메뉴 건너뛰기




Volumn 191, Issue 17, 2009, Pages 5549-5552

Polyamines are not required for aerobic growth of Escherichia coli: Preparation of a strain with deletions in all of the genes for polyamine biosynthesis

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSYLMETHIONINE DECARBOXYLASE; AGMATINE UREAHYDROLASE; ARGININE DECARBOXYLASE; HYDROLASE; LYSINE DECARBOXYLASE; ORNITHINE DECARBOXYLASE; POLYAMINE DERIVATIVE; SPERMIDINE; SPERMIDINE SYNTHASE; UNCLASSIFIED DRUG;

EID: 68949159908     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.00381-09     Document Type: Article
Times cited : (63)

References (27)
  • 1
    • 31544450286 scopus 로고    scopus 로고
    • Baba, T., T. Ara, M. Hasegawa, Y. Takai, Y. Okumura, M. Baba, K. A. Datsenko, M. Tomita, B. L. Wanner, and H. Mori. 2006. Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection. Mol. Syst. Biol. 2:2006.0008.
    • Baba, T., T. Ara, M. Hasegawa, Y. Takai, Y. Okumura, M. Baba, K. A. Datsenko, M. Tomita, B. L. Wanner, and H. Mori. 2006. Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection. Mol. Syst. Biol. 2:2006.0008.
  • 2
    • 0027318197 scopus 로고
    • Oxygen toxicity in a polyamine-depleted spe2 delta mutant of Saccharomyces cerevisiae
    • Balasundaram, D., C. W. Tabor, and H. Tabor. 1993. Oxygen toxicity in a polyamine-depleted spe2 delta mutant of Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA 90:4693-4697.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 4693-4697
    • Balasundaram, D.1    Tabor, C.W.2    Tabor, H.3
  • 3
    • 44349133214 scopus 로고    scopus 로고
    • Hypusine modification for growth is the major function of spermidine in Saccharomyces cerevisiae polyamine auxotrophs grown in limiting spermidine
    • Chattopadhyay, M. K., M. H. Park, and H. Tabor. 2008. Hypusine modification for growth is the major function of spermidine in Saccharomyces cerevisiae polyamine auxotrophs grown in limiting spermidine. Proc. Natl. Acad. Sci. USA 105:6554-6559.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 6554-6559
    • Chattopadhyay, M.K.1    Park, M.H.2    Tabor, H.3
  • 4
    • 0037418252 scopus 로고    scopus 로고
    • Polyamines protect Escherichia coli cells from the toxic effect of oxygen
    • Chattopadhyay, M. K., C. W. Tabor, and H. Tabor. 2003. Polyamines protect Escherichia coli cells from the toxic effect of oxygen. Proc. Natl. Acad. Sci. USA 100:2261-2265.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 2261-2265
    • Chattopadhyay, M.K.1    Tabor, C.W.2    Tabor, H.3
  • 5
    • 0004139057 scopus 로고    scopus 로고
    • Cohen, S, ed, Oxford University Press, New York, NY
    • Cohen, S. (ed.). 1998. A guide to the polyamines. Oxford University Press, New York, NY.
    • (1998) A guide to the polyamines
  • 6
    • 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. USA 97:6640-6645.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 7
    • 0018836655 scopus 로고
    • Lysine decarboxylase mutants of Escherichia coli: Evidence for two enzyme forms
    • Goldemberg, S. H. 1980. Lysine decarboxylase mutants of Escherichia coli: evidence for two enzyme forms. J. Bacteriol. 141:1428-1431.
    • (1980) J. Bacteriol , vol.141 , pp. 1428-1431
    • Goldemberg, S.H.1
  • 8
    • 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. 139:11-16.
    • (2006) J. Biochem , vol.139 , pp. 11-16
    • Igarashi, K.1    Kashiwagi, K.2
  • 9
    • 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
  • 10
    • 0141651685 scopus 로고    scopus 로고
    • Abnormal growth of polyamine-deficient Escherichia coli mutant is partially caused by oxidative stress-induced damage
    • Jung, T. J. Oh, and I. G. Kim. 2003. Abnormal growth of polyamine-deficient Escherichia coli mutant is partially caused by oxidative stress-induced damage. Arch. Biochem. Biophys. 418:125-132.
    • (2003) Arch. Biochem. Biophys , vol.418 , pp. 125-132
    • Jung, T.J.O.1    Kim, I.G.2
  • 12
    • 57249098381 scopus 로고    scopus 로고
    • Polyamine as a signaling molecule for controlling an adaptive mutation
    • Jung, I. L., and I. G. Kim. 2008. Polyamine as a signaling molecule for controlling an adaptive mutation. Biochemistry 73:1228-1234.
    • (2008) Biochemistry , vol.73 , pp. 1228-1234
    • Jung, I.L.1    Kim, I.G.2
  • 13
    • 0025720216 scopus 로고
    • Coexistence of the genes for putrescine transport protein and ornithine decarboxylase at 16 min on Escherichia coli chromosome
    • Kashiwagi, K., T. Suzuki, F. Suzuki, T. Furuchi, H. Kobayashi, and K. Igarashi. 1991. Coexistence of the genes for putrescine transport protein and ornithine decarboxylase at 16 min on Escherichia coli chromosome. J. Biol. Chem. 266:20922-20927.
    • (1991) J. Biol. Chem , vol.266 , pp. 20922-20927
    • Kashiwagi, K.1    Suzuki, T.2    Suzuki, F.3    Furuchi, T.4    Kobayashi, H.5    Igarashi, K.6
  • 14
    • 0030840870 scopus 로고    scopus 로고
    • Characterization of a second lysine decarboxylase isolated from Escherichia coli
    • Kikuchi, Y., H. Kojima, T. Tanaka, Y. Takatsuka, and Y. Kamio. 1997. Characterization of a second lysine decarboxylase isolated from Escherichia coli. J. Bacteriol. 179:4486-4492.
    • (1997) J. Bacteriol , vol.179 , pp. 4486-4492
    • Kikuchi, Y.1    Kojima, H.2    Tanaka, T.3    Takatsuka, Y.4    Kamio, Y.5
  • 15
    • 0032457906 scopus 로고    scopus 로고
    • Oxygen sensing by the global regulator, FNR: The role of the iron-sulfur cluster
    • Kiley, P. J., and H. Beinert. 1998. Oxygen sensing by the global regulator, FNR: the role of the iron-sulfur cluster. FEMS Microbiol. Rev. 22:341-352.
    • (1998) FEMS Microbiol. Rev , vol.22 , pp. 341-352
    • Kiley, P.J.1    Beinert, H.2
  • 16
    • 0026772547 scopus 로고
    • Nucleotide sequence of the Escherichia coli cad operon: A system for neutralization of low extracellular pH
    • Meng, S. Y., and G. N. Bennett. 1992. Nucleotide sequence of the Escherichia coli cad operon: a system for neutralization of low extracellular pH. J. Bacteriol. 174:2659-2669.
    • (1992) J. Bacteriol , vol.174 , pp. 2659-2669
    • Meng, S.Y.1    Bennett, G.N.2
  • 17
    • 0003842951 scopus 로고
    • Miller, J. H, ed, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Miller, J. H. (ed.). 1992. A short course in bacterial genetics. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1992) A short course in bacterial genetics
  • 18
    • 0024521325 scopus 로고
    • Involvement of antizyme in stabilization of ornithine decarboxylase caused by inhibitors of polyamine synthesis
    • Murakami, Y., M. Nishiyama, and S. Hayashi. 1989. Involvement of antizyme in stabilization of ornithine decarboxylase caused by inhibitors of polyamine synthesis. Eur. J. Biochem. 180:181-184.
    • (1989) Eur. J. Biochem , vol.180 , pp. 181-184
    • Murakami, Y.1    Nishiyama, M.2    Hayashi, S.3
  • 19
    • 0015970007 scopus 로고
    • Chemical properties of Escherichia coli lysine decarboxylase including a segment of its pyridoxal 5-phosphate binding site
    • Sabo, D. L., and E. H. Fischer. 1974. Chemical properties of Escherichia coli lysine decarboxylase including a segment of its pyridoxal 5-phosphate binding site. Biochemistry 13:670-676.
    • (1974) Biochemistry , vol.13 , pp. 670-676
    • Sabo, D.L.1    Fischer, E.H.2
  • 20
    • 0023673760 scopus 로고
    • Two-dimensional gel electrophoretic analysis of Escherichia coli proteins: Influence of various anaerobic growth conditions and the fnr gene product on cellular protein composition
    • Sawers, R. G., E. Zehelein, and A. Bock. 1988. Two-dimensional gel electrophoretic analysis of Escherichia coli proteins: influence of various anaerobic growth conditions and the fnr gene product on cellular protein composition. Arch. Microbiol. 149:240-244.
    • (1988) Arch. Microbiol , vol.149 , pp. 240-244
    • Sawers, R.G.1    Zehelein, E.2    Bock, A.3
  • 21
    • 0027479926 scopus 로고
    • Nucleotide sequence of the adi gene, which encodes the biodegradative acid-induced arginine decarboxylase of Escherichia coli
    • Stim, K. P., and G. N. Bennett. 1993. Nucleotide sequence of the adi gene, which encodes the biodegradative acid-induced arginine decarboxylase of Escherichia coli. J. Bacteriol. 175:1221-1234.
    • (1993) J. Bacteriol , vol.175 , pp. 1221-1234
    • Stim, K.P.1    Bennett, G.N.2
  • 23
    • 0022001625 scopus 로고
    • Polyamines in microorganisms
    • Tabor, C. W., and H. Tabor. 1985. Polyamines in microorganisms. Microbiol. Rev. 49:81-99.
    • (1985) Microbiol. Rev , vol.49 , pp. 81-99
    • Tabor, C.W.1    Tabor, H.2
  • 24
    • 0019196018 scopus 로고
    • Construction of an Escherichia coli strain unable to synthesize putrescine, spermidine, or cadaverine: Characterization of two genes controlling lysine decarboxylase
    • Tabor, H., E. W. Hafner, and C. W. Tabor. 1980. Construction of an Escherichia coli strain unable to synthesize putrescine, spermidine, or cadaverine: characterization of two genes controlling lysine decarboxylase. J. Bacteriol. 144:952-956.
    • (1980) J. Bacteriol , vol.144 , pp. 952-956
    • Tabor, H.1    Hafner, E.W.2    Tabor, C.W.3
  • 25
    • 77049313195 scopus 로고
    • Acetylornithinase of Escherichia coli: Partial purification and some properties
    • Vogel, H. J., and D. M. Bonner. 1956. Acetylornithinase of Escherichia coli: partial purification and some properties. J. Biol. Chem. 218:97-106.
    • (1956) J. Biol. Chem , vol.218 , pp. 97-106
    • Vogel, H.J.1    Bonner, D.M.2
  • 26
    • 34547676811 scopus 로고    scopus 로고
    • Posttranslational synthesis of hypusine: Evolutionary progression and specificity of the hypusine modification
    • Wolff, E. C., K. R. Kang, Y. S. Kim, and M. H. Park. 2007. Posttranslational synthesis of hypusine: evolutionary progression and specificity of the hypusine modification. Amino Acids 33:341-350.
    • (2007) Amino Acids , vol.33 , pp. 341-350
    • Wolff, E.C.1    Kang, K.R.2    Kim, Y.S.3    Park, M.H.4
  • 27
    • 0030808549 scopus 로고    scopus 로고
    • The Escherichia coli ldcC gene encodes another lysine decarboxylase, probably a constitutive enzyme
    • Yamamoto, Y., Y. Miwa, K. Miyoshi, J. Furuyama, and H. Ohmori. 1997. The Escherichia coli ldcC gene encodes another lysine decarboxylase, probably a constitutive enzyme. Genes Genet. Syst. 72:167-172.
    • (1997) Genes Genet. Syst , vol.72 , pp. 167-172
    • Yamamoto, Y.1    Miwa, Y.2    Miyoshi, K.3    Furuyama, J.4    Ohmori, H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.