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Volumn 112, Issue 4, 2012, Pages 775-781

Adenosine deamination increases the survival under acidic conditions in Escherichia coli

Author keywords

Acid resistance; Add; Adenosine deamination; Escherichia coli

Indexed keywords

ACID RESISTANCE; AMINES; AMINO ACIDS; CARBOXYLATION;

EID: 84862789502     PISSN: 13645072     EISSN: 13652672     Source Type: Journal    
DOI: 10.1111/j.1365-2672.2012.05246.x     Document Type: Article
Times cited : (29)

References (33)
  • 1
    • 31544450286 scopus 로고    scopus 로고
    • Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection
    • Baba, T., Ara, T., Hasegawa, M., Takai, Y., Okumura, Y., Baba, M., Datsenko, K.A., Tomita, M. et al. (2006) Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection. Mol Syst Biol 2, 2006.0008.
    • (2006) Mol Syst Biol , vol.2 , pp. 20060008
    • Baba, T.1    Ara, T.2    Hasegawa, M.3    Takai, Y.4    Okumura, Y.5    Baba, M.6    Datsenko, K.A.7    Tomita, M.8
  • 2
    • 79952323803 scopus 로고    scopus 로고
    • The role of OmpC and OmpF in acidic resistance in Escherichia coli
    • Bekhit, A., Fukamachi, T., Saito, H. and Kobayashi, H. (2011) The role of OmpC and OmpF in acidic resistance in Escherichia coli. Biol Pharm Bull 34, 330-334.
    • (2011) Biol Pharm Bull , vol.34 , pp. 330-334
    • Bekhit, A.1    Fukamachi, T.2    Saito, H.3    Kobayashi, H.4
  • 3
    • 64549116752 scopus 로고    scopus 로고
    • HU participates in expression of a specific set of genes required for growth and survival at acidic pH in Escherichia coli
    • Bi, H., Sun, L., Fukamachi, T., Saito, H. and Kobayashi, H. (2009) HU participates in expression of a specific set of genes required for growth and survival at acidic pH in Escherichia coli. Curr Microbiol 58, 443-448.
    • (2009) Curr Microbiol , vol.58 , pp. 443-448
    • Bi, H.1    Sun, L.2    Fukamachi, T.3    Saito, H.4    Kobayashi, H.5
  • 4
    • 0035086021 scopus 로고    scopus 로고
    • Escherichia coli acid resistance: cAMP receptor protein and a 20bp cis-acting sequence control pH and stationary phase expression of the gadA and gadBC glutamate decarboxylase genes
    • Castanie-Cornet, M.P. and Foster, J.W. (2001) Escherichia coli acid resistance: cAMP receptor protein and a 20bp cis-acting sequence control pH and stationary phase expression of the gadA and gadBC glutamate decarboxylase genes. Microbiology 147, 709-715.
    • (2001) Microbiology , vol.147 , pp. 709-715
    • Castanie-Cornet, M.P.1    Foster, J.W.2
  • 6
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko, K.A. and Wanner, B.L. (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
    • 9444285788 scopus 로고    scopus 로고
    • Escherichia coli acid resistance: tales of an amateur acidophile
    • Foster, J.W. (2004) Escherichia coli acid resistance: tales of an amateur acidophile. Nat Rev Microbiol 2, 898-907.
    • (2004) Nat Rev Microbiol , vol.2 , pp. 898-907
    • Foster, J.W.1
  • 8
    • 0038782170 scopus 로고    scopus 로고
    • YjdE (AdiC) is the arginine:agmatine antiporter essential for arginine-dependent acid resistance in Escherichia coli
    • Gong, S., Richard, H. and Foster, J.W. (2003) YjdE (AdiC) is the arginine:agmatine antiporter essential for arginine-dependent acid resistance in Escherichia coli. J Bacteriol 185, 4402-4409.
    • (2003) J Bacteriol , vol.185 , pp. 4402-4409
    • Gong, S.1    Richard, H.2    Foster, J.W.3
  • 9
    • 0014060882 scopus 로고
    • Inosine 5′-phosphate dehydrogenase. Site of inhibition by guanosine 5′-phosphate and of inactivation by 6-chloro- and 6-mercaptopurine ribonucleoside 5′-phosphates
    • Hampton, A. and Nomura, A. (1967) Inosine 5′-phosphate dehydrogenase. Site of inhibition by guanosine 5′-phosphate and of inactivation by 6-chloro- and 6-mercaptopurine ribonucleoside 5′-phosphates. Biochemistry 6, 679-689.
    • (1967) Biochemistry , vol.6 , pp. 679-689
    • Hampton, A.1    Nomura, A.2
  • 12
    • 0242659209 scopus 로고    scopus 로고
    • Arginine-agmatine antiporter in extreme acid resistance in Escherichia coli
    • Iyer, R., Williams, C. and Miller, C. (2003) Arginine-agmatine antiporter in extreme acid resistance in Escherichia coli. J Bacteriol 185, 6556-6561.
    • (2003) J Bacteriol , vol.185 , pp. 6556-6561
    • Iyer, R.1    Williams, C.2    Miller, C.3
  • 13
    • 0027251266 scopus 로고
    • The Escherichia coli K-12 "wild types" W3110 and MG1655 have an rph frameshift mutation that leads to pyrimidine starvation due to low pyrE expression levels
    • Jensen, K.F. (1993) The Escherichia coli K-12 "wild types" W3110 and MG1655 have an rph frameshift mutation that leads to pyrimidine starvation due to low pyrE expression levels. J Bacteriol 175, 3401-3407.
    • (1993) J Bacteriol , vol.175 , pp. 3401-3407
    • Jensen, K.F.1
  • 14
    • 0027909395 scopus 로고
    • In situ fermentation monitoring with recombinant firefly luciferase
    • Lasko, D.R. and Wang, D.I. (1993) In situ fermentation monitoring with recombinant firefly luciferase. Biotechnol Bioeng 42, 30-36.
    • (1993) Biotechnol Bioeng , vol.42 , pp. 30-36
    • Lasko, D.R.1    Wang, D.I.2
  • 15
    • 50449147866 scopus 로고
    • Transduction of linked genetic characters of the host by bacteriophage P1
    • Lennox, E.S. (1955) Transduction of linked genetic characters of the host by bacteriophage P1. Virology 1, 190-206.
    • (1955) Virology , vol.1 , pp. 190-206
    • Lennox, E.S.1
  • 17
    • 0037330622 scopus 로고    scopus 로고
    • Global metabolite analysis: the influence of extraction methodology on metabolome profiles of Escherichia coli
    • Maharjan, R.P. and Ferenci, T. (2003) Global metabolite analysis: the influence of extraction methodology on metabolome profiles of Escherichia coli. Anal Biochem 313, 145-154.
    • (2003) Anal Biochem , vol.313 , pp. 145-154
    • Maharjan, R.P.1    Ferenci, T.2
  • 18
    • 11144263144 scopus 로고    scopus 로고
    • pH regulates genes for flagellar motility, catabolism, and oxidative stress in Escherichia coli K-12
    • Maurer, L.M., Yohannes, E., Bondurant, S.S., Radmacher, M. and Slonczewski, J.L. (2005) pH regulates genes for flagellar motility, catabolism, and oxidative stress in Escherichia coli K-12. J Bacteriol 187, 304-319.
    • (2005) J Bacteriol , vol.187 , pp. 304-319
    • Maurer, L.M.1    Yohannes, E.2    Bondurant, S.S.3    Radmacher, M.4    Slonczewski, J.L.5
  • 19
    • 0026772547 scopus 로고
    • Nucleotide sequence of the Escherichia coli cad operon: a system for neutralization of low extracellular pH
    • Meng, S.Y. and Bennett, G.N. (1992a) 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
  • 20
    • 0026772549 scopus 로고
    • Regulation of the Escherichia coli cad operon: location of a site required for acid induction
    • Meng, S.Y. and Bennett, G.N. (1992b) Regulation of the Escherichia coli cad operon: location of a site required for acid induction. J Bacteriol 174, 2670-2678.
    • (1992) J Bacteriol , vol.174 , pp. 2670-2678
    • Meng, S.Y.1    Bennett, G.N.2
  • 21
    • 0017795560 scopus 로고
    • Adenosine deaminase from Escherichia coli
    • Nygaard, P. (1978) Adenosine deaminase from Escherichia coli. Methods Enzymol 51, 508-512.
    • (1978) Methods Enzymol , vol.51 , pp. 508-512
    • Nygaard, P.1
  • 22
    • 65549120315 scopus 로고    scopus 로고
    • A regulatory role of the Bateman domain of IMP dehydrogenase in adenylate nucleotide biosynthesis
    • Pimkin, M., Pimkina, J. and Markham, G.D. (2009) A regulatory role of the Bateman domain of IMP dehydrogenase in adenylate nucleotide biosynthesis. J Biol Chem 284, 7960-7969.
    • (2009) J Biol Chem , vol.284 , pp. 7960-7969
    • Pimkin, M.1    Pimkina, J.2    Markham, G.D.3
  • 24
    • 0041472380 scopus 로고    scopus 로고
    • Acid resistance in Escherichia coli
    • Richard, H.T. and Foster, J.W. (2003) Acid resistance in Escherichia coli. Adv Appl Microbiol 52, 167-186.
    • (2003) Adv Appl Microbiol , vol.52 , pp. 167-186
    • Richard, H.T.1    Foster, J.W.2
  • 25
    • 4444226939 scopus 로고    scopus 로고
    • Escherichia coli glutamate- and arginine-dependent acid resistance systems increase internal pH and reverse transmembrane potential
    • Richard, H. and Foster, J.W. (2004) Escherichia coli glutamate- and arginine-dependent acid resistance systems increase internal pH and reverse transmembrane potential. J Bacteriol 186, 6032-6041.
    • (2004) J Bacteriol , vol.186 , pp. 6032-6041
    • Richard, H.1    Foster, J.W.2
  • 26
    • 0029038513 scopus 로고
    • Nucleic acid related compounds. 86. Nucleophilic functionalization of adenine, adenosine, tubercidin, and formycin derivatives via elaboration of the heterocyclic amino group into a readily displaced 1,2,4-triazol-4-y1 substituent
    • Robert, W.M., Vicente, S. and Morris, J.R. (1995) Nucleic acid related compounds. 86. Nucleophilic functionalization of adenine, adenosine, tubercidin, and formycin derivatives via elaboration of the heterocyclic amino group into a readily displaced 1, 2, 4-triazol-4-y1 substituent. J Am Chem Soc 117, 5951-5957.
    • (1995) J Am Chem Soc , vol.117 , pp. 5951-5957
    • Robert, W.M.1    Vicente, S.2    Morris, J.R.3
  • 27
    • 0038508659 scopus 로고    scopus 로고
    • Peptide bond formation on the ribosome: structure and mechanism
    • Rodnina, M.V. and Wintermeyer, W. (2003) Peptide bond formation on the ribosome: structure and mechanism. Curr Opin Struct Biol 13, 334-340.
    • (2003) Curr Opin Struct Biol , vol.13 , pp. 334-340
    • Rodnina, M.V.1    Wintermeyer, W.2
  • 29
    • 20044396589 scopus 로고    scopus 로고
    • Carbon dioxide increases acid resistance in Escherichia coli
    • Sun, L., Fukamachi, T., Saito, H. and Kobayashi, H. (2005) Carbon dioxide increases acid resistance in Escherichia coli. Lett Appl Microbiol 40, 397-400.
    • (2005) Lett Appl Microbiol , vol.40 , pp. 397-400
    • Sun, L.1    Fukamachi, T.2    Saito, H.3    Kobayashi, H.4
  • 30
    • 79958076326 scopus 로고    scopus 로고
    • ATP requirement for acidic resistance in Escherichia coli
    • Sun, Y., Fukamachi, T., Saito, H. and Kobayashi, H. (2011) ATP requirement for acidic resistance in Escherichia coli. J Bacteriol 193, 3072-3077.
    • (2011) J Bacteriol , vol.193 , pp. 3072-3077
    • Sun, Y.1    Fukamachi, T.2    Saito, H.3    Kobayashi, H.4
  • 31
    • 77049313195 scopus 로고
    • Acetylornithinase of Escherichia coli: partial purification and some properties
    • Vogel, H.J. and Bonner, D.M. (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
  • 32
    • 0022356413 scopus 로고
    • Identification of functional murine adenosine deaminase cDNA clones by complementation in Escherichia coli
    • Yeung, C.Y., Ingolia, D.E., Roth, D.B., Shoemaker, C., Al-Ubaidi, M.R., Yen, J.Y., Ching, C., Bobonis, C. et al. (1985) Identification of functional murine adenosine deaminase cDNA clones by complementation in Escherichia coli. J Biol Chem 260, 10299-10307.
    • (1985) J Biol Chem , vol.260 , pp. 10299-10307
    • Yeung, C.Y.1    Ingolia, D.E.2    Roth, D.B.3    Shoemaker, C.4    Al-Ubaidi, M.R.5    Yen, J.Y.6    Ching, C.7    Bobonis, C.8


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