis confirms distal location of subunits NuoL and NuoM in Escherichia coli complex I. J Struct Biol 159:238-242.
    • (2007) J Struct Biol , vol.159 , pp. 238-242
    • Baranova, E.A.1    Morgan, D.J.2    Sazanov, L.A.3
  • 14
    • 22544452689 scopus 로고    scopus 로고
    • Characterization of a multigene-encoded sodium/hydrogen antiporter (Sha) from Pseudomonas aeruginosa: Its involvement in pathogenesis
    • Kosono S, Haga K, Tomizawa R, Kajiyama Y, Hatano K, Takeda S, Wakai Y, Hino M, Kudo T (2005) Characterization of a multigene-encoded sodium/hydrogen antiporter (Sha) from Pseudomonas aeruginosa: its involvement in pathogenesis. J Bacteriol 187:5242-5248.
    • (2005) J Bacteriol , vol.187 , pp. 5242-5248
    • Kosono, S.1    Haga, K.2    Tomizawa, R.3    Kajiyama, Y.4    Hatano, K.5    Takeda, S.6    Wakai, Y.7    Hino, M.8    Kudo, T.9
  • 15
    • 33745245705 scopus 로고    scopus 로고
    • Functional involvement of membrane-embedded and conserved acidic residues in the ShaA subunit of the multigene-encoded Na+/H+ antiporter in Bacillus subtilis
    • Kosono S, Kajiyama Y, Kawasaki S, Yoshinaka T, Haga K, Kudo T (2006) Functional involvement of membrane-embedded and conserved acidic residues in the ShaA subunit of the multigene-encoded Na+/H+ antiporter in Bacillus subtilis. Biochim Biophys Acta 1758: 627-635.
    • (2006) Biochim Biophys Acta , vol.1758 , pp. 627-635
    • Kosono, S.1    Kajiyama, Y.2    Kawasaki, S.3    Yoshinaka, T.4    Haga, K.5    Kudo, T.6
  • 16
    • 34247874630 scopus 로고    scopus 로고
    • Catalytic properties of Staphylococcus aureus and Bacillus members of the secondary cation/proton antiporter-3 (Mrp) family are revealed by an optimized assay in an Escherichia coli host
    • DOI 10.1128/JB.00021-07
    • Swartz TH, Ito M, Ohira T, Natsui S, Hicks DB, Krulwich TA (2007) Catalytic properties of Staphylococcus aureus and Bacillus members of the secondary cation/proton antiporter-3 (Mrp) family are revealed by an optimized assay in an Escherichia coli host. J Bacteriol 189:3081-3090. (Pubitemid 46697397)
    • (2007) Journal of Bacteriology , vol.189 , Issue.8 , pp. 3081-3090
    • Swartz, T.H.1    Ito, M.2    Ohira, T.3    Natsui, S.4    Hicks, D.B.5    Krulwich, T.A.6
  • 17
    • 44949253200 scopus 로고    scopus 로고
    • + antiporter of alkaliphilic Bacillus and formation of hetero-oligomeric Mrp complexes
    • DOI 10.1128/JB.00294-08
    • Morino M, Natsui S, Swartz TH, Krulwich TA, Ito M (2008) Single gene deletions of mrpA to mrpG and mrpE point mutations affect activity of the Mrp Na+/H+ antiporter of alkaliphilic Bacillus and formation of hetero-monieric Mrp complexes. J Bacteriol 190:4162-4172. (Pubitemid 351812862)
    • (2008) Journal of Bacteriology , vol.190 , Issue.12 , pp. 4162-4172
    • Morino, M.1    Natsui, S.2    Swartz, T.H.3    Krulwich, T.A.4    Ito, M.5
  • 18
    • 69949138140 scopus 로고    scopus 로고
    • pH-dependent regulation of the multi-subunit cation/proton antiporter Pha1 system from Sinorhizobium meliloti
    • Yamaguchi T, Tsutsumi F, Putnoky P, Fukuhara M, Nakamura T (2009) pH-dependent regulation of the multi-subunit cation/proton antiporter Pha1 system from Sinorhizobium meliloti. Microbiology 155:2750-2756.
    • (2009) Microbiology , vol.155 , pp. 2750-2756
    • Yamaguchi, T.1    Tsutsumi, F.2    Putnoky, P.3    Fukuhara, M.4    Nakamura, T.5
  • 19
    • 69949185951 scopus 로고    scopus 로고
    • The MrpA, MrpB and MrpD subunits of the Mrp antiporter complex in Bacillus subtilis contain membrane-embedded and essential acidic residues
    • Kajiyama Y, Otagiri M, Sekiguchi J, Kudo T, Kosono S (2009) The MrpA, MrpB and MrpD subunits of the Mrp antiporter complex in Bacillus subtilis contain membrane-embedded and essential acidic residues. Microbiology 155:2137-2147.
    • (2009) Microbiology , vol.155 , pp. 2137-2147
    • Kajiyama, Y.1    Otagiri, M.2    Sekiguchi, J.3    Kudo, T.4    Kosono, S.5
  • 21
    • 35348845412 scopus 로고    scopus 로고
    • +by an antiporter-related subunit from the Escherichia coli NADH dehydrogenase I produced in Saccharomyces cerevisiae
    • + by an antiporter-related subunit from the Escherichia coli NADH dehydrogenase I produced in Saccharomyces cerevisiae. Arch Microbiol 188:509-521.
    • (2007) Arch Microbiol , vol.188 , pp. 509-521
    • Gemperli, A.C.1    Schaffitzel, C.2    Jakob, C.3    Steuber, J.4
  • 22
    • 0037995650 scopus 로고    scopus 로고
    • Mutagenesis of subunit N of the Escherichia coli complex I. Identification of the initiation codon and the sensitivity of mutants to decylubiquinone
    • Amarneh B, Vik SB (2003) Mutagenesis of subunit N of the Escherichia coli complex I. Identification of the initiation codon and the sensitivity of mutants to decylubiquinone. Biochemistry 42:4800-4808.
    • (2003) Biochemistry , vol.42 , pp. 4800-4808
    • Amarneh, B.1    Vik, S.B.2
  • 23
    • 49349107465 scopus 로고    scopus 로고
    • Conserved lysine residues of the membrane subunit NuoM are involved in energy conversion by the proton-pumping NADH: Ubiquinone oxidoreductase (Complex I)
    • Euro L, Belevich G, Verkhovsky MI, Wikström M, Verkhovskaya M (2008) Conserved lysine residues of the membrane subunit NuoM are involved in energy conversion by the proton-pumping NADH: ubiquinone oxidoreductase (Complex I). Biochim Biophys Acta 1777: 1166-1172.
    • (2008) Biochim Biophys Acta , vol.1777 , pp. 1166-1172
    • Euro, L.1    Belevich, G.2    Verkhovsky, M.I.3    Wikström, M.4    Verkhovskaya, M.5
  • 24
    • 37549049790 scopus 로고    scopus 로고
    • Characterization of the NuoM (ND4) subunit in Escherichia coli NDH-1 - Conserved charged residues essential for energy-coupled activities
    • Torres-Bacete J, Nakamaru-Ogiso E, Matsuno-Yagi A, Yagi T (2007) Characterization of the NuoM (ND4) subunit in Escherichia coli NDH-1 - conserved charged residues essential for energy-coupled activities. J Biol Chem 282:36914-36922.
    • (2007) J Biol Chem , vol.282 , pp. 36914-36922
    • Torres-Bacete, J.1    Nakamaru-Ogiso, E.2    Matsuno-Yagi, A.3    Yagi, T.4
  • 25
    • 70549113296 scopus 로고    scopus 로고
    • Features of subunit NuoM (ND4) in Escherichia coli NDH-1 topology and implications of conserved glu(144) for coupling site 1
    • Torres-Bacete J, Sinha PK, Castro-Guerrero N, Matsuno-Yagi A, Yagi T (2009) Features of subunit NuoM (ND4) in Escherichia coli NDH-1 topology and implications of conserved glu(144) for coupling site 1. J Biol Chem 284:33062-33069.
    • (2009) J Biol Chem , vol.284 , pp. 33062-33069
    • Torres-Bacete, J.1    Sinha, P.K.2    Castro-Guerrero, N.3    Matsuno-Yagi, A.4    Yagi, T.5
  • 26
    • 0024997335 scopus 로고
    • Bacillus subtilis 13-kilodalton cytochrome c-550 encoded by cccA consists of a membrane-anchor and a heme domain
    • von Wachenfeldt C, Hederstedt L (1990) Bacillus subtilis 13-kilodalton cytochrome c-550 encoded by cccA consists of a membrane-anchor and a heme domain. J Biol Chem 265:13939-13948.
    • (1990) J Biol Chem , vol.265 , pp. 13939-13948
    • Von Wachenfeldt, C.1    Hederstedt, L.2
  • 27
    • 0027403011 scopus 로고
    • Physico-chemical characterisation of membrane-bound and water-soluble forms of Bacillus subtilis cytochrome c-550
    • von Wachenfeldt C, Hederstedt L (1993) Physico-chemical characterisation of membrane-bound and water-soluble forms of Bacillus subtilis cytochrome c-550. Eur J Biochem 212:499-509.
    • (1993) Eur J Biochem , vol.212 , pp. 499-509
    • Von Wachenfeldt, C.1    Hederstedt, L.2
  • 28
    • 0025002908 scopus 로고
    • Bacillus subtilis holo-cytochrome c-550 can be synthesised in aerobic Escherichia coli
    • von Wachenfeldt C, Hederstedt L (1990) Bacillus subtilis holo-cytochrome c-550 can be synthesised in aerobic Escherichia coli. FEBS Lett 270:147-151.
    • (1990) FEBS Lett , vol.270 , pp. 147-151
    • Von Wachenfeldt, C.1    Hederstedt, L.2
  • 29
    • 0023652658 scopus 로고
    • Photolabelling of a mitochondrially encoded subunit of NADH dehydrogenase with [3-H]-dehydrorotenone
    • Earley FG, Patel SD, Ragan CI, Attardi G (1987) Photolabelling of a mitochondrially encoded subunit of NADH dehydrogenase with [3-H]- dehydrorotenone. FEBS Lett 219:108-113.
    • (1987) FEBS Lett , vol.219 , pp. 108-113
    • Earley, F.G.1    Patel, S.D.2    Ragan, C.I.3    Attardi, G.4
  • 30
    • 0032833421 scopus 로고    scopus 로고
    • Mitochondrial DNA variation in human evolution and disease
    • DOI 10.1016/S0378-1119(99)00295-4, PII S0378111999002954
    • Wallace DC, Brown MD, Lott MT (1999) Mitochondrial DNA variation in human evolution and disease. Gene 238:211-230. (Pubitemid 29436110)
    • (1999) Gene , vol.238 , Issue.1 , pp. 211-230
    • Wallace, D.C.1    Brown, M.D.2    Lott, M.T.3
  • 31
    • 0034619491 scopus 로고    scopus 로고
    • Mutagenesis of three conserved Glu residues in a bacterial homologue of the ND1 subunit of complex I affects ubiquinone reduction kinetics but not inhibition by dicyclohexylcarbodiimide
    • Kurki S, Zickermann V, Kervinen M, Hassinen I, Finel M (2000) Mutagenesis of three conserved Glu residues in a bacterial homologue of the ND1 subunit of complex I affects ubiquinone reduction kinetics but not inhibition by dicyclohexylcarbodiimide. Biochemistry 39: 13496-13502.
    • (2000) Biochemistry , vol.39 , pp. 13496-13502
    • Kurki, S.1    Zickermann, V.2    Kervinen, M.3    Hassinen, I.4    Finel, M.5
  • 32
    • 0032588194 scopus 로고    scopus 로고
    • - stoichiometry in NADH-quinone reductase reactions catalyzed by bovine heart submitochondrial particles
    • - stoichiometry in NADH-quinone reductase reactions catalyzed by bovine heart submitochondrial particles. FEBS Lett 451:157-161.
    • (1999) FEBS Lett , vol.451 , pp. 157-161
    • Galkin, A.1    Grivennikova, V.G.2    Vinogradov, A.D.3
  • 33
    • 0037072803 scopus 로고    scopus 로고
    • The respiratory complex I (NDH I) from Klebsiella pneumoniae, a sodium pump
    • Gemperli AC, Dimroth P, Steuber J (2002) The respiratory complex I (NDH I) from Klebsiella pneumoniae, a sodium pump. J Biol Chem 277:33811-33817.
    • (2002) J Biol Chem , vol.277 , pp. 33811-33817
    • Gemperli, A.C.1    Dimroth, P.2    Steuber, J.3
  • 34
    • 0033955767 scopus 로고    scopus 로고
    • + translocation by complex I (NADH:quinone oxidoreductase) of Escherichia coli
    • DOI 10.1046/j.1365-2958.2000.01712.x
    • Steuber J, Schmid C, Rufibach M, Dimroth P (2000) Na+ translocation by complex I (NADH : quinone oxidoreductase) of Escherichia coli. Mol Microbiol 35: 428-434. (Pubitemid 30055239)
    • (2000) Molecular Microbiology , vol.35 , Issue.2 , pp. 428-434
    • Steuber, J.1    Schmid, C.2    Rufibach, M.3    Dimroth, P.4
  • 35
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors and host strains: Nucleotide sequences of the M13mp18 and pUC19 vectors
    • DOI 10.1016/0378-1119(85)90120-9
    • Yanisch-Perron C, Vieira J, Messing J (1985) Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors. Gene 33:103-119. (Pubitemid 15122816)
    • (1985) Gene , vol.33 , Issue.1 , pp. 103-119
    • Yanisch-Perron, C.1    Vieira, J.2    Messing, J.3
  • 38
    • 0025972526 scopus 로고
    • Redox analysis of the cytochrome o-type quinol oxidase complex of Escherichia coli reveals 3 redox components
    • Bolgiano B, Salmon I, Ingledew WJ, Poole RK (1991) Redox analysis of the cytochrome o-type quinol oxidase complex of Escherichia coli reveals 3 redox components. Biochem J 274:723-730.
    • (1991) Biochem J , vol.274 , pp. 723-730
    • Bolgiano, B.1    Salmon, I.2    Ingledew, W.J.3    Poole, R.K.4
  • 39
    • 0024969510 scopus 로고
    • One-step purification from Escherichia coli of complex II (succinate: Ubiquinone oxidoreductase) associated with succinate-reducible cytochrome b556
    • Kita K, Vibat CR, Meinhardt S, Guest JR, Gennis RB (1989) One-step purification from Escherichia coli of complex II (succinate: ubiquinone oxidoreductase) associated with succinate-reducible cytochrome b556. J Biol Chem 264:2672-2677.
    • (1989) J Biol Chem , vol.264 , pp. 2672-2677
    • Kita, K.1    Vibat, C.R.2    Meinhardt, S.3    Guest, J.R.4    Gennis, R.B.5
  • 40
    • 0037172810 scopus 로고    scopus 로고
    • Proteomic analysis of a highly active photosystem II preparation from the cyanobacterium Synechocystis sp. PCC 6803 reveals the presence of novel polypeptides
    • DOI 10.1021/bi026012+
    • Kashino Y, Lauber WM, Carroll JA, Wang QJ, Whitmarsh J, Satoh K, Pakrasi HB (2002) Proteomic analysis of a highly active photosystem II preparation from the cyanobacterium Synechocystis sp PCC 6803 reveals the presence of novel polypeptides. Biochemistry 41: 8004-8012. (Pubitemid 34655167)
    • (2002) Biochemistry , vol.41 , Issue.25 , pp. 8004-8012
    • Kashino, Y.1    Lauber, W.M.2    Carroll, J.A.3    Wang, Q.4    Whitmarsh, J.5    Satoh, K.6    Pakrasi, H.B.7
  • 41
    • 0035844045 scopus 로고    scopus 로고
    • + antiporters of Bacillus exhibit characteristics that are unanticipated for completely secondary active transporters
    • + antiporters of Bacillus exhibit characteristics that are unanticipated for completely secondary active transporters. FEBS Lett 496:117-120.
    • (2001) FEBS Lett , vol.496 , pp. 117-120
    • Ito, M.1    Guffanti, A.A.2    Krulwich, T.A.3
  • 42
    • 0344196984 scopus 로고    scopus 로고
    • +and in pH homeostasis
    • Ito M, Guffanti AA, Oudega B, Krulwich TA (1999) Mrp, a multigene, multifunctional locus in Bacillus subtilis with roles in resistance to cholate and to Na(+) and in pH homeostasis. J Bacteriol 181:2394-2402. (Pubitemid 29181561)
    • (1999) Journal of Bacteriology , vol.181 , Issue.8 , pp. 2394-2402
    • Masahiro, I.1    Guffanti, A.A.2    Oudega, B.3    Krulwich, T.A.4
  • 45
    • 85010439719 scopus 로고
    • A procedure for the isolation of deoxyribonucleic acid from bacteria
    • Marmur J (1961) A procedure for the isolation of deoxyribonucleic acid from bacteria. J Mol Biol 3:208-218.
    • (1961) J Mol Biol , vol.3 , pp. 208-218
    • Marmur, J.1
  • 46
    • 0015787997 scopus 로고
    • Transformation in Bacillus subtilis - Fate of newly introduced transforming DNA
    • Arwert F, Venema G (1973) Transformation in Bacillus subtilis - fate of newly introduced transforming DNA. Mol Gen Genet 123:185-198.
    • (1973) Mol Gen Genet , vol.123 , pp. 185-198
    • Arwert, F.1    Venema, G.2
  • 47
    • 0015240315 scopus 로고
    • Molecular weight determination of protein-dodecyl sulfate complexes by gel electrophoresis in a discontinuous buffer system
    • Neville DM (1971) Molecular weight determination of protein-dodecyl sulfate complexes by gel electrophoresis in a discontinuous buffer system. J Biol Chem 246: 6328-6334.
    • (1971) J Biol Chem , vol.246 , pp. 6328-6334
    • Neville, D.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.