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Volumn 39, Issue 10, 2011, Pages 4180-4191

Two forms of ribosomal protein L2 of Escherichia coli that inhibit DnaA in DNA replication

Author keywords

[No Author keywords available]

Indexed keywords

REPLICATION INITIATOR PROTEIN DNAA; RIBOSOME PROTEIN; RIBOSOME PROTEIN L2; UNCLASSIFIED DRUG; ADENOSINE TRIPHOSPHATE; BACTERIAL DNA; BACTERIAL PROTEIN; DNA BINDING PROTEIN; DNAA PROTEIN, BACTERIA; ESCHERICHIA COLI PROTEIN; PEPTIDE FRAGMENT; RIBOSOMAL PROTEIN L2, E COLI;

EID: 79961180476     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkq1203     Document Type: Article
Times cited : (24)

References (68)
  • 1
    • 67650717209 scopus 로고    scopus 로고
    • DnaA structure, function, and dynamics in the initiation at the chromosomal origin
    • Ozaki, S. and Katayama, T. (2009) DnaA structure, function, and dynamics in the initiation at the chromosomal origin. Plasmid, 62, 71-82.
    • (2009) Plasmid , vol.62 , pp. 71-82
    • Ozaki, S.1    Katayama, T.2
  • 2
    • 66149123740 scopus 로고    scopus 로고
    • Initiating chromosome replication in E. coli: It makes sense to recycle
    • Leonard, A.C. and Grimwade, J.E. (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
  • 3
    • 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
    • DOI 10.1046/j.1365-2958.2003.03603.x
    • Simmons, L.A., Felczak, M. and Kaguni, J.M. (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. (Pubitemid 36918701)
    • (2003) Molecular Microbiology , vol.49 , Issue.3 , pp. 849-858
    • Simmons, L.A.1    Felczak, M.2    Kaguni, J.M.3
  • 4
    • 21644437635 scopus 로고    scopus 로고
    • An essential tryptophan of Escherichia coli DnaA protein functions in oligomerization at the E. coli replication origin
    • DOI 10.1074/jbc.M503684200
    • Felczak, M.M., Simmons, L.A. and Kaguni, J.M. (2005) An essential tryptophan of Escherichia coli DnaA protein functions in oligomerization at the E. coli replication origin. J. Biol. Chem., 280, 24627-24633. (Pubitemid 40934551)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.26 , pp. 24627-24633
    • Felczak, M.M.1    Simmonst, L.A.2    Kaguni, J.M.3
  • 5
    • 0033213720 scopus 로고    scopus 로고
    • Replisome assembly at oriC, the replication origin of E. coli, reveals an explanation for initiation sites outside an origin
    • DOI 10.1016/S1097-2765(00)80205-1
    • Fang, L., Davey, M.J. and O'Donnell, M. (1999) Replisome assembly at oriC, the replication origin of E. coli, reveals an explanation for initiation sites outside an origin. Mol. Cell, 4, 541-553. (Pubitemid 29531134)
    • (1999) Molecular Cell , vol.4 , Issue.4 , pp. 541-553
    • Fang, L.1    Davey, M.J.2    O'Donnell, M.3
  • 6
    • 0035977018 scopus 로고    scopus 로고
    • Stoichiometry of DnaA and DnaB protein in initiation at the Escherichia coli chromosomal origin
    • Carr, K.M. and Kaguni, J.M. (2001) Stoichiometry of DnaA and DnaB protein in initiation at the Escherichia coli chromosomal origin. J. Biol. Chem., 276, 44919-44925.
    • (2001) J. Biol. Chem , vol.276 , pp. 44919-44925
    • Carr, K.M.1    Kaguni, J.M.2
  • 7
    • 73649145533 scopus 로고    scopus 로고
    • Primase directs the release of DnaC from DnaB
    • Makowska-Grzyska, M. and Kaguni, J.M. (2010) Primase directs the release of DnaC from DnaB. Mol. Cell, 37, 90-101.
    • (2010) Mol. Cell , vol.37 , pp. 90-101
    • Makowska-Grzyska, M.1    Kaguni, J.M.2
  • 8
    • 0026463867 scopus 로고
    • Opening of the replication origin of Escherichia coli by DnaA protein with protein HU or IHF
    • Hwang, D.S. and Kornberg, A. (1992) Opening of the replication origin of Escherichia coli by DnaA protein with protein HU or IHF. J. Biol. Chem., 267, 23083-23086.
    • (1992) J. Biol. Chem , vol.267 , pp. 23083-23086
    • Hwang, D.S.1    Kornberg, A.2
  • 9
    • 38449105269 scopus 로고    scopus 로고
    • Escherichia coli DnaA interacts with HU in initiation at the E. coli replication origin
    • DOI 10.1111/j.1365-2958.2007.06094.x
    • Chodavarapu, S., Felczak, M.M., Yaniv, J.R. and Kaguni, J.M. (2008) Escherichia coli DnaA interacts with HU in initiation at the E. coli replication origin. Mol. Microbiol., 67, 781-792. (Pubitemid 351143691)
    • (2008) Molecular Microbiology , vol.67 , Issue.4 , pp. 781-792
    • Chodavarapu, S.1    Felczak, M.M.2    Yaniv, J.R.3    Kaguni, J.M.4
  • 10
    • 69949170409 scopus 로고    scopus 로고
    • DiaA dynamics are coupled with changes in initial origin complexes leading to helicase loading
    • Keyamura, K., Abe, Y., Higashi, M., Ueda, T. and Katayama, T. (2009) DiaA dynamics are coupled with changes in initial origin complexes leading to helicase loading. J. Biol. Chem., 284, 25038-25050.
    • (2009) J. Biol. Chem , vol.284 , pp. 25038-25050
    • Keyamura, K.1    Abe, Y.2    Higashi, M.3    Ueda, T.4    Katayama, T.5
  • 11
    • 0035076833 scopus 로고    scopus 로고
    • Roles of Escherichia coli histone-like protein HU in DNA replication: HU-beta suppresses the thermosensitivity of dnaA46ts
    • DOI 10.1016/S0300-9084(01)01246-9
    • Bahloul, A., Boubrik, F. and Rouviere-Yaniv, J. (2001) Roles of Escherichia coli histone-like protein HU in DNA replication: HU-beta suppresses the thermosensitivity of dnaA46ts. Biochimie, 83, 219-229. (Pubitemid 32243567)
    • (2001) Biochimie , vol.83 , Issue.2 , pp. 219-229
    • Bahloul, A.1    Boubrik, F.2    Rouviere-Yaniv, J.3
  • 12
    • 34547941118 scopus 로고    scopus 로고
    • The interaction of DiaA and DnaA regulates the replication cycle in E. coli by directly promoting ATP-DnaA-specific initiation complexes
    • DOI 10.1101/gad.1561207
    • Keyamura, K., Fujikawa, N., Ishida, T., Ozaki, S., Su'etsugu, M., Fujimitsu, K., Kagawa, W., Yokoyama, S., Kurumizaka, H. and Katayama, T. (2007) The interaction of DiaA and DnaA regulates the replication cycle in E. coli by directly promoting ATP DnaA-specific initiation complexes. Genes Dev., 21, 2083-2099. (Pubitemid 47267293)
    • (2007) Genes and Development , vol.21 , Issue.16 , pp. 2083-2099
    • Keyamura, K.1    Fujikawa, N.2    Ishida, T.3    Ozaki, S.4    Su'etsugu, M.5    Fujimitsu, K.6    Kagawa, W.7    Yokoyama, S.8    Kurumizaka, H.9    Katayama, T.10
  • 13
    • 0035038813 scopus 로고    scopus 로고
    • The sequence requirements for a functional Escherichia coli replication origin are different for the chromosome and a minichromosome
    • DOI 10.1046/j.1365-2958.2001.02409.x
    • Weigel, C., Messer, W., Preiss, S., Welzeck, M., Morigen. and Boye, E. (2001) The sequence requirements for a functional Escherichia coli replication origin are different for the chromosome and a minichromosome. Mol. Microbiol., 40, 498-507. (Pubitemid 32391643)
    • (2001) Molecular Microbiology , vol.40 , Issue.2 , pp. 498-507
    • Weigel, C.1    Messer, W.2    Preiss, S.3    Welzeck, M.4    Morigen5
  • 14
    • 0025370024 scopus 로고
    • Bending of the origin of replication of E. coli by binding of IHF at a specific site
    • Polaczek, P. (1990) Bending of the origin of replication of E. coli by binding of IHF at a specific site. New Biol., 2, 265-271. (Pubitemid 20187148)
    • (1990) New Biologist , vol.2 , Issue.3 , pp. 265-271
    • Polaczek, P.1
  • 15
    • 0028575868 scopus 로고
    • Functions of histone-like proteins in the initiation of DNA replication at oriC of Escherichia coli
    • Roth, A., Urmoneit, B. and Messer, W. (1994) Functions of histone-like proteins in the initiation of DNA replication at oriC of Escherichia coli. Biochimie, 76, 917-923.
    • (1994) Biochimie , vol.76 , pp. 917-923
    • Roth, A.1    Urmoneit, B.2    Messer, W.3
  • 17
    • 0030811135 scopus 로고    scopus 로고
    • Protection of DNA during oxidative stress by the nonspecific DNA- binding protein Dps
    • Martinez, A. and Kolter, R. (1997) Protection of DNA during oxidative stress by the nonspecific DNA-binding protein Dps. J. Bacteriol., 179, 5188-5194. (Pubitemid 27340555)
    • (1997) Journal of Bacteriology , vol.179 , Issue.16 , pp. 5188-5194
    • Martinez, A.1    Kolter, R.2
  • 18
    • 0031959912 scopus 로고    scopus 로고
    • The crystal structure of Dps, a ferritin homolog that binds and protects DNA
    • DOI 10.1038/nsb0498-294
    • Grant, R.A., Filman, D.J., Finkel, S.E., Kolter, R. and Hogle, J.M. (1998) The crystal structure of Dps, a ferritin homolog that binds and protects DNA. Nat. Struct. Biol., 5, 294-303. (Pubitemid 28164882)
    • (1998) Nature Structural Biology , vol.5 , Issue.4 , pp. 294-303
    • Grant, R.A.1    Filman, D.J.2    Finkel, S.E.3    Kolter, R.4    Hogle, J.M.5
  • 19
    • 0033986734 scopus 로고    scopus 로고
    • The dodecameric ferritin from Listeria innocua contains a novel intersubunit iron-binding site
    • DOI 10.1038/71236
    • Ilari, A., Stefanini, S., Chiancone, E. and Tsernoglou, D. (2000) The dodecameric ferritin from Listeria innocua contains a novel intersubunit iron-binding site. Nat. Struct. Biol., 7, 38-43. (Pubitemid 30043246)
    • (2000) Nature Structural Biology , vol.7 , Issue.1 , pp. 38-43
    • Ilari, A.1    Stefanini, S.2    Chiancone, E.3    Tsernoglou, D.4
  • 20
    • 39849091042 scopus 로고    scopus 로고
    • Escherichia coli Dps interacts with DnaA protein to impede initiation: A model of adaptive mutation
    • DOI 10.1111/j.1365-2958.2008.06127.x
    • Chodavarapu, S., Gomez, R., Vicente, M. and Kaguni, J.M. (2008) Escherichia coli Dps interacts with DnaA protein to impede initiation: a model of adaptive mutation. Mol. Microbiol., 67, 1331-1346. (Pubitemid 351316958)
    • (2008) Molecular Microbiology , vol.67 , Issue.6 , pp. 1331-1346
    • Chodavarapu, S.1    Gomez, R.2    Vicente, M.3    Kaguni, J.M.4
  • 21
    • 10044234372 scopus 로고    scopus 로고
    • rRNA transcription in Escherichia coli
    • DOI 10.1146/annurev.genet.38.072902.091347
    • Paul, B.J., Ross, W., Gaal, T. and Gourse, R.L. (2004) rRNA transcription in Escherichia coli. Annu. Rev. Genet., 38, 749-770. (Pubitemid 40013744)
    • (2004) Annual Review of Genetics , vol.38 , pp. 749-770
    • Paul, B.J.1    Ross, W.2    Gaal, T.3    Gourse, R.L.4
  • 22
    • 0033559924 scopus 로고    scopus 로고
    • The three-dimensional structure of the RNA-binding domain of ribosomal protein L2; a protein at the peptidyl transferase center of the ribosome
    • Nakagawa, A., Nakashima, T., Taniguchi, M., Hosaka, H., Kimura, M. and Tanaka, I. (1999) The three-dimensional structure of the RNA-binding domain of ribosomal protein L2; a protein at the peptidyl transferase center of the ribosome. EMBO J., 18, 1459-1467. (Pubitemid 29127060)
    • (1999) EMBO Journal , vol.18 , Issue.6 , pp. 1459-1467
    • Nakagawa, A.1    Nakashima, T.2    Taniguchi, M.3    Hosaka, H.4    Kimura, M.5    Tanaka, I.6
  • 23
    • 0023732715 scopus 로고
    • Interaction of dnaA46 protein with a stimulatory protein in replication from the Escherichia coli chromosomal origin
    • Hwang, D.S. and Kaguni, J.M. (1988) Interaction of dnaA46 protein with a stimulatory protein in replication from the Escherichia coli chromosomal origin. J. Biol. Chem., 263, 10633-10640.
    • (1988) J. Biol. Chem , vol.263 , pp. 10633-10640
    • Hwang, D.S.1    Kaguni, J.M.2
  • 24
    • 0028102357 scopus 로고
    • DnaA protein directs the binding of DnaB protein in initiation of DNA replication in Escherichia coli
    • Marszalek, J. and Kaguni, J.M. (1994) DnaA protein directs the binding of DnaB protein in initiation of DNA replication in Escherichia coli. J. Biol. Chem., 269, 4883-4890. (Pubitemid 24239465)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.7 , pp. 4883-4890
    • Marszalek, J.1    Kaguni, J.M.2
  • 25
    • 27944445504 scopus 로고    scopus 로고
    • Escherichia coli DnaA protein: Specific biochemical defects of mutant DnaAs reduce initiation frequency to suppress a temperature-sensitive dnaX mutation
    • DOI 10.1016/j.biochi.2005.08.009, PII S0300908405002026
    • Walker, J.R., Severson, K.A., Hermandson, M.J., Blinkova, A., Carr, K.M. and Kaguni, J.M. (2006) Escherichia coli DnaA protein: specific biochemical defects of mutant DnaAs reduce initiation frequency to suppress a temperature-sensitive dnaX mutation. Biochimie, 88, 1-10. (Pubitemid 41668613)
    • (2006) Biochimie , vol.88 , Issue.1 , pp. 1-10
    • Walker, J.R.1    Severson, K.A.2    Hermandson, M.J.3    Blinkova, A.4    Carr, K.M.5    Kaguni, J.M.6
  • 26
    • 10944257577 scopus 로고    scopus 로고
    • The box VII motif of Escherichia coli DnaA protein is required for DnaA oligomerization at the E. coli replication origin
    • DOI 10.1074/jbc.M409695200
    • Felczak, M.M. and Kaguni, J.M. (2004) The box VII motif of Escherichia coli DnaA protein is required for DnaA oligomerization at the E. coli replication origin. J. Biol. Chem., 279, 51156-51162. (Pubitemid 40017858)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.49 , pp. 51156-51162
    • Felczak, M.M.1    Kaguni, J.M.2
  • 27
    • 0030823757 scopus 로고    scopus 로고
    • Threonine 435 of Escherichia coli DnaA protein confers sequence-specific DNA binding activity
    • DOI 10.1074/jbc.272.37.23017
    • Sutton, M.D. and Kaguni, J.M. (1997) Threonine 435 of Escherichia coli DnaA protein confers sequence-specific DNA binding activity. J. Biol. Chem., 272, 23017-23024. (Pubitemid 27392425)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.37 , pp. 23017-23024
    • Sutton, M.D.1    Kagnni, J.M.2
  • 28
    • 0027165161 scopus 로고
    • Carbohydrate-binding protein 35. I. Properties of the recombinant polypeptide and the individuality of the domains
    • Agrwal, N., Sun, Q., Wang, S.Y. and Wang, J.L. (1993) Carbohydrate-binding protein 35. I. Properties of the recombinant polypeptide and the individuality of the domains. J. Biol. Chem., 268, 14932-14939. (Pubitemid 23206641)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.20 , pp. 14932-14939
    • Agrwal, N.1    Sun, Q.2    Wang, S.-Y.3    Wang, J.L.4
  • 29
    • 0029785959 scopus 로고    scopus 로고
    • Domains of DnaA protein involved in interaction with DnaB protein, and in unwinding the Escherichia coli chromosomal origin
    • DOI 10.1074/jbc.271.31.18535
    • Marszalek, J., Zhang, W., Hupp, T.R., Margulies, C., Carr, K.M., Cherry, S. and Kaguni, J.M. (1996) Domains of DnaA protein involved in interaction with DnaB protein, and in unwinding the Escherichia coli chromosomal origin. J. Biol. Chem., 271, 18535-18542. (Pubitemid 26322713)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.31 , pp. 18535-18542
    • Marszalek, J.1    Zhang, W.2    Hupp, T.R.3    Margulies, C.4    Carr, K.M.5    Cherry, S.6    Kaguni, J.M.7
  • 30
    • 0021751199 scopus 로고
    • Replication initiated at the origin (oriC) of the E. coli chromosome reconstituted with purified enzymes
    • Kaguni, J.M. and Kornberg, A. (1984) Replication initiated at the origin (oriC) of the E. coli chromosome reconstituted with purified enzymes. Cell, 38, 183-190. (Pubitemid 15216546)
    • (1984) Cell , vol.38 , Issue.1 , pp. 183-190
    • Kaguni, J.M.1    Kornberg, A.2
  • 31
    • 0028998688 scopus 로고
    • DnaA-dependent assembly of the ABC primosome at the A site a single-stranded DNA hairpin containing a dnaA box
    • Masai, H. and Arai, K.I. (1995) DnaA-dependent assembly of the ABC primosome at the A site, a single-stranded DNA hairpin containing a dnaA box. Eur. J. Biochem., 230, 384-395.
    • (1995) Eur. J. Biochem , vol.230 , pp. 384-395
    • Masai, H.1    Arai, K.I.2
  • 33
    • 0026726799 scopus 로고
    • Defective replication activity of a dominant-lethal dnaB gene product from Escherichia coli
    • Marszalek, J. and Kaguni, J.M. (1992) Defective replication activity of a dominant-lethal dnaB gene product from Escherichia coli. J. Biol. Chem., 267, 19334-19340.
    • (1992) J. Biol. Chem , vol.267 , pp. 19334-19340
    • Marszalek, J.1    Kaguni, J.M.2
  • 34
    • 0024284091 scopus 로고
    • Duplex opening by dnaA protein at novel sequences in initiation of replication at the origin of the E. coli chromosome
    • Bramhill, D. and Kornberg, A. (1988) Duplex opening by dnaA protein at novel sequences in initiation of replication at the origin of the E. coli chromosome. Cell, 52, 743-755.
    • (1988) Cell , vol.52 , pp. 743-755
    • Bramhill, D.1    Kornberg, A.2
  • 35
    • 0032545466 scopus 로고    scopus 로고
    • E. coli DnaA protein: The N-terminal domain and loading of DnaB helicase at the E. coli chromosomal origin
    • Sutton, M.D., Carr, K.M., Vicente, M. and Kaguni, J.M. (1998) E. coli DnaA protein: the N-terminal domain and loading of DnaB helicase at the E. coli chromosomal origin. J. Biol. Chem., 273, 34255-34262.
    • (1998) J. Biol. Chem , vol.273 , pp. 34255-34262
    • Sutton, M.D.1    Carr, K.M.2    Vicente, M.3    Kaguni, J.M.4
  • 37
    • 0024280870 scopus 로고
    • Transcriptional activation of initiation of replication from the E. coli chromosomal origin: An RNA-DNA hybrid near oriC
    • Baker, T.A. and Kornberg, A. (1988) Transcriptional activation of initiation of replication from the E. coli chromosomal origin: an RNA-DNA hybrid near oriC. Cell, 55, 113-123.
    • (1988) Cell , vol.55 , pp. 113-123
    • Baker, T.A.1    Kornberg, A.2
  • 38
    • 0037131160 scopus 로고    scopus 로고
    • Escherichia coli DnaA protein loads a single DnaB helicase at a DnaA box hairpin
    • DOI 10.1074/jbc.M205031200
    • Carr, K.M. and Kaguni, J.M. (2002) Escherichia coli DnaA protein loads a single DnaB helicase at a DnaA box hairpin. J. Biol. Chem., 277, 39815-39822. (Pubitemid 35190966)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.42 , pp. 39815-39822
    • Carr, K.M.1    Kaguni, J.M.2
  • 39
    • 0018405881 scopus 로고
    • E. coli DNA binding protein HU forms nucleosome like structure with circular double stranded DNA
    • Rouviere-Yaniv, J., Yaniv, M. and Germond, J.E. (1979) E. coli DNA binding protein HU forms nucleosomelike structure with circular double-stranded DNA. Cell, 17, 265-274. (Pubitemid 9230307)
    • (1979) Cell , vol.17 , Issue.2 , pp. 265-274
    • Rouviere-Yaniv, J.1    Yaniv, M.2    Germond, J.E.3
  • 40
    • 0025314725 scopus 로고
    • Strand separation required for initiation of replication at the chromosomal origin of E. coli is facilitated by a distant RNA-DNA hybrid
    • Skarstad, K., Baker, T.A. and Kornberg, A. (1990) Strand separation required for initiation of replication at the chromosomal origin of E. coli is facilitated by a distant RNA-DNA hybrid. EMBO J., 9, 2341-2348.
    • (1990) EMBO J , vol.9 , pp. 2341-2348
    • Skarstad, K.1    Baker, T.A.2    Kornberg, A.3
  • 41
    • 0032533770 scopus 로고    scopus 로고
    • The FIS protein fails to block the binding of DnaA protein to oriC, the Escherichia coli chromosomal origin
    • Margulies, C. and Kaguni, J.M. (1998) The FIS protein fails to block the binding of DnaA protein to oriC, the Escherichia coli chromosomal origin. Nucleic Acids Res., 26, 5170-5175. (Pubitemid 28517575)
    • (1998) Nucleic Acids Research , vol.26 , Issue.22 , pp. 5170-5175
    • Margulies, C.1    Kaguni, J.M.2
  • 42
    • 0023046634 scopus 로고
    • Extensive unwinding of the plasmid template during staged enzymatic initiation of DNA replication from the origin of the Escherichia coli chromosome
    • Baker, T.A., Sekimizu, K., Funnell, B.E. and Kornberg, A. (1986) Extensive unwinding of the plasmid template during staged enzymatic initiation of DNA replication from the origin of the Escherichia coli chromosome. Cell, 45, 53-64.
    • (1986) Cell , vol.45 , pp. 53-64
    • Baker, T.A.1    Sekimizu, K.2    Funnell, B.E.3    Kornberg, A.4
  • 43
    • 35948965576 scopus 로고    scopus 로고
    • Determination of the primary target of a quinolone drug and the effect of quinolone resistance-conferring mutations by measuring quinolone sensitivity based on its mode of action
    • DOI 10.1128/AAC.00362-07
    • Pfeiffer, E.S. and Hiasa, H. (2007) Determination of the primary target of a quinolone drug and the effect of quinolone resistance-conferring mutations by measuring quinolone sensitivity based on its mode of action. Antimicrob. Agents Chemother., 51, 3410-3412. (Pubitemid 350067567)
    • (2007) Antimicrobial Agents and Chemotherapy , vol.51 , Issue.9 , pp. 3410-3412
    • Pfeiffer, E.S.1    Hiasa, H.2
  • 44
    • 0023658349 scopus 로고
    • ATP activates dnaA protein in initiating replication of plasmids bearing the origin of the E. coli chromosome
    • Sekimizu, K., Bramhill, D. and Kornberg, A. (1987) ATP activates dnaA protein in initiating replication of plasmids bearing the origin of the E. coli chromosome. Cell, 50, 259-265.
    • (1987) Cell , vol.50 , pp. 259-265
    • Sekimizu, K.1    Bramhill, D.2    Kornberg, A.3
  • 45
    • 0030035666 scopus 로고    scopus 로고
    • Ordered and sequential binding of DnaA protein to oriC, the chromosomal origin of Escherichia coli
    • DOI 10.1074/jbc.271.29.17035
    • Margulies, C. and Kaguni, J.M. (1996) Ordered and sequential binding of DnaA protein to oriC, the chromosomal origin of Escherichia coli. J. Biol. Chem., 271, 17035-17040. (Pubitemid 26244249)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.29 , pp. 17035-17040
    • Margulies, C.1    Kaguni, J.M.2
  • 46
    • 77949691819 scopus 로고    scopus 로고
    • The ribosomal protein L2 interacts with the RNA polymerase alpha subunit and acts as a transcription modulator in Escherichia coli
    • Rippa, V., Cirulli, C., Di Palo, B., Doti, N., Amoresano, A. and Duilio, A. (2010) The ribosomal protein L2 interacts with the RNA polymerase alpha subunit and acts as a transcription modulator in Escherichia coli. J. Bacteriol., 192, 1882-1889.
    • (2010) J. Bacteriol. , vol.192 , pp. 1882-1889
    • Rippa, V.1    Cirulli, C.2    Di Palo, B.3    Doti, N.4    Amoresano, A.5    Duilio, A.6
  • 48
    • 1542343886 scopus 로고    scopus 로고
    • Understanding the biochemical activities of galectin-1 and galectin-3 in the nucleus
    • DOI 10.1023/B:GLYC.0000014079.87862.c7
    • Patterson, R.J., Wang, W. and Wang, J.L. (2004) Understanding the biochemical activities of galectin-1 and galectin-3 in the nucleus. Glycoconj. J., 19, 499-506. (Pubitemid 38316523)
    • (2002) Glycoconjugate Journal , vol.19 , Issue.7-9 , pp. 499-506
    • Patterson, R.J.1    Wang, W.2    Wang, J.L.3
  • 49
    • 0028804889 scopus 로고
    • Control of rRNA transcription in Escherichia coli
    • Condon, C., Squires, C. and Squires, C.L. (1995) Control of rRNA transcription in Escherichia coli. Microbiol. Rev., 59, 623-645.
    • (1995) Microbiol. Rev , vol.59 , pp. 623-645
    • Condon, C.1    Squires, C.2    Squires, C.L.3
  • 50
    • 0035898536 scopus 로고    scopus 로고
    • Ribosomal protein S4 is a transcription factor with properties remarkably similar to NusA, a protein involved in both non-ribosomal and ribosomal RNA antitermination
    • DOI 10.1093/emboj/20.14.3811
    • Torres, M., Condon, C., Balada, J.M., Squires, C. and Squires, C.L. (2001) Ribosomal protein S4 is a transcription factor with properties remarkably similar to NusA, a protein involved in both non-ribosomal and ribosomal RNA antitermination. EMBO J., 20, 3811-3820. (Pubitemid 32691792)
    • (2001) EMBO Journal , vol.20 , Issue.14 , pp. 3811-3820
    • Torres, M.1    Condon, C.2    Balada, J.-M.3    Squires, C.4    Squires, C.L.5
  • 51
    • 0018370008 scopus 로고
    • RNA replication: Function and structure of Qbeta-replicase
    • Blumenthal, T. and Carmichael, G.G. (1979) RNA replication: function and structure of Qbeta-replicase. Annu. Rev. Biochem., 48, 525-548.
    • (1979) Annu. Rev. Biochem , vol.48 , pp. 525-548
    • Blumenthal, T.1    Carmichael, G.G.2
  • 52
    • 0025880360 scopus 로고
    • The DNA unwinding reaction catalyzed by Rep protein is facilitated by an RHSP - DNA interaction
    • Yancey, J.E. and Matson, S.W. (1991) The DNA unwinding reaction catalyzed by Rep protein is facilitated by an RHSP-DNA interaction. Nucleic Acids Res., 19, 3943-3951. (Pubitemid 21912765)
    • (1991) Nucleic Acids Research , vol.19 , Issue.14 , pp. 3943-3951
    • Yancey, J.E.1    Matson, S.W.2
  • 54
    • 0024553093 scopus 로고
    • The histone-like H protein of Escherichia coli is ribosomal protein S3
    • Bruckner, R.C. and Cox, M.M. (1989) The histone-like H protein of Escherichia coli is ribosomal protein S3. Nucleic Acids Res., 17, 3145-3161. (Pubitemid 19122230)
    • (1989) Nucleic Acids Research , vol.17 , Issue.8 , pp. 3145-3161
    • Bruckner, R.C.1    Cox, M.M.2
  • 55
    • 0016811847 scopus 로고
    • Pools of ribosomal proteins in Escherichia coli. Studies on the exchange of proteins between pools and ribosomes
    • Ulbrich, B. and Nierhaus, K.H. (1975) Pools of ribosomal proteins in Escherichia coli. Studies on the exchange of proteins between pools and ribosomes. Eur. J. Biochem., 57, 49-54.
    • (1975) Eur. J. Biochem , vol.57 , pp. 49-54
    • Ulbrich, B.1    Nierhaus, K.H.2
  • 56
    • 36549087125 scopus 로고    scopus 로고
    • Translation factor IF2 at the interface of transposition and replication by the PriA-PriC pathway
    • DOI 10.1111/j.1365-2958.2007.06022.x
    • North, S.H., Kirtland, S.E. and Nakai, H. (2007) Translation factor IF2 at the interface of transposition and replication by the PriA-PriC pathway. Mol. Microbiol., 66, 1566-1578. (Pubitemid 350179687)
    • (2007) Molecular Microbiology , vol.66 , Issue.6 , pp. 1566-1578
    • North, S.H.1    Kirtland, S.E.2    Nakai, H.3
  • 59
    • 0036491423 scopus 로고    scopus 로고
    • Requirement for C-terminal extension to the RNA binding domain for efficient RNA binding by ribosomal protein L2
    • Hayashi, T., Tahara, M., Iwasaki, K., Kouzuma, Y. and Kimura, M. (2002) Requirement for C-terminal extension to the RNA binding domain for efficient RNA binding by ribosomal protein L2. Biosci. Biotechnol. Biochem., 66, 682-684. (Pubitemid 39251034)
    • (2002) Bioscience, Biotechnology and Biochemistry , vol.66 , Issue.3 , pp. 682-684
    • Hayashi, T.1    Tahara, M.2    Iwasaki, K.3    Kouzuma, Y.4    Kimura, M.5
  • 61
    • 42149158392 scopus 로고    scopus 로고
    • Control of bacterial transcription translation and replication by (p)ppGpp
    • Srivatsan, A. and Wang, J.D. (2008) Control of bacterial transcription, translation and replication by (p)ppGpp. Curr. Opin. Microbiol., 11, 100-105.
    • (2008) Curr. Opin. Microbiol , vol.11 , pp. 100-105
    • Srivatsan, A.1    Wang, J.D.2
  • 62
    • 0025894778 scopus 로고
    • The stringent response blocks DNA replication outside the ori region in Bacillus subtilis and at the origin in Escherichia coli
    • Levine, A., Vannier, F., Dehbi, M., Henckes, G. and Seror, S.J. (1991) The stringent response blocks DNA replication outside the ori region in Bacillus subtilis and at the origin in Escherichia coli. J. Mol. Biol., 219, 605-613. (Pubitemid 121003535)
    • (1991) Journal of Molecular Biology , vol.219 , Issue.4 , pp. 605-613
    • Levine, A.1    Vannier, F.2    Dehbi, M.3    Henckes, G.4    Seror, S.J.5
  • 63
    • 0028960079 scopus 로고
    • Ppgpp-mediated regulation of DNA replication and cell division in Escherichia coli
    • Schreiber, G., Ron, E.Z. and Glaser, G. (1995) ppGpp-mediated regulation of DNA replication and cell division in Escherichia coli. Curr. Microbiol., 30, 27-32.
    • (1995) Curr. Microbiol , vol.30 , pp. 27-32
    • Schreiber, G.1    Ron, E.Z.2    Glaser, G.3
  • 64
    • 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
    • DOI 10.1074/jbc.M701841200
    • Abe, Y., Jo, T., Matsuda, Y., Matsunaga, C., Katayama, T. and Ueda, T. (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. (Pubitemid 47100271)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.24 , pp. 17816-17827
    • Abe, Y.1    Jo, T.2    Matsuda, Y.3    Matsunaga, C.4    Katayama, T.5    Ueda, T.6
  • 65
    • 8544240894 scopus 로고    scopus 로고
    • DiaA, a novel DnaA-binding protein, ensures the timely initiation of Escherichia coli chromosome replication
    • DOI 10.1074/jbc.M402762200
    • Ishida, T., Akimitsu, N., Kashioka, T., Hatano, M., Kubota, T., Ogata, Y., Sekimizu, K. and Katayama, T. (2004) DiaA, a novel DnaA-binding protein, ensures the timely initiation of Escherichia coli chromosome replication. J. Biol. Chem., 279, 45546-45555. (Pubitemid 39491541)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.44 , pp. 45546-45555
    • Ishida, T.1    Akimitsu, N.2    Kashioka, T.3    Hatano, M.4    Kubota, T.5    Ogata, Y.6    Sekimizu, K.7    Katayama, T.8
  • 66
    • 23044509515 scopus 로고    scopus 로고
    • Conservation of eubacterial replicases
    • DOI 10.1080/15216540500138246
    • Wijffels, G., Dalrymple, B., Kongsuwan, K. and Dixon, N.E. (2005) Conservation of eubacterial replicases. IUBMB Life, 57, 413-419. (Pubitemid 41073123)
    • (2005) IUBMB Life , vol.57 , Issue.6 , pp. 413-419
    • Wijffels, G.1    Dalrymple, B.2    Kongsuwan, K.3    Dixon, N.E.4
  • 67
    • 0348134870 scopus 로고    scopus 로고
    • Competitive processivity-clamp usage by DNA polymerases during DNA replication and repair
    • DOI 10.1093/emboj/cdg603
    • Lopez de Saro, F.J., Georgescu, R.E., Goodman, M.F. and O'Donnell, M. (2003) Competitive processivity-clamp usage by DNA polymerases during DNA replication and repair. EMBO J., 22, 6408-6418. (Pubitemid 37522597)
    • (2003) EMBO Journal , vol.22 , Issue.23 , pp. 6408-6418
    • Lopez De Saro, F.J.1    Georgescu, R.E.2    Goodman, M.F.3    O'Donnell, M.4
  • 68
    • 0031897878 scopus 로고    scopus 로고
    • Characterization of dnaC2 and dnaC28 mutants by flow cytometry
    • Withers, H.L. and Bernander, R. (1998) Characterization of dnaC2 and dnaC28 mutants by flow cytometry. J. Bacteriol., 180, 1624-1631. (Pubitemid 28173038)
    • (1998) Journal of Bacteriology , vol.180 , Issue.7 , pp. 1624-1631
    • Withers, H.L.1    Bernander, R.2


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