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Volumn 189, Issue 6, 2007, Pages 2359-2368

Enhancement of the synthesis of RpoN, Cra, and H-NS by polyamines at the level of translation in Escherichia coli cultured with glucose and glutamate

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL DNA; ESCHERICHIA COLI PROTEIN; FACTOR FOR INVERSION STIMULATION; GLUCOSE; GLUTAMIC ACID; HISTONE LIKE NUCLEOID STRUCTURING PROTEIN; MESSENGER RNA; POLYAMINE; PROTEIN CRA; SIGMA FACTOR RPON; SIGMA FACTOR RPOS; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR CRA; TRANSCRIPTION FACTOR CYA; UNCLASSIFIED DRUG;

EID: 33947096829     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.01562-06     Document Type: Article
Times cited : (36)

References (39)
  • 1
    • 0032716841 scopus 로고    scopus 로고
    • Growth phase-dependent variation in protein composition of the Escherichia coli nucleoid
    • Ali Azam, T., 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
    • Ali Azam, T.1    Iwata, A.2    Nishimura, A.3    Ueda, S.4    Ishihama, A.5
  • 2
    • 0025293534 scopus 로고
    • F RNA polymerase by flhD and flhC flagellar regulatory genes
    • F RNA polymerase by flhD and flhC flagellar regulatory genes. J. Bacteriol. 172:4106-4108.
    • (1990) J. Bacteriol , vol.172 , pp. 4106-4108
    • Arnosti, D.N.1
  • 4
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 5
    • 0004139057 scopus 로고    scopus 로고
    • Oxford University Press, Oxford, United Kingdom
    • Cohen, S. S. 1998. A guide to the polyamines, p. 1-543. Oxford University Press, Oxford, United Kingdom.
    • (1998) A guide to the polyamines , pp. 1-543
    • Cohen, S.S.1
  • 6
    • 0016757779 scopus 로고
    • Isolation, characterization, and mapping of Escherichia coli mutants blocked in the synthesis of ornithine decarboxylase
    • Cunningham-Rundles, S., and W. K. Maas. 1975. Isolation, characterization, and mapping of Escherichia coli mutants blocked in the synthesis of ornithine decarboxylase. J. Bacteriol. 124:791-799.
    • (1975) J. Bacteriol , vol.124 , pp. 791-799
    • Cunningham-Rundles, S.1    Maas, W.K.2
  • 7
    • 0025312772 scopus 로고
    • The ompA 5′ untranslated RNA segment functions in Escherichia coli as a growth-rate-regulated mRNA stabilizer whose activity is unrelated to translational efficiency
    • Emory, S. A., and J. G. Belasco. 1990. The ompA 5′ untranslated RNA segment functions in Escherichia coli as a growth-rate-regulated mRNA stabilizer whose activity is unrelated to translational efficiency. J. Bacteriol. 172:4472-4481.
    • (1990) J. Bacteriol , vol.172 , pp. 4472-4481
    • Emory, S.A.1    Belasco, J.G.2
  • 8
    • 33646902489 scopus 로고    scopus 로고
    • Enhancement of +1 frameshift by polyamines during translation of polypeptide release factor 2 in Escherichia coli
    • Higashi, K., K. Kashiwagi, S. Taniguchi, Y. Terui, K. Yamamoto, A. Ishihama, and K. Igarashi. 2006. Enhancement of +1 frameshift by polyamines during translation of polypeptide release factor 2 in Escherichia coli. J. Biol. Chem. 281:9527-9537.
    • (2006) J. Biol. Chem , vol.281 , pp. 9527-9537
    • Higashi, K.1    Kashiwagi, K.2    Taniguchi, S.3    Terui, Y.4    Yamamoto, K.5    Ishihama, A.6    Igarashi, K.7
  • 9
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • Ho, S. N., H. D. Hunt, R. M. Horton, J. K. Pullen, and L. R. Pease. 1989. Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 77:51-59.
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 11
    • 0022512208 scopus 로고
    • Formation of a compensatory polyamine by Escherichia coli polyamine-requiring mutants during growth in the absence of polyamines
    • Igarashi, K., K. Kashiwagi, H. Hamasaki, A. Miura, T. Kakegawa, S. Hirose, and S. Matsuzaki. 1986. Formation of a compensatory polyamine by Escherichia coli polyamine-requiring mutants during growth in the absence of polyamines. J. Bacteriol. 166:128-134.
    • (1986) J. Bacteriol , vol.166 , pp. 128-134
    • Igarashi, K.1    Kashiwagi, K.2    Hamasaki, H.3    Miura, A.4    Kakegawa, T.5    Hirose, S.6    Matsuzaki, S.7
  • 12
    • 0031047822 scopus 로고    scopus 로고
    • Molecular mechanism of polyamine stimulation of the synthesis of oligopeptide-binding protein
    • Igarashi, K., T. Saisho, M. Yuguchi, and K. Kashiwagi. 1997. Molecular mechanism of polyamine stimulation of the synthesis of oligopeptide-binding protein. J. Biol. Chem. 272:4058-4064.
    • (1997) J. Biol. Chem , vol.272 , pp. 4058-4064
    • Igarashi, K.1    Saisho, T.2    Yuguchi, M.3    Kashiwagi, K.4
  • 13
    • 0033572636 scopus 로고    scopus 로고
    • Polyamine transport in bacteria and yeast
    • Igarashi, K., and K. Kashiwagi. 1999. Polyamine transport in bacteria and yeast. Biochem. J. 344:633-642.
    • (1999) Biochem. J , vol.344 , pp. 633-642
    • Igarashi, K.1    Kashiwagi, K.2
  • 14
    • 0034685624 scopus 로고    scopus 로고
    • Polyamines: Mysterious modulators of cellular functions
    • Igarashi, K., and K. Kashiwagi. 2000. Polyamines: mysterious modulators of cellular functions. Biochem. Biophys. Res. Commun. 271:559-564.
    • (2000) Biochem. Biophys. Res. Commun , vol.271 , pp. 559-564
    • Igarashi, K.1    Kashiwagi, K.2
  • 15
    • 32944472627 scopus 로고    scopus 로고
    • Polyamine modulon in Escherichia coli: Genes involved in the stimulation of cell growth by polyamines
    • Igarashi, K., and K. Kashiwagi. 2006. Polyamine modulon in Escherichia coli: genes involved in the stimulation of cell growth by polyamines. J. Biochem. (Tokyo) 139:11-16.
    • (2006) J. Biochem. (Tokyo) , vol.139 , pp. 11-16
    • Igarashi, K.1    Kashiwagi, K.2
  • 16
    • 0033765113 scopus 로고    scopus 로고
    • Functional modulation of Escherichia coli RNA polymerase
    • Ishihama, A. 2000. Functional modulation of Escherichia coli RNA polymerase. Annu. Rev. Microbiol. 54:499-518.
    • (2000) Annu. Rev. Microbiol , vol.54 , pp. 499-518
    • Ishihama, A.1
  • 17
    • 0032493451 scopus 로고    scopus 로고
    • Single amino acid substitution in prokaryote polypeptide release factor 2 permits it to terminate translation at all three stop codons
    • Ito, K., M. Uno, and Y. Nakamura. 1998. Single amino acid substitution in prokaryote polypeptide release factor 2 permits it to terminate translation at all three stop codons. Proc. Natl. Acad. Sci. USA 95:8165-8169.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 8165-8169
    • Ito, K.1    Uno, M.2    Nakamura, Y.3
  • 18
    • 0029810991 scopus 로고    scopus 로고
    • Regulation of RNA polymerase sigma subunit synthesis in Escherichia coli: Intracellular levels of four species of sigma subunit under various growth conditions
    • Jishage, M., A. Iwata, S. Ueda, and A. Ishihama. 1996. Regulation of RNA polymerase sigma subunit synthesis in Escherichia coli: intracellular levels of four species of sigma subunit under various growth conditions. J. Bacteriol. 178:5447-5451.
    • (1996) J. Bacteriol , vol.178 , pp. 5447-5451
    • Jishage, M.1    Iwata, A.2    Ueda, S.3    Ishihama, A.4
  • 19
    • 0032574843 scopus 로고    scopus 로고
    • A stationary phase protein in Escherichia coli with binding activity to the major σ subunit of RNA polymerase
    • Jishage, M., and A. Ishihama. 1998. A stationary phase protein in Escherichia coli with binding activity to the major σ subunit of RNA polymerase. Proc. Natl. Acad. Sci. USA 95:4953-4958.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 4953-4958
    • Jishage, M.1    Ishihama, A.2
  • 20
    • 0028337298 scopus 로고
    • Involvement of ribonuclease III in the enhancement of expression of the speF-potE operon encoding inducible ornithine decarboxylase and polyamine transport protein
    • Kashiwagi, K., R. Watanabe, and K. Igarashi. 1994. Involvement of ribonuclease III in the enhancement of expression of the speF-potE operon encoding inducible ornithine decarboxylase and polyamine transport protein. Biochem. Biophys. Res. Commun. 200:591-597.
    • (1994) Biochem. Biophys. Res. Commun , vol.200 , pp. 591-597
    • Kashiwagi, K.1    Watanabe, R.2    Igarashi, K.3
  • 21
    • 0030943084 scopus 로고    scopus 로고
    • Autogenous and global control of the flagellar master operon
    • Mol. Gen. Genet
    • Kutsukake, K. 1997. Autogenous and global control of the flagellar master operon, flhD, in Salmonella typhimurium. Mol. Gen. Genet. 254:440-448.
    • (1997) flhD, in Salmonella typhimurium , vol.254 , pp. 440-448
    • Kutsukake, K.1
  • 23
    • 0027265852 scopus 로고
    • Estimation of polyamine distribution and polyamine stimulation of protein synthesis in Escherichia coli
    • Miyamoto, S., K. Kashiwagi, K. Ito, S. Watanabe, and K. Igarashi. 1993. Estimation of polyamine distribution and polyamine stimulation of protein synthesis in Escherichia coli. Arch. Biochem. Biophys. 300:63-68.
    • (1993) Arch. Biochem. Biophys , vol.300 , pp. 63-68
    • Miyamoto, S.1    Kashiwagi, K.2    Ito, K.3    Watanabe, S.4    Igarashi, K.5
  • 24
    • 0020408545 scopus 로고
    • The phosphorylation of ribosomal protein S6 in rat tissues following cycloheximide injection, in diabetes, and after denervation of diaphragm. A simple immunological determination of the extent of S6 phosphorylation on protein blots
    • Nielsen, P. J., K. L. Manchester, H. Towbin, J. Gordon, and G. Thomas. 1982. The phosphorylation of ribosomal protein S6 in rat tissues following cycloheximide injection, in diabetes, and after denervation of diaphragm. A simple immunological determination of the extent of S6 phosphorylation on protein blots. J. Biol. Chem. 257:12316-12321.
    • (1982) J. Biol. Chem , vol.257 , pp. 12316-12321
    • Nielsen, P.J.1    Manchester, K.L.2    Towbin, H.3    Gordon, J.4    Thomas, G.5
  • 25
    • 0036366541 scopus 로고    scopus 로고
    • Genome-wide analysis of deoxyadenosine methyltransferase-mediated control of gene expression in Escherichia coli
    • Oshima, T., C. Wada, Y. Kawagoe, T. Ara, M. Maeda, Y. Masuda, S. Hiraga, and H. Mori. 2002. Genome-wide analysis of deoxyadenosine methyltransferase-mediated control of gene expression in Escherichia coli. Mol. Microbiol. 45:673-695.
    • (2002) Mol. Microbiol , vol.45 , pp. 673-695
    • Oshima, T.1    Wada, C.2    Kawagoe, Y.3    Ara, T.4    Maeda, M.5    Masuda, Y.6    Hiraga, S.7    Mori, H.8
  • 26
    • 0027444619 scopus 로고    scopus 로고
    • Ramseier, T. M., D. Nègre, J.-C. Cortay, M. Scarabel, A. J. Cozzone, and M. H. Saier, Jr. 1993. In vitro binding of the pleiotropic transcriptional regulatory protein, FruR, to the fru, pps, ace, pts and icd operons of Escherichia coli and Salmonella typhimurium. J. Mol. Biol. 234:28-44.
    • Ramseier, T. M., D. Nègre, J.-C. Cortay, M. Scarabel, A. J. Cozzone, and M. H. Saier, Jr. 1993. In vitro binding of the pleiotropic transcriptional regulatory protein, FruR, to the fru, pps, ace, pts and icd operons of Escherichia coli and Salmonella typhimurium. J. Mol. Biol. 234:28-44.
  • 27
    • 0004136246 scopus 로고    scopus 로고
    • Dot and slot hybridization of purified RNA
    • J. Sambrook and D. W. Russell ed, 3rd ed. Cold Spring Harbor Laboratory, Cold Spring Harbor, NY
    • Sambrook, J., E. F. Fritsch, and T. Maniatis. 2001. Dot and slot hybridization of purified RNA, p. 7.46-7.50. In J. Sambrook and D. W. Russell (ed.), Molecular cloning: a laboratory manual, 3rd ed. Cold Spring Harbor Laboratory, Cold Spring Harbor, NY.
    • (2001) Molecular cloning: A laboratory manual
    • Sambrook, J.1    Fritsch, E.F.2    Maniatis, T.3
  • 28
    • 0028806048 scopus 로고
    • Quantitative monitoring of gene expression patterns with a complementary DNA microarray
    • Schena, M., D. Shalon, R. W. Davis, and P. O. Brown. 1995. Quantitative monitoring of gene expression patterns with a complementary DNA microarray. Science 270:467-470.
    • (1995) Science , vol.270 , pp. 467-470
    • Schena, M.1    Shalon, D.2    Davis, R.W.3    Brown, P.O.4
  • 29
    • 0021064523 scopus 로고
    • New versatile plasmid vectors for expression of hybrid proteins coded by a cloned gene fused to lacZ gene sequences encoding an enzymatically active carboxyterminal portion of beta-galactosidase
    • Shapira, S. K., J. Chou, F. V. Richaud, and M. J. Casadaban. 1983. New versatile plasmid vectors for expression of hybrid proteins coded by a cloned gene fused to lacZ gene sequences encoding an enzymatically active carboxyterminal portion of beta-galactosidase. Gene 25:71-82.
    • (1983) Gene , vol.25 , pp. 71-82
    • Shapira, S.K.1    Chou, J.2    Richaud, F.V.3    Casadaban, M.J.4
  • 30
    • 24344490227 scopus 로고    scopus 로고
    • Systematic search for the Cra-binding promoters using genomic SELEX system
    • Shimada, T., N. Fujita, M. Maeda, and A. Ishihama. 2005. Systematic search for the Cra-binding promoters using genomic SELEX system. Genes Cells 10:907-918.
    • (2005) Genes Cells , vol.10 , pp. 907-918
    • Shimada, T.1    Fujita, N.2    Maeda, M.3    Ishihama, A.4
  • 31
    • 0032796421 scopus 로고    scopus 로고
    • Multiple control of flagellum biosynthesis in Escherichia coli: Role of H-NS protein and the cyclic AMP-catabolite activator protein complex in transcription of the flhDC master operon
    • Soutourina, O., A. Kolb, E. Krin, C. Laurent-Winter, S. Rimsky, A. Danchin, and P. Bertin. 1999. Multiple control of flagellum biosynthesis in Escherichia coli: role of H-NS protein and the cyclic AMP-catabolite activator protein complex in transcription of the flhDC master operon. J. Bacteriol. 181:7500-7508.
    • (1999) J. Bacteriol , vol.181 , pp. 7500-7508
    • Soutourina, O.1    Kolb, A.2    Krin, E.3    Laurent-Winter, C.4    Rimsky, S.5    Danchin, A.6    Bertin, P.7
  • 32
    • 0030601826 scopus 로고    scopus 로고
    • Systematic mutational analysis revealing the functional domain organization of Escherichia coli nucleoid protein H-NS
    • Ueguchi, C., T. Suzuki, T. Yoshida, K. Tanaka, and T. Mizuno. 1996. Systematic mutational analysis revealing the functional domain organization of Escherichia coli nucleoid protein H-NS. J. Mol. Biol. 263:149-162.
    • (1996) J. Mol. Biol , vol.263 , pp. 149-162
    • Ueguchi, C.1    Suzuki, T.2    Yoshida, T.3    Tanaka, K.4    Mizuno, T.5
  • 33
    • 0025786779 scopus 로고
    • Estimation of polyamine binding to macromolecules and ATP in bovine lymphocytes and rat liver
    • Watanabe, S., K. Kusama-Eguchi, H. Kobayashi, and K. Igarashi. 1991. Estimation of polyamine binding to macromolecules and ATP in bovine lymphocytes and rat liver. J. Biol. Chem. 266:20803-20809.
    • (1991) J. Biol. Chem , vol.266 , pp. 20803-20809
    • Watanabe, S.1    Kusama-Eguchi, K.2    Kobayashi, H.3    Igarashi, K.4
  • 34
    • 33947109647 scopus 로고    scopus 로고
    • Wilson, K., F. M. Ausubel, R. Brent, and R. E. Kingston. 1987. Miniprep of bacterial genomic DNA, p. 2.4.1-2.4.2. In F. M. Ausubel, R. Brent, R. E. Kingston, D. D. Moore, J. G. Seidman, J. A. Smith, and K, Struhl (ed.), Current protocols in molecular biology John Wiley & Sons, Inc., New York, NY.
    • Wilson, K., F. M. Ausubel, R. Brent, and R. E. Kingston. 1987. Miniprep of bacterial genomic DNA, p. 2.4.1-2.4.2. In F. M. Ausubel, R. Brent, R. E. Kingston, D. D. Moore, J. G. Seidman, J. A. Smith, and K, Struhl (ed.), Current protocols in molecular biology John Wiley & Sons, Inc., New York, NY.
  • 35
    • 16244398023 scopus 로고    scopus 로고
    • Transcriptional response of Escherichia coli to external copper
    • Yamamoto, K., and A. Ishihama. 2005. Transcriptional response of Escherichia coli to external copper. Mol. Microbiol. 56:215-227.
    • (2005) Mol. Microbiol , vol.56 , pp. 215-227
    • Yamamoto, K.1    Ishihama, A.2
  • 39
    • 0033529644 scopus 로고    scopus 로고
    • Polyamine stimulation of the synthesis of oligopeptide-binding protein (OppA). Involvement of a structural change of the Shine-Dalgarno sequence and the initiation codon AUG in OppA mRNA
    • Yoshida, M., D. Meksuriyen, K. Kashiwagi, G. Kawai, and K. Igarashi. 1999. Polyamine stimulation of the synthesis of oligopeptide-binding protein (OppA). Involvement of a structural change of the Shine-Dalgarno sequence and the initiation codon AUG in OppA mRNA. J. Biol. Chem. 274:22723-22728.
    • (1999) J. Biol. Chem , vol.274 , pp. 22723-22728
    • Yoshida, M.1    Meksuriyen, D.2    Kashiwagi, K.3    Kawai, G.4    Igarashi, K.5


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