메뉴 건너뛰기




Volumn 7, Issue 5, 2012, Pages

Association of the chromosome replication initiator dnaa with the escherichia coli inner membrane in vivo: Quantity and mode of binding

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; CELL DNA; DNA FRAGMENT; DNA HYBRID; NUCLEOTIDE; REPLICATION INITIATOR PROTEIN DNAA; BACTERIAL PROTEIN; DNA BINDING PROTEIN; DNAA PROTEIN, BACTERIA; HYBRID PROTEIN; PEPTIDE FRAGMENT; PHOTOPROTEIN; RED FLUORESCENT PROTEIN;

EID: 84860506918     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0036441     Document Type: Article
Times cited : (18)

References (68)
  • 1
    • 33750312968 scopus 로고    scopus 로고
    • DnaA: controlling the initiation of bacterial DNA replication and more
    • Kaguni JM, (2006) DnaA: controlling the initiation of bacterial DNA replication and more. Annu Rev Microbiol 60: 351-375.
    • (2006) Annu Rev Microbiol , vol.60 , pp. 351-375
    • Kaguni, J.M.1
  • 2
    • 34247271405 scopus 로고    scopus 로고
    • DNA replication initiation: mechanisms and regulation in bacteria
    • Mott ML, Berger JM, (2007) DNA replication initiation: mechanisms and regulation in bacteria. Nat Rev Microbiol 5: 343-354.
    • (2007) Nat Rev Microbiol , vol.5 , pp. 343-354
    • Mott, M.L.1    Berger, J.M.2
  • 4
    • 76949086750 scopus 로고    scopus 로고
    • Regulation of the replication cycle: conserved and diverse regulatory systems for DnaA and oriC
    • Katayama T, Ozaki S, Keyamura K, Fujimitsu K, (2010) Regulation of the replication cycle: conserved and diverse regulatory systems for DnaA and oriC. Nature Reviews Microbiology 8: 163-170.
    • (2010) Nature Reviews Microbiology , vol.8 , pp. 163-170
    • Katayama, T.1    Ozaki, S.2    Keyamura, K.3    Fujimitsu, K.4
  • 6
    • 34547100313 scopus 로고    scopus 로고
    • Structure and function of DnaA N-terminal domains: specific sites and mechanisms in inter-DnaA interaction and in DnaB helicase loading on oriC
    • Abe Y, Jo T, Matsuda Y, Matsunaga C, Katayama T, et al. (2007) Structure and function of DnaA N-terminal domains: specific sites and mechanisms in inter-DnaA interaction and in DnaB helicase loading on oriC. J Biol Chem 282: 17816-17827.
    • (2007) J Biol Chem , vol.282 , pp. 17816-17827
    • Abe, Y.1    Jo, T.2    Matsuda, Y.3    Matsunaga, C.4    Katayama, T.5
  • 8
    • 0032844522 scopus 로고    scopus 로고
    • The N-terminus promotes oligomerization of the Escherichia coli initiator protein DnaA
    • Weigel C, Schmidt A, Seitz H, Tungler D, Welzeck M, et al. (1999) The N-terminus promotes oligomerization of the Escherichia coli initiator protein DnaA. Mol Microbiol 34: 53-66.
    • (1999) Mol Microbiol , vol.34 , pp. 53-66
    • Weigel, C.1    Schmidt, A.2    Seitz, H.3    Tungler, D.4    Welzeck, M.5
  • 9
    • 0042665854 scopus 로고    scopus 로고
    • DnaA Protein of Escherichia coli: oligomerization at the E. coli chromosomal origin is required for initiation and involves specific N-terminal amino acids
    • Simmons LA, Felczak M, Kaguni JM, (2003) DnaA Protein of Escherichia coli: oligomerization at the E. coli chromosomal origin is required for initiation and involves specific N-terminal amino acids. Mol Microbiol 49: 849-858.
    • (2003) Mol Microbiol , vol.49 , pp. 849-858
    • Simmons, L.A.1    Felczak, M.2    Kaguni, J.M.3
  • 10
    • 0033812649 scopus 로고    scopus 로고
    • The interaction domains of the DnaA and DnaB replication proteins of Escherichia coli
    • Seitz H, Weigel C, Messer W, (2000) The interaction domains of the DnaA and DnaB replication proteins of Escherichia coli. Mol Microbiol 37: 1270-1279.
    • (2000) Mol Microbiol , vol.37 , pp. 1270-1279
    • Seitz, H.1    Weigel, C.2    Messer, W.3
  • 11
    • 70350155327 scopus 로고    scopus 로고
    • A role for nonessential domain II of initiator protein, DnaA, in replication control
    • Molt KL, Sutera VA Jr, Moore KK, Lovett ST, (2009) A role for nonessential domain II of initiator protein, DnaA, in replication control. Genetics 183: 39-49.
    • (2009) Genetics , vol.183 , pp. 39-49
    • Molt, K.L.1    Sutera Jr., V.A.2    Moore, K.K.3    Lovett, S.T.4
  • 12
    • 65349083151 scopus 로고    scopus 로고
    • Escherichia coli DnaA forms helical structures along the longitudinal cell axis distinct from MreB filaments
    • Boeneman K, Fossum S, Yang Y, Fingland N, Skarstad K, et al. (2009) Escherichia coli DnaA forms helical structures along the longitudinal cell axis distinct from MreB filaments. Mol Microbiol 72: 645-657.
    • (2009) Mol Microbiol , vol.72 , pp. 645-657
    • Boeneman, K.1    Fossum, S.2    Yang, Y.3    Fingland, N.4    Skarstad, K.5
  • 13
    • 67749135363 scopus 로고    scopus 로고
    • Replication Initiator DnaA of Escherichia coli Changes its Assembly Form on the Replication Origin During the Cell Cycle
    • J Bacteriol
    • Nozaki S, Niki H, Ogawa T, (2009) Replication Initiator DnaA of Escherichia coli Changes its Assembly Form on the Replication Origin During the Cell Cycle. J Bacteriol.
    • (2009)
    • Nozaki, S.1    Niki, H.2    Ogawa, T.3
  • 14
    • 0037119995 scopus 로고    scopus 로고
    • The structure of bacterial DnaA: implications for general mechanisms underlying DNA replication initiation
    • Erzberger JP, Pirruccello MM, Berger JM, (2002) The structure of bacterial DnaA: implications for general mechanisms underlying DNA replication initiation. Embo J 21: 4763-4773.
    • (2002) Embo J , vol.21 , pp. 4763-4773
    • Erzberger, J.P.1    Pirruccello, M.M.2    Berger, J.M.3
  • 15
    • 33746860263 scopus 로고    scopus 로고
    • Structural basis for ATP-dependent DnaA assembly and replication-origin remodeling
    • Erzberger JP, Mott ML, Berger JM, (2006) Structural basis for ATP-dependent DnaA assembly and replication-origin remodeling. Nat Struct Mol Biol 13: 676-683.
    • (2006) Nat Struct Mol Biol , vol.13 , pp. 676-683
    • Erzberger, J.P.1    Mott, M.L.2    Berger, J.M.3
  • 16
    • 0000549939 scopus 로고    scopus 로고
    • Timing of Synthetic Activities in the Cell Cycle
    • In: Neidhardt FC, editors, 2nd ed. Washington, D.C., ASM Press
    • Helmstetter CE, (1996) Timing of Synthetic Activities in the Cell Cycle. In: Neidhardt FC, editors. Escherichia coli and Salmonella typhimurium 2nd ed. Washington, D.C. ASM Press pp. 1627-1639.
    • (1996) Escherichia Coli and Salmonella Typhimurium , pp. 1627-1639
    • Helmstetter, C.E.1
  • 17
    • 0022744245 scopus 로고
    • Timing of initiation of chromosome replication in individual Escherichia coli cells
    • Skarstad K, Boye E, Steen HB, (1986) Timing of initiation of chromosome replication in individual Escherichia coli cells. Embo J 5: 1711-1717.
    • (1986) Embo J , vol.5 , pp. 1711-1717
    • Skarstad, K.1    Boye, E.2    Steen, H.B.3
  • 18
    • 0033935409 scopus 로고    scopus 로고
    • The Escherichia coli SeqA protein binds specifically and co-operatively to two sites in hemimethylated and fully methylated oriC
    • Skarstad K, Lueder G, Lurz R, Speck C, Messer W, (2000) The Escherichia coli SeqA protein binds specifically and co-operatively to two sites in hemimethylated and fully methylated oriC. Mol Microbiol 36: 1319-1326.
    • (2000) Mol Microbiol , vol.36 , pp. 1319-1326
    • Skarstad, K.1    Lueder, G.2    Lurz, R.3    Speck, C.4    Messer, W.5
  • 19
    • 0032190630 scopus 로고    scopus 로고
    • Negative control of replication initiation by a novel chromosomal locus exhibiting exceptional affinity for Escherichia coli DnaA protein
    • Kitagawa R, Ozaki T, Moriya S, Ogawa T, (1998) Negative control of replication initiation by a novel chromosomal locus exhibiting exceptional affinity for Escherichia coli DnaA protein. Genes Dev 12: 3032-3043.
    • (1998) Genes Dev , vol.12 , pp. 3032-3043
    • Kitagawa, R.1    Ozaki, T.2    Moriya, S.3    Ogawa, T.4
  • 20
    • 66149123740 scopus 로고    scopus 로고
    • Initiating chromosome replication in E. coli: it makes sense to recycle
    • Leonard AC, Grimwade JE, (2009) Initiating chromosome replication in E. coli: it makes sense to recycle. Genes Dev 23: 1145-1150.
    • (2009) Genes Dev , vol.23 , pp. 1145-1150
    • Leonard, A.C.1    Grimwade, J.E.2
  • 21
    • 0036843139 scopus 로고    scopus 로고
    • The bacterial replication initiator DnaA. DnaA and oriC, the bacterial mode to initiate DNA replication
    • Messer W, (2002) The bacterial replication initiator DnaA. DnaA and oriC, the bacterial mode to initiate DNA replication. FEMS Microbiol Rev 26: 355-374.
    • (2002) FEMS Microbiol Rev , vol.26 , pp. 355-374
    • Messer, W.1
  • 22
    • 0033485526 scopus 로고    scopus 로고
    • Replication cycle-coordinated change of the adenine nucleotide-bound forms of DnaA protein in Escherichia coli
    • Kurokawa K, Nishida S, Emoto A, Sekimizu K, Katayama T, (1999) Replication cycle-coordinated change of the adenine nucleotide-bound forms of DnaA protein in Escherichia coli. Embo J 18: 6642-6652.
    • (1999) Embo J , vol.18 , pp. 6642-6652
    • Kurokawa, K.1    Nishida, S.2    Emoto, A.3    Sekimizu, K.4    Katayama, T.5
  • 23
    • 66149097454 scopus 로고    scopus 로고
    • Specific genomic sequences of E. coli promote replicational initiation by directly reactivating ADP-DnaA
    • Fujimitsu K, Senriuchi T, Katayama T, (2009) Specific genomic sequences of E. coli promote replicational initiation by directly reactivating ADP-DnaA. Genes Dev 23: 1221-1233.
    • (2009) Genes Dev , vol.23 , pp. 1221-1233
    • Fujimitsu, K.1    Senriuchi, T.2    Katayama, T.3
  • 24
    • 0344020676 scopus 로고
    • Membrane attachment activates dnaA protein, the initiation protein of chromosome replication in Escherichia coli
    • Yung BY, Kornberg A, (1988) Membrane attachment activates dnaA protein, the initiation protein of chromosome replication in Escherichia coli. Proc Natl Acad Sci U S A 85: 7202-7205.
    • (1988) Proc Natl Acad Sci U S A , vol.85 , pp. 7202-7205
    • Yung, B.Y.1    Kornberg, A.2
  • 25
    • 0023904203 scopus 로고
    • Cardiolipin activation of dnaA protein, the initiation protein of replication in Escherichia coli
    • Sekimizu K, Kornberg A, (1988) Cardiolipin activation of dnaA protein, the initiation protein of replication in Escherichia coli. J Biol Chem 263: 7131-7135.
    • (1988) J Biol Chem , vol.263 , pp. 7131-7135
    • Sekimizu, K.1    Kornberg, A.2
  • 26
    • 0027431099 scopus 로고
    • Fluid membranes with acidic domains activate DnaA, the initiator protein of replication in Escherichia coli
    • Castuma CE, Crooke E, Kornberg A, (1993) Fluid membranes with acidic domains activate DnaA, the initiator protein of replication in Escherichia coli. J Biol Chem 268: 24665-24668.
    • (1993) J Biol Chem , vol.268 , pp. 24665-24668
    • Castuma, C.E.1    Crooke, E.2    Kornberg, A.3
  • 27
    • 0028837935 scopus 로고
    • In vivo evidence for the involvement of anionic phospholipids in initiation of DNA replication in Escherichia coli
    • Xia W, Dowhan W, (1995) In vivo evidence for the involvement of anionic phospholipids in initiation of DNA replication in Escherichia coli. Proc Natl Acad Sci U S A 92: 783-787.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 783-787
    • Xia, W.1    Dowhan, W.2
  • 28
    • 0029880647 scopus 로고    scopus 로고
    • Membrane regulation of the chromosomal replication activity of E. coli DnaA requires a discrete site on the protein
    • Garner J, Crooke E, (1996) Membrane regulation of the chromosomal replication activity of E. coli DnaA requires a discrete site on the protein. Embo J 15: 2313-2321.
    • (1996) Embo J , vol.15 , pp. 2313-2321
    • Garner, J.1    Crooke, E.2
  • 29
    • 0032570678 scopus 로고    scopus 로고
    • Membrane-mediated release of nucleotide from an initiator of chromosomal replication, Escherichia coli DnaA, occurs with insertion of a distinct region of the protein into the lipid bilayer
    • Garner J, Durrer P, Kitchen J, Brunner J, Crooke E, (1998) Membrane-mediated release of nucleotide from an initiator of chromosomal replication, Escherichia coli DnaA, occurs with insertion of a distinct region of the protein into the lipid bilayer. J Biol Chem 273: 5167-5173.
    • (1998) J Biol Chem , vol.273 , pp. 5167-5173
    • Garner, J.1    Durrer, P.2    Kitchen, J.3    Brunner, J.4    Crooke, E.5
  • 30
    • 0033153493 scopus 로고    scopus 로고
    • Involvement of Arg-328, Arg-334 and Arg-342 of DnaA protein in the functional interaction with acidic phospholipids
    • Yamaguchi Y, Hase M, Makise M, Mima S, Yoshimi T, et al. (1999) Involvement of Arg-328, Arg-334 and Arg-342 of DnaA protein in the functional interaction with acidic phospholipids. Biochem J 340 (Pt 2): 433-438.
    • (1999) Biochem J , vol.340 Pt 2 , pp. 433-438
    • Yamaguchi, Y.1    Hase, M.2    Makise, M.3    Mima, S.4    Yoshimi, T.5
  • 31
    • 0034635464 scopus 로고    scopus 로고
    • Identification of amino acids involved in the functional interaction between DnaA protein and acidic phospholipids
    • Makise M, Mima S, Tsuchiya T, Mizushima T, (2000) Identification of amino acids involved in the functional interaction between DnaA protein and acidic phospholipids. J Biol Chem 275: 4513-4518.
    • (2000) J Biol Chem , vol.275 , pp. 4513-4518
    • Makise, M.1    Mima, S.2    Tsuchiya, T.3    Mizushima, T.4
  • 32
    • 0035831539 scopus 로고    scopus 로고
    • Molecular mechanism for functional interaction between DnaA protein and acidic phospholipids: identification of important amino acids
    • Makise M, Mima S, Tsuchiya T, Mizushima T, (2001) Molecular mechanism for functional interaction between DnaA protein and acidic phospholipids: identification of important amino acids. J Biol Chem 276: 7450-7456.
    • (2001) J Biol Chem , vol.276 , pp. 7450-7456
    • Makise, M.1    Mima, S.2    Tsuchiya, T.3    Mizushima, T.4
  • 33
    • 0036499931 scopus 로고    scopus 로고
    • Biochemical analysis of DnaA protein with mutations in both Arg328 and Lys372
    • Makise M, Mima S, Koterasawa M, Tsuchiya T, Mizushima T, (2002) Biochemical analysis of DnaA protein with mutations in both Arg328 and Lys372. Biochem J 362: 453-458.
    • (2002) Biochem J , vol.362 , pp. 453-458
    • Makise, M.1    Mima, S.2    Koterasawa, M.3    Tsuchiya, T.4    Mizushima, T.5
  • 34
    • 33744958175 scopus 로고    scopus 로고
    • Membrane-catalyzed nucleotide exchange on DnaA. Effect of surface molecular crowding
    • Aranovich A, Gdalevsky GY, Cohen-Luria R, Fishov I, Parola AH, (2006) Membrane-catalyzed nucleotide exchange on DnaA. Effect of surface molecular crowding. J Biol Chem 281: 12526-12534.
    • (2006) J Biol Chem , vol.281 , pp. 12526-12534
    • Aranovich, A.1    Gdalevsky, G.Y.2    Cohen-Luria, R.3    Fishov, I.4    Parola, A.H.5
  • 35
    • 0035282783 scopus 로고    scopus 로고
    • Mutations in DnaA protein suppress the growth arrest of acidic phospholipid-deficient Escherichia coli cells
    • Zheng W, Li Z, Skarstad K, Crooke E, (2001) Mutations in DnaA protein suppress the growth arrest of acidic phospholipid-deficient Escherichia coli cells. Embo J 20: 1164-1172.
    • (2001) Embo J , vol.20 , pp. 1164-1172
    • Zheng, W.1    Li, Z.2    Skarstad, K.3    Crooke, E.4
  • 36
    • 34548444511 scopus 로고    scopus 로고
    • The reactivation of DnaA(L366K) requires less acidic phospholipids supporting their role in the initiation of chromosome replication in Escherichia coli
    • Aranovich A, Parola AH, Fishov I, (2007) The reactivation of DnaA(L366K) requires less acidic phospholipids supporting their role in the initiation of chromosome replication in Escherichia coli. FEBS Lett 581: 4439-4442.
    • (2007) FEBS Lett , vol.581 , pp. 4439-4442
    • Aranovich, A.1    Parola, A.H.2    Fishov, I.3
  • 37
    • 15744398051 scopus 로고    scopus 로고
    • Role of membrane lipids in bacterial division-site selection
    • Mileykovskaya E, Dowhan W, (2005) Role of membrane lipids in bacterial division-site selection. Curr Opin Microbiol 8: 135-142.
    • (2005) Curr Opin Microbiol , vol.8 , pp. 135-142
    • Mileykovskaya, E.1    Dowhan, W.2
  • 39
    • 0023879189 scopus 로고
    • The dnaA protein of Escherichia coli. Abundance, improved purification, and membrane binding
    • Sekimizu K, Yung BY, Kornberg A, (1988) The dnaA protein of Escherichia coli. Abundance, improved purification, and membrane binding. J Biol Chem 263: 7136-7140.
    • (1988) J Biol Chem , vol.263 , pp. 7136-7140
    • Sekimizu, K.1    Yung, B.Y.2    Kornberg, A.3
  • 40
  • 41
    • 46349097501 scopus 로고    scopus 로고
    • Facilitation of dissociation reaction of nucleotides bound to Mycobacterium tuberculosis DnaA
    • Yamamoto K, Moomey M, Rajagopalan M, Madiraju MV, (2008) Facilitation of dissociation reaction of nucleotides bound to Mycobacterium tuberculosis DnaA. J Biochem 143: 759-764.
    • (2008) J Biochem , vol.143 , pp. 759-764
    • Yamamoto, K.1    Moomey, M.2    Rajagopalan, M.3    Madiraju, M.V.4
  • 42
    • 0034001328 scopus 로고    scopus 로고
    • DnaA, the initiator of Escherichia coli chromosomal replication, is located at the cell membrane
    • Newman G, Crooke E, (2000) DnaA, the initiator of Escherichia coli chromosomal replication, is located at the cell membrane. J Bacteriol 182: 2604-2610.
    • (2000) J Bacteriol , vol.182 , pp. 2604-2610
    • Newman, G.1    Crooke, E.2
  • 43
    • 57049113817 scopus 로고    scopus 로고
    • Cell-cycle-dependent spatial sequestration of the DnaA replication initiator protein in Bacillus subtilis
    • Soufo CD, Soufo HJ, Noirot-Gros MF, Steindorf A, Noirot P, et al. (2008) Cell-cycle-dependent spatial sequestration of the DnaA replication initiator protein in Bacillus subtilis. Dev Cell 15: 935-941.
    • (2008) Dev Cell , vol.15 , pp. 935-941
    • Soufo, C.D.1    Soufo, H.J.2    Noirot-Gros, M.F.3    Steindorf, A.4    Noirot, P.5
  • 45
    • 0024695933 scopus 로고
    • Initiation of DNA replication in Escherichia coli after overproduction of the DnaA protein
    • Skarstad K, Lobner-Olesen A, Atlung T, von Meyenburg K, Boye E, (1989) Initiation of DNA replication in Escherichia coli after overproduction of the DnaA protein. Mol Gen Genet 218: 50-56.
    • (1989) Mol Gen Genet , vol.218 , pp. 50-56
    • Skarstad, K.1    Lobner-Olesen, A.2    Atlung, T.3    von Meyenburg, K.4    Boye, E.5
  • 46
    • 0027515321 scopus 로고
    • Three distinct chromosome replication states are induced by increasing concentrations of DnaA protein in Escherichia coli
    • Atlung T, Hansen FG, (1993) Three distinct chromosome replication states are induced by increasing concentrations of DnaA protein in Escherichia coli. J Bacteriol 175: 6537-6545.
    • (1993) J Bacteriol , vol.175 , pp. 6537-6545
    • Atlung, T.1    Hansen, F.G.2
  • 47
    • 77954065271 scopus 로고    scopus 로고
    • I-TASSER: a unified platform for automated protein structure and function prediction
    • Roy A, Kucukural A, Zhang Y, (2010) I-TASSER: a unified platform for automated protein structure and function prediction. Nat Protoc 5: 725-738.
    • (2010) Nat Protoc , vol.5 , pp. 725-738
    • Roy, A.1    Kucukural, A.2    Zhang, Y.3
  • 48
    • 39449115394 scopus 로고    scopus 로고
    • I-TASSER server for protein 3D structure prediction
    • Zhang Y, (2008) I-TASSER server for protein 3D structure prediction. BMC Bioinformatics 9: 40.
    • (2008) BMC Bioinformatics , vol.9 , pp. 40
    • Zhang, Y.1
  • 49
    • 15844388042 scopus 로고    scopus 로고
    • Reduced initiation frequency from oriC restores viability of a temperature-sensitive Escherichia coli replisome mutant
    • Skovgaard O, Lobner-Olesen A, (2005) Reduced initiation frequency from oriC restores viability of a temperature-sensitive Escherichia coli replisome mutant. Microbiology 151: 963-973.
    • (2005) Microbiology , vol.151 , pp. 963-973
    • Skovgaard, O.1    Lobner-Olesen, A.2
  • 50
    • 43749087597 scopus 로고    scopus 로고
    • A common mechanism for the ATP-DnaA-dependent formation of open complexes at the replication origin
    • Ozaki S, Kawakami H, Nakamura K, Fujikawa N, Kagawa W, et al. (2008) A common mechanism for the ATP-DnaA-dependent formation of open complexes at the replication origin. J Biol Chem 283: 8351-8362.
    • (2008) J Biol Chem , vol.283 , pp. 8351-8362
    • Ozaki, S.1    Kawakami, H.2    Nakamura, K.3    Fujikawa, N.4    Kagawa, W.5
  • 51
    • 0034016324 scopus 로고    scopus 로고
    • Analysis of the DNA-binding domain of Escherichia coli DnaA protein
    • Blaesing F, Weigel C, Welzeck M, Messer W, (2000) Analysis of the DNA-binding domain of Escherichia coli DnaA protein. Mol Microbiol 36: 557-569.
    • (2000) Mol Microbiol , vol.36 , pp. 557-569
    • Blaesing, F.1    Weigel, C.2    Welzeck, M.3    Messer, W.4
  • 52
    • 14444273862 scopus 로고    scopus 로고
    • Site-directed mutational analysis for the membrane binding of DnaA protein. Identification of amino acids involved in the functional interaction between DnaA protein and acidic phospholipids
    • Hase M, Yoshimi T, Ishikawa Y, Ohba A, Guo L, et al. (1998) Site-directed mutational analysis for the membrane binding of DnaA protein. Identification of amino acids involved in the functional interaction between DnaA protein and acidic phospholipids. J Biol Chem 273: 28651-28656.
    • (1998) J Biol Chem , vol.273 , pp. 28651-28656
    • Hase, M.1    Yoshimi, T.2    Ishikawa, Y.3    Ohba, A.4    Guo, L.5
  • 53
    • 0032716841 scopus 로고    scopus 로고
    • Growth phase-dependent variation in protein composition of the Escherichia coli nucleoid
    • Ali Azam T, Iwata A, Nishimura A, Ueda S, Ishihama A, (1999) Growth phase-dependent variation in protein composition of the Escherichia coli nucleoid. J Bacteriol 181: 6361-6370.
    • (1999) J Bacteriol , vol.181 , pp. 6361-6370
    • Ali Azam, T.1    Iwata, A.2    Nishimura, A.3    Ueda, S.4    Ishihama, A.5
  • 54
    • 0026322679 scopus 로고
    • Initiator (DnaA) protein concentration as a function of growth rate in Escherichia coli and Salmonella typhimurium
    • Hansen FG, Atlung T, Braun RE, Wright A, Hughes P, et al. (1991) Initiator (DnaA) protein concentration as a function of growth rate in Escherichia coli and Salmonella typhimurium. J Bacteriol 173: 5194-5199.
    • (1991) J Bacteriol , vol.173 , pp. 5194-5199
    • Hansen, F.G.1    Atlung, T.2    Braun, R.E.3    Wright, A.4    Hughes, P.5
  • 55
    • 0031897521 scopus 로고    scopus 로고
    • High-affinity binding sites for the initiator protein DnaA on the chromosome of Escherichia coli
    • Roth A, Messer W, (1998) High-affinity binding sites for the initiator protein DnaA on the chromosome of Escherichia coli. Mol Microbiol 28: 395-401.
    • (1998) Mol Microbiol , vol.28 , pp. 395-401
    • Roth, A.1    Messer, W.2
  • 56
    • 0030003443 scopus 로고    scopus 로고
    • A novel DnaA protein-binding site at 94.7 min on the Escherichia coli chromosome
    • Kitagawa R, Mitsuki H, Okazaki T, Ogawa T, (1996) A novel DnaA protein-binding site at 94.7 min on the Escherichia coli chromosome. Mol Microbiol 19: 1137-1147.
    • (1996) Mol Microbiol , vol.19 , pp. 1137-1147
    • Kitagawa, R.1    Mitsuki, H.2    Okazaki, T.3    Ogawa, T.4
  • 57
    • 0141707074 scopus 로고    scopus 로고
    • Titration of the Escherichia coli DnaA protein to excess datA sites causes destabilization of replication forks, delayed replication initiation and delayed cell division
    • Morigen, Lobner-Olesen A, Skarstad K, (2003) Titration of the Escherichia coli DnaA protein to excess datA sites causes destabilization of replication forks, delayed replication initiation and delayed cell division. Mol Microbiol 50: 349-362.
    • (2003) Mol Microbiol , vol.50 , pp. 349-362
    • Morigen1    Lobner-Olesen, A.2    Skarstad, K.3
  • 58
    • 0033545836 scopus 로고    scopus 로고
    • Electrostatic interactions during acidic phospholipid reactivation of DnaA protein, the Escherichia coli initiator of chromosomal replication
    • Kitchen JL, Li Z, Crooke E, (1999) Electrostatic interactions during acidic phospholipid reactivation of DnaA protein, the Escherichia coli initiator of chromosomal replication. Biochemistry 38: 6213-6221.
    • (1999) Biochemistry , vol.38 , pp. 6213-6221
    • Kitchen, J.L.1    Li, Z.2    Crooke, E.3
  • 59
    • 33845350971 scopus 로고    scopus 로고
    • Amphipathic helices as mediators of the membrane interaction of amphitropic proteins, and as modulators of bilayer physical properties
    • Cornell RB, Taneva SG, (2006) Amphipathic helices as mediators of the membrane interaction of amphitropic proteins, and as modulators of bilayer physical properties. Curr Protein Pept Sci 7: 539-552.
    • (2006) Curr Protein Pept Sci , vol.7 , pp. 539-552
    • Cornell, R.B.1    Taneva, S.G.2
  • 60
    • 0032872786 scopus 로고    scopus 로고
    • Amphitropic proteins: regulation by reversible membrane interactions (review)
    • Johnson JE, Cornell RB, (1999) Amphitropic proteins: regulation by reversible membrane interactions (review). Mol Membr Biol 16: 217-235.
    • (1999) Mol Membr Biol , vol.16 , pp. 217-235
    • Johnson, J.E.1    Cornell, R.B.2
  • 61
    • 41849084510 scopus 로고    scopus 로고
    • Role of helix B residues in interfacial activation of a bacterial phosphatidylinositol-specific phospholipase C
    • Guo S, Zhang X, Seaton BA, Roberts MF, (2008) Role of helix B residues in interfacial activation of a bacterial phosphatidylinositol-specific phospholipase C. Biochemistry 47: 4201-4210.
    • (2008) Biochemistry , vol.47 , pp. 4201-4210
    • Guo, S.1    Zhang, X.2    Seaton, B.A.3    Roberts, M.F.4
  • 63
    • 0031886989 scopus 로고    scopus 로고
    • Initiation and velocity of chromosome replication in Escherichia coli B/r and K-12
    • Bipatnath M, Dennis PP, Bremer H, (1998) Initiation and velocity of chromosome replication in Escherichia coli B/r and K-12. J Bacteriol 180: 265-273.
    • (1998) J Bacteriol , vol.180 , pp. 265-273
    • Bipatnath, M.1    Dennis, P.P.2    Bremer, H.3
  • 64
    • 0024402876 scopus 로고
    • The DnaA protein determines the initiation mass of Escherichia coli K-12
    • Lobner-Olesen A, Skarstad K, Hansen FG, von Meyenburg K, Boye E, (1989) The DnaA protein determines the initiation mass of Escherichia coli K-12. Cell 57: 881-889.
    • (1989) Cell , vol.57 , pp. 881-889
    • Lobner-Olesen, A.1    Skarstad, K.2    Hansen, F.G.3    von Meyenburg, K.4    Boye, E.5
  • 65
    • 58149190056 scopus 로고    scopus 로고
    • Lipid domains in bacterial membranes and the action of antimicrobial agents
    • Epand RM, Epand RF, (2009) Lipid domains in bacterial membranes and the action of antimicrobial agents. Biochim Biophys Acta 1788: 289-294.
    • (2009) Biochim Biophys Acta , vol.1788 , pp. 289-294
    • Epand, R.M.1    Epand, R.F.2
  • 66
    • 15444379601 scopus 로고    scopus 로고
    • Restoration of growth to acidic phospholipid-deficient cells by DnaA(L366K) is independent of its capacity for nucleotide binding and exchange and requires DnaA
    • Li Z, Kitchen JL, Boeneman K, Anand P, Crooke E, (2005) Restoration of growth to acidic phospholipid-deficient cells by DnaA(L366K) is independent of its capacity for nucleotide binding and exchange and requires DnaA. J Biol Chem 280: 9796-9801.
    • (2005) J Biol Chem , vol.280 , pp. 9796-9801
    • Li, Z.1    Kitchen, J.L.2    Boeneman, K.3    Anand, P.4    Crooke, E.5
  • 67
    • 0015523228 scopus 로고
    • Mechanism of assembly of the outer membrane of Salmonella typhimurium. Isolation and characterization of cytoplasmic and outer membrane
    • Osborn MJ, Gander JE, Parisi E, Carson J, (1972) Mechanism of assembly of the outer membrane of Salmonella typhimurium. Isolation and characterization of cytoplasmic and outer membrane. J Biol Chem 247: 3962-3972.
    • (1972) J Biol Chem , vol.247 , pp. 3962-3972
    • Osborn, M.J.1    Gander, J.E.2    Parisi, E.3    Carson, J.4
  • 68
    • 0015993851 scopus 로고
    • Orientation of membrane vesicles from Escherichia coli prepared by different procedures
    • Futai M, (1974) Orientation of membrane vesicles from Escherichia coli prepared by different procedures. J Membr Biol 15: 15-28.
    • (1974) J Membr Biol , vol.15 , pp. 15-28
    • Futai, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.