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Volumn 193, Issue 21, 2011, Pages 5985-5996

Role of ArgP (IciA) in lysine-mediated repression in Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL DNA; BETA GALACTOSIDASE; ESCHERICHIA COLI PROTEIN; LYSINE; NUCLEOTIDE BINDING PROTEIN; PROTEIN ARGO; PROTEIN ARGP; PROTEIN ASD; PROTEIN CADA; PROTEIN CADB; PROTEIN DAPB; PROTEIN DAPD; PROTEIN GDHA; PROTEIN ICIA; PROTEIN LYSA; PROTEIN LYSC; PROTEIN LYSP; PROTEIN NRDA; REPLICATION INITIATOR PROTEIN DNAA; SODIUM CHLORIDE; UNCLASSIFIED DRUG;

EID: 80055056735     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.05869-11     Document Type: Article
Times cited : (23)

References (50)
  • 1
    • 0026326004 scopus 로고
    • Importance of the position of TYR R boxes for repression and activation of the tyrP and aroF genes in Escherichia coli
    • Andrews, A. E., B. Dickson, B. Lawley, C. Cobbett, and A. J. Pittard. 1991. Importance of the position of TYR R boxes for repression and activation of the tyrP and aroF genes in Escherichia coli. J. Bacteriol. 173:5079-5085.
    • (1991) J. Bacteriol. , vol.173 , pp. 5079-5085
    • Andrews, A.E.1    Dickson, B.2    Lawley, B.3    Cobbett, C.4    Pittard, A.J.5
  • 2
    • 0032731196 scopus 로고    scopus 로고
    • Twelve species of the nucleoid-associated protein from Escherichia coli. Sequence recognition specificity and DNA binding affinity
    • Azam, T. A., and A. Ishihama. 1999. Twelve species of the nucleoid-associated protein from Escherichia coli. Sequence recognition specificity and DNA binding affinity. J. Biol. Chem. 274:33105-33113.
    • (1999) J. Biol. Chem. , vol.274 , pp. 33105-33113
    • Azam, T.A.1    Ishihama, A.2
  • 3
    • 0032716841 scopus 로고    scopus 로고
    • Growth phase-dependent variation in protein composition of the Escherichia coli nucleoid
    • Azam, T. A., A. Iwata, A. Nishimura, S. Ueda, and A. Ishihama. 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
    • Azam, T.A.1    Iwata, A.2    Nishimura, A.3    Ueda, S.4    Ishihama, A.5
  • 4
    • 31544450286 scopus 로고    scopus 로고
    • Construction of Escherichia coli K-12 in-frame, singlegene knockout mutants: the Keio collection
    • Baba, T., et al. 2006. Construction of Escherichia coli K-12 in-frame, singlegene knockout mutants: the Keio collection. Mol. Syst. Biol. 2:1-11.
    • (2006) Mol. Syst. Biol. , vol.2 , pp. 1-11
    • Baba, T.1
  • 5
    • 0034926912 scopus 로고    scopus 로고
    • Expression control and specificity of the basic amino acid exporter LysE of Corynebacterium glutamicum
    • Bellmann, A., et al. 2001. Expression control and specificity of the basic amino acid exporter LysE of Corynebacterium glutamicum. Microbiology 147:1765-1774.
    • (2001) Microbiology , vol.147 , pp. 1765-1774
    • Bellmann, A.1
  • 6
    • 0031670734 scopus 로고    scopus 로고
    • Linkage map of Escherichia coli K-12, edition 10: the traditional map
    • Berlyn, M. K. 1998. Linkage map of Escherichia coli K-12, edition 10: the traditional map. Microbiol. Mol. Biol. Rev. 62:814-984.
    • (1998) Microbiol. Mol. Biol. Rev. , vol.62 , pp. 814-984
    • Berlyn, M.K.1
  • 7
    • 48149095073 scopus 로고    scopus 로고
    • Lysine represses transcription of the Escherichia coli dapB gene by preventing its activation by the ArgP activator
    • Bouvier, J., P. Stragier, V. Morales, E. Remy, and C. Gutierrez. 2008. Lysine represses transcription of the Escherichia coli dapB gene by preventing its activation by the ArgP activator. J. Bacteriol. 190:5224-5229.
    • (2008) J. Bacteriol. , vol.190 , pp. 5224-5229
    • Bouvier, J.1    Stragier, P.2    Morales, V.3    Remy, E.4    Gutierrez, C.5
  • 8
    • 33750938822 scopus 로고    scopus 로고
    • The arginine regulon of Escherichia coli: whole-system transcriptome analysis discovers new genes and provides an integrated view of arginine regulation
    • Caldara, M., D. Charlier, and R. Cunin. 2006. The arginine regulon of Escherichia coli: whole-system transcriptome analysis discovers new genes and provides an integrated view of arginine regulation. Microbiology 152:3343-3354.
    • (2006) Microbiology , vol.152 , pp. 3343-3354
    • Caldara, M.1    Charlier, D.2    Cunin, R.3
  • 9
    • 34548821892 scopus 로고    scopus 로고
    • ArgR-dependent repression of arginine and histidine transport genes in Escherichia coli K-12
    • Caldara, M., P. N. Minh, S. Bostoen, J. Massant, and D. Charlier. 2007. ArgR-dependent repression of arginine and histidine transport genes in Escherichia coli K-12. J. Mol. Biol. 373:251-267.
    • (2007) J. Mol. Biol. , vol.373 , pp. 251-267
    • Caldara, M.1    Minh, P.N.2    Bostoen, S.3    Massant, J.4    Charlier, D.5
  • 10
    • 0033579535 scopus 로고    scopus 로고
    • Repression and activation of arginine transport genes in Escherichia coli K 12 by the ArgP protein
    • Celis, R. T. 1999. Repression and activation of arginine transport genes in Escherichia coli K 12 by the ArgP protein. J. Mol. Biol. 294:1087-1095.
    • (1999) J. Mol. Biol. , vol.294 , pp. 1087-1095
    • Celis, R.T.1
  • 12
    • 80052615116 scopus 로고    scopus 로고
    • The PurR regulon in Escherichia coli K-12 MG1655
    • Cho, B. K., et al. 2011. The PurR regulon in Escherichia coli K-12 MG1655. Nucleic Acids Res. 39:6456-6464.
    • (2011) Nucleic Acids Res. , vol.39 , pp. 6456-6464
    • Cho, B.K.1
  • 13
    • 0001570910 scopus 로고    scopus 로고
    • Osmoregulation
    • F. C. Neidhardt et al. (ed.), 2nd ed. American Society for Microbiology, Washington, DC
    • Csonka, L. N., and W. Epstein. 1996. Osmoregulation, p. 1210-1223. In F. C. Neidhardt et al. (ed.), Escherichia coli and Salmonella: cellular and molecular biology, 2nd ed. American Society for Microbiology, Washington, DC.
    • (1996) Escherichia coli and Salmonella: cellular and molecular biology , pp. 1210-1223
    • Csonka, L.N.1    Epstein, W.2
  • 14
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko, K. A., and B. L. Wanner. 2000. One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc. Natl. Acad. Sci. U. S. A. 97:6640-6645.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 15
    • 44949166755 scopus 로고    scopus 로고
    • The ArgP protein stimulates the Klebsiella pneumoniae gdhA promoter in a lysine-sensitive manner
    • Goss, T. J. 2008. The ArgP protein stimulates the Klebsiella pneumoniae gdhA promoter in a lysine-sensitive manner. J. Bacteriol. 190:4351-4359.
    • (2008) J. Bacteriol. , vol.190 , pp. 4351-4359
    • Goss, T.J.1
  • 16
    • 33846659467 scopus 로고    scopus 로고
    • Transcription factor distribution in Escherichia coli: studies with FNR protein
    • Grainger, D. C., H. Aiba, D. Hurd, D. F. Browning, and S. J. Busby. 2007. Transcription factor distribution in Escherichia coli: studies with FNR protein. Nucleic Acids Res. 35:269-278.
    • (2007) Nucleic Acids Res. , vol.35 , pp. 269-278
    • Grainger, D.C.1    Aiba, H.2    Hurd, D.3    Browning, D.F.4    Busby, S.J.5
  • 17
    • 29144431508 scopus 로고    scopus 로고
    • Studies of the distribution of Escherichia coli cAMP-receptor protein and RNA polymerase along the E. coli chromosome
    • Grainger, D. C., D. Hurd, M. Harrison, J. Holdstock, and S. J. Busby. 2005. Studies of the distribution of Escherichia coli cAMP-receptor protein and RNA polymerase along the E. coli chromosome. Proc. Natl. Acad. Sci. U. S. A. 102:17693-17698.
    • (2005) Proc. Natl. Acad. Sci. U. S. A , vol.102 , pp. 17693-17698
    • Grainger, D.C.1    Hurd, D.2    Harrison, M.3    Holdstock, J.4    Busby, S.J.5
  • 18
    • 4944225301 scopus 로고    scopus 로고
    • Genomic studies with Escherichia coli MelR protein: applications of chromatin immunoprecipitation and microarrays
    • Grainger, D. C., et al. 2004. Genomic studies with Escherichia coli MelR protein: applications of chromatin immunoprecipitation and microarrays. J. Bacteriol. 186:6938-6943.
    • (2004) J. Bacteriol. , vol.186 , pp. 6938-6943
    • Grainger, D.C.1
  • 20
    • 0031796019 scopus 로고    scopus 로고
    • Effect of IciA protein on the expression of the nrd gene encoding ribonucleoside diphosphate reductase in E. coli
    • Han, J. S., H. S. Kwon, J. B. Yim, and D. S. Hwang. 1998. Effect of IciA protein on the expression of the nrd gene encoding ribonucleoside diphosphate reductase in E. coli. Mol. Gen. Genet. 259:610-614.
    • (1998) Mol. Gen. Genet. , vol.259 , pp. 610-614
    • Han, J.S.1    Kwon, H.S.2    Yim, J.B.3    Hwang, D.S.4
  • 21
    • 0025038425 scopus 로고
    • A novel protein binds a key origin sequence to block replication of an E. coli minichromosome
    • Hwang, D. S., and A. Kornberg. 1990. A novel protein binds a key origin sequence to block replication of an E. coli minichromosome. Cell 63:325-331.
    • (1990) Cell , vol.63 , pp. 325-331
    • Hwang, D.S.1    Kornberg, A.2
  • 22
    • 0026490232 scopus 로고
    • Opposed actions of regulatory proteins, DnaA and IciA, in opening the replication origin of Escherichia coli
    • Hwang, D. S., and A. Kornberg. 1992. Opposed actions of regulatory proteins, DnaA and IciA, in opening the replication origin of Escherichia coli. J. Biol. Chem. 267:23087-23091.
    • (1992) J. Biol. Chem. , vol.267 , pp. 23087-23091
    • Hwang, D.S.1    Kornberg, A.2
  • 23
    • 0026806408 scopus 로고
    • IciA protein, a specific inhibitor of initiation of Escherichia coli chromosomal replication
    • Hwang, D. S., B. Thony, and A. Kornberg. 1992. IciA protein, a specific inhibitor of initiation of Escherichia coli chromosomal replication. J. Biol. Chem. 267:2209-2213.
    • (1992) J. Biol. Chem. , vol.267 , pp. 2209-2213
    • Hwang, D.S.1    Thony, B.2    Kornberg, A.3
  • 24
    • 77955141792 scopus 로고    scopus 로고
    • Prokaryotic genome regulation: multifactor promoters, multitarget regulators and hierarchic networks
    • Ishihama, A. 2010. Prokaryotic genome regulation: multifactor promoters, multitarget regulators and hierarchic networks. FEMS Microbiol. Rev. 34:628-645.
    • (2010) FEMS Microbiol. Rev. , vol.34 , pp. 628-645
    • Ishihama, A.1
  • 25
    • 58349095446 scopus 로고    scopus 로고
    • In-vitro helix opening of M. tuberculosis oriC by DnaA occurs at precise location and is inhibited by IciA like protein
    • Kumar, S., A. Farhana, and S. E. Hasnain. 2009. In-vitro helix opening of M. tuberculosis oriC by DnaA occurs at precise location and is inhibited by IciA like protein. PLoS One 4:e4139.
    • (2009) PLoS One , vol.4
    • Kumar, S.1    Farhana, A.2    Hasnain, S.E.3
  • 26
    • 34248997589 scopus 로고    scopus 로고
    • Environmental regulation operating at the promoter clearance step of bacterial transcription
    • Laishram, R. S., and J. Gowrishankar. 2007. Environmental regulation operating at the promoter clearance step of bacterial transcription. Genes Dev. 21:1258-1272.
    • (2007) Genes Dev. , vol.21 , pp. 1258-1272
    • Laishram, R.S.1    Gowrishankar, J.2
  • 27
    • 0030742606 scopus 로고    scopus 로고
    • The binding of two dimers of IciA protein to the dnaA promoter 1P element enhances the binding of RNA polymerase to the dnaA promoter 1P
    • Lee, Y., H. Lee, J. Yim, and D. Hwang. 1997. The binding of two dimers of IciA protein to the dnaA promoter 1P element enhances the binding of RNA polymerase to the dnaA promoter 1P. Nucleic Acids Res. 25:3486-3489.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 3486-3489
    • Lee, Y.1    Lee, H.2    Yim, J.3    Hwang, D.4
  • 28
    • 0040075183 scopus 로고    scopus 로고
    • Occlusion of RNA polymerase by oligomerization of DnaA protein over the dnaA promoter of Escherichia coli
    • Lee, Y. S., and D. S. Hwang. 1997. Occlusion of RNA polymerase by oligomerization of DnaA protein over the dnaA promoter of Escherichia coli. J. Biol. Chem. 272:83-88.
    • (1997) J. Biol. Chem. , vol.272 , pp. 83-88
    • Lee, Y.S.1    Hwang, D.S.2
  • 29
    • 0030063215 scopus 로고    scopus 로고
    • Transcriptional activation of the dnaA gene encoding the initiator for oriC replication by IciA protein, an inhibitor of in vitro oriC replication in Escherichia coli
    • Lee, Y. S., H. Kim, and D. S. Hwang. 1996. Transcriptional activation of the dnaA gene encoding the initiator for oriC replication by IciA protein, an inhibitor of in vitro oriC replication in Escherichia coli. Mol. Microbiol. 19:389-396.
    • (1996) Mol. Microbiol. , vol.19 , pp. 389-396
    • Lee, Y.S.1    Kim, H.2    Hwang, D.S.3
  • 30
    • 58949097886 scopus 로고    scopus 로고
    • Structure and function of the LysR-type transcriptional regulator (LTTR) family proteins
    • Maddocks, S. E., and P. C. Oyston. 2008. Structure and function of the LysR-type transcriptional regulator (LTTR) family proteins. Microbiology 154:3609-3623.
    • (2008) Microbiology , vol.154 , pp. 3609-3623
    • Maddocks, S.E.1    Oyston, P.C.2
  • 32
    • 2442667786 scopus 로고    scopus 로고
    • Evidence for an arginine exporter encoded by yggA (argO) that is regulated by the LysR-type transcriptional regulator ArgP in Escherichia coli
    • Nandineni, M. R., and J. Gowrishankar. 2004. Evidence for an arginine exporter encoded by yggA (argO) that is regulated by the LysR-type transcriptional regulator ArgP in Escherichia coli. J. Bacteriol. 186:3539-3546.
    • (2004) J. Bacteriol. , vol.186 , pp. 3539-3546
    • Nandineni, M.R.1    Gowrishankar, J.2
  • 33
    • 4544359324 scopus 로고    scopus 로고
    • Osmosensitivity associated with insertions in argP (iciA) or glnE in glutamate synthasedeficient mutants of Escherichia coli
    • Nandineni, M. R., R. S. Laishram, and J. Gowrishankar. 2004. Osmosensitivity associated with insertions in argP (iciA) or glnE in glutamate synthasedeficient mutants of Escherichia coli. J. Bacteriol. 186:6391-6399.
    • (2004) J. Bacteriol. , vol.186 , pp. 6391-6399
    • Nandineni, M.R.1    Laishram, R.S.2    Gowrishankar, J.3
  • 34
    • 0028229613 scopus 로고
    • Roles of LysP and CadC in mediating the lysine requirement for acid induction of the Escherichia coli cad operon
    • Neely, M. N., C. L. Dell, and E. R. Olson. 1994. Roles of LysP and CadC in mediating the lysine requirement for acid induction of the Escherichia coli cad operon. J. Bacteriol. 176:3278-3285.
    • (1994) J. Bacteriol. , vol.176 , pp. 3278-3285
    • Neely, M.N.1    Dell, C.L.2    Olson, E.R.3
  • 35
    • 70350144292 scopus 로고    scopus 로고
    • NsrR targets in the Escherichia coli genome: new insights into DNA sequence requirements for binding and a role for NsrR in the regulation of motility
    • Partridge, J. D., D. M. Bodenmiller, M. S. Humphrys, and S. Spiro. 2009. NsrR targets in the Escherichia coli genome: new insights into DNA sequence requirements for binding and a role for NsrR in the regulation of motility. Mol. Microbiol. 73:680-694.
    • (2009) Mol. Microbiol. , vol.73 , pp. 680-694
    • Partridge, J.D.1    Bodenmiller, D.M.2    Humphrys, M.S.3    Spiro, S.4
  • 36
    • 0001501761 scopus 로고    scopus 로고
    • Biosynthesis of threonine and lysine
    • F. C. Neidhardt et al. (ed.), 2nd ed. American Society for Microbiology, Washington, DC
    • Patte, J.-C. 1996. Biosynthesis of threonine and lysine, p. 528-541. In F. C. Neidhardt et al. (ed.), Escherichia coli and Salmonella: cellular and molecular biology, 2nd ed. American Society for Microbiology, Washington, DC.
    • (1996) Escherichia coli and Salmonella: cellular and molecular biology , pp. 528-541
    • Patte, J.-C.1
  • 37
    • 72049118848 scopus 로고    scopus 로고
    • Competitive activation of the Escherichia coli argO gene coding for an arginine exporter by the transcriptional regulators Lrp and ArgP
    • Peeters, E., P. N. Le Minh, M. Foulquie-Moreno, and D. Charlier. 2009. Competitive activation of the Escherichia coli argO gene coding for an arginine exporter by the transcriptional regulators Lrp and ArgP. Mol. Microbiol. 74:1513-1526.
    • (2009) Mol. Microbiol. , vol.74 , pp. 1513-1526
    • Peeters, E.1    Le Minh, P.N.2    Foulquie-Moreno, M.3    Charlier, D.4
  • 38
    • 84959039264 scopus 로고    scopus 로고
    • Biosynthesis of glutamate, aspartate, asparagine, L-alanine, and D-alanine
    • 6 July, R. Curtiss III et al.(ed.), ASM Press, Washington, DC. doi:10.1128/ecosal.3.6.1.3
    • Reitzer, L. 6 July 2004, posting date. Module 3.6.1.3, Biosynthesis of glutamate, aspartate, asparagine, L-alanine, and D-alanine. In R. Curtiss III et al. (ed.), EcoSal Escherichia coli and Salmonella: cellular and molecular biology. ASM Press, Washington, DC. doi:10.1128/ecosal.3.6.1.3.
    • (2004) EcoSal Escherichia coli and Salmonella: cellular and molecular biology
    • Reitzer, L.1
  • 39
    • 0345531094 scopus 로고    scopus 로고
    • Regulation of lysine biosynthesis and transport genes in bacteria: yet another RNA riboswitch?
    • Rodionov, D. A., A. G. Vitreschak, A. A. Mironov, and M. S. Gelfand. 2003. Regulation of lysine biosynthesis and transport genes in bacteria: yet another RNA riboswitch? Nucleic Acids Res. 31:6748-6757.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 6748-6757
    • Rodionov, D.A.1    Vitreschak, A.G.2    Mironov, A.A.3    Gelfand, M.S.4
  • 40
    • 0031696840 scopus 로고    scopus 로고
    • Linkage map of Escherichia coli K-12, edition 10: the physical map
    • Rudd, K. E. 1998. Linkage map of Escherichia coli K-12, edition 10: the physical map. Microbiol. Mol. Biol. Rev. 62:985-1019.
    • (1998) Microbiol. Mol. Biol. Rev. , vol.62 , pp. 985-1019
    • Rudd, K.K.1
  • 41
    • 79956103571 scopus 로고    scopus 로고
    • Identification of ArgP and Lrp as transcriptional regulators of lysP, the gene encoding the specific lysine permease of Escherichia coli
    • Ruiz, J., I. Haneburger, and K. Jung. 2011. Identification of ArgP and Lrp as transcriptional regulators of lysP, the gene encoding the specific lysine permease of Escherichia coli. J. Bacteriol. 193:2536-2548.
    • (2011) J. Bacteriol. , vol.193 , pp. 2536-2548
    • Ruiz, J.1    Haneburger, I.2    Jung, K.3
  • 43
    • 47249152834 scopus 로고    scopus 로고
    • The Escherichia coli RutR transcription factor binds at targets within genes as well as intergenic regions
    • Shimada, T., A. Ishihama, S. J. Busby, and D. C. Grainger. 2008. The Escherichia coli RutR transcription factor binds at targets within genes as well as intergenic regions. Nucleic Acids Res. 36:3950-3955.
    • (2008) Nucleic Acids Res. , vol.36 , pp. 3950-3955
    • Shimada, T.1    Ishihama, A.2    Busby, S.J.3    Grainger, D.C.4
  • 44
    • 0242298623 scopus 로고    scopus 로고
    • An mRNA structure in bacteria that controls gene expression by binding lysine
    • Sudarsan, N., J. K. Wickiser, S. Nakamura, M. S. Ebert, and R. R. Breaker. 2003. An mRNA structure in bacteria that controls gene expression by binding lysine. Genes Dev. 17:2688-2697.
    • (2003) Genes Dev. , vol.17 , pp. 2688-2697
    • Sudarsan, N.1    Wickiser, J.K.2    Nakamura, S.3    Ebert, M.S.4    Breaker, R.R.5
  • 45
    • 37749014565 scopus 로고    scopus 로고
    • The membraneintegrated transcriptional activator CadC of Escherichia coli senses lysine indirectly via the interaction with the lysine permease LysP
    • Tetsch, L., C. Koller, I. Haneburger, and K. Jung. 2008. The membraneintegrated transcriptional activator CadC of Escherichia coli senses lysine indirectly via the interaction with the lysine permease LysP. Mol. Microbiol. 67:570-583.
    • (2008) Mol. Microbiol. , vol.67 , pp. 570-583
    • Tetsch, L.1    Koller, C.2    Haneburger, I.3    Jung, K.4
  • 46
    • 0025828522 scopus 로고
    • iciA, an Escherichia coli gene encoding a specific inhibitor of chromosomal initiation of replication in vitro
    • Thony, B., D. S. Hwang, L. Fradkin, and A. Kornberg. 1991. iciA, an Escherichia coli gene encoding a specific inhibitor of chromosomal initiation of replication in vitro. Proc. Natl. Acad. Sci. U. S. A. 88:4066-4070.
    • (1991) Proc. Natl. Acad. Sci. U. S. A , vol.88 , pp. 4066-4070
    • Thony, B.1    Hwang, D.S.2    Fradkin, L.3    Kornberg, A.4
  • 47
    • 34250619055 scopus 로고    scopus 로고
    • Genomic analysis of protein-DNA interactions in bacteria: insights into transcription and chromosome organization
    • Wade, J. T., K. Struhl, S. J. Busby, and D. C. Grainger. 2007. Genomic analysis of protein-DNA interactions in bacteria: insights into transcription and chromosome organization. Mol. Microbiol. 65:21-26.
    • (2007) Mol. Microbiol. , vol.65 , pp. 21-26
    • Wade, J.T.1    Struhl, K.2    Busby, S.J.3    Grainger, D.C.4
  • 48
    • 0030014707 scopus 로고    scopus 로고
    • Interaction of the IciA protein with ATrich regions in plasmid replication origins
    • Wei, T., and R. Bernander. 1996. Interaction of the IciA protein with ATrich regions in plasmid replication origins. Nucleic Acids Res. 24:1865-1872.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 1865-1872
    • Wei, T.1    Bernander, R.2
  • 49
    • 79952382558 scopus 로고    scopus 로고
    • The Escherichia coli K-12 MntR miniregulon includes dps, which encodes the major stationary-phase DNA-binding protein
    • Yamamoto, K., A. Ishihama, S. J. Busby, and D. C. Grainger. 2011. The Escherichia coli K-12 MntR miniregulon includes dps, which encodes the major stationary-phase DNA-binding protein. J. Bacteriol. 193:1477-1480.
    • (2011) J. Bacteriol. , vol.193 , pp. 1477-1480
    • Yamamoto, K.1    Ishihama, A.2    Busby, S.J.3    Grainger, D.C.4
  • 50
    • 77649270286 scopus 로고    scopus 로고
    • Crystal structure of ArgP from Mycobacterium tuberculosis confirms two distinct conformations of full-length LysR transcriptional regulators and reveals its function in DNA binding and transcriptional regulation
    • Zhou, X., et al. 2010. Crystal structure of ArgP from Mycobacterium tuberculosis confirms two distinct conformations of full-length LysR transcriptional regulators and reveals its function in DNA binding and transcriptional regulation. J. Mol. Biol. 396:1012-1024.
    • (2010) J. Mol. Biol. , vol.396 , pp. 1012-1024
    • Zhou, X.1


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