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Volumn 15, Issue 2, 2011, Pages 165-175

Comparative study on dihydrofolate reductases from Shewanella species living in deep-sea and ambient atmospheric-pressure environments

Author keywords

Deep sea; DHFR; High pressure; Molecular adaptation; Shewanella species

Indexed keywords

DIHYDROFOLATE REDUCTASE;

EID: 79952252302     PISSN: 14310651     EISSN: 14334909     Source Type: Journal    
DOI: 10.1007/s00792-010-0345-0     Document Type: Article
Times cited : (31)

References (37)
  • 1
    • 0030822053 scopus 로고    scopus 로고
    • Shewanella gelidimarina sp. nov. and Shewanella frigidimarina sp. nov., novel Antarctic species with the ability to produce eicosapentaenoic acid (20:5 omega 3) and grow anaerobically by dissimilatory Fe(III) reduction
    • Bowman JP, McCammon SA, Nichols DS, Skerratt JH, Rea SM, Nichols PD, McMeekin TA (1997) Shewanella gelidimarina sp. nov. and Shewanella frigidimarina sp. nov., novel Antarctic species with the ability to produce eicosapentaenoic acid (20: 5 omega 3) and grow anaerobically by dissimilatory Fe(III) reduction. Int J Syst Bacteriol 47: 1040-1047.
    • (1997) Int J Syst Bacteriol , vol.47 , pp. 1040-1047
    • Bowman, J.P.1    McCammon, S.A.2    Nichols, D.S.3    Skerratt, J.H.4    Rea, S.M.5    Nichols, P.D.6    McMeekin, T.A.7
  • 2
    • 0030988210 scopus 로고    scopus 로고
    • Isolation and characterization of the gene encoding single-stranded-DNA-binding protein (SSB) from four marine Shewanella strains that differ in their temperature and pressure optima for growth
    • Chilukuri LN, Bartlett DH (1997) Isolation and characterization of the gene encoding single-stranded-DNA-binding protein (SSB) from four marine Shewanella strains that differ in their temperature and pressure optima for growth. Microbiology 143: 1163-1174.
    • (1997) Microbiology , vol.143 , pp. 1163-1174
    • Chilukuri, L.N.1    Bartlett, D.H.2
  • 3
    • 0036783001 scopus 로고    scopus 로고
    • Comparison of high pressure-induced dissociation of single-stranded DNA-binding protein (SSB) from high pressure-sensitive and high pressure-adapted marine Shewanella species
    • Chilukuri LN, Bartlett DH, Fortes PAG (2002) Comparison of high pressure-induced dissociation of single-stranded DNA-binding protein (SSB) from high pressure-sensitive and high pressure-adapted marine Shewanella species. Extremophiles 6: 377-383.
    • (2002) Extremophiles , vol.6 , pp. 377-383
    • Chilukuri, L.N.1    Bartlett, D.H.2    Fortes, P.A.G.3
  • 5
    • 0030989775 scopus 로고    scopus 로고
    • Evolutionary relationships of cultivated psychrophilic and barophilic deep-sea bacteria
    • DeLong EF, Franks DG, Yayanos AA (1997) Evolutionary relationships of cultivated psychrophilic and barophilic deep-sea bacteria. Appl Environ Microbiol 63: 2105-2108.
    • (1997) Appl Environ Microbiol , vol.63 , pp. 2105-2108
    • Delong, E.F.1    Franks, D.G.2    Yayanos, A.A.3
  • 6
    • 0021200404 scopus 로고
    • The ribonucleotide sequence of 5s rRNA from two strains of deep-sea barophilic bacteria
    • Deming JW, Hada H, Colwell RR, Luehrsen KR, Fox GE (1984) The ribonucleotide sequence of 5s rRNA from two strains of deep-sea barophilic bacteria. J Gen Microbiol 130: 1911-1920.
    • (1984) J Gen Microbiol , vol.130 , pp. 1911-1920
    • Deming, J.W.1    Hada, H.2    Colwell, R.R.3    Luehrsen, K.R.4    Fox, G.E.5
  • 7
    • 0023668190 scopus 로고
    • Construction and evaluation of the kinetic scheme associated with dihydrofolate reductase from Escherichia coli
    • Fierke CA, Johnson KA, Benkovic SJ (1987) Construction and evaluation of the kinetic scheme associated with dihydrofolate reductase from Escherichia coli. Biochemistry 26: 4085-4092.
    • (1987) Biochemistry , vol.26 , pp. 4085-4092
    • Fierke, C.A.1    Johnson, K.A.2    Benkovic, S.J.3
  • 8
    • 0027998347 scopus 로고
    • Point mutations at glycine-121 of Escherichia coli dihydrofolate reductase: important roles of a flexible loop in the stability and function
    • Gekko K, Kunori Y, Takeuchi H, Ichihara S, Kodama M, Iwakura M (1994) Point mutations at glycine-121 of Escherichia coli dihydrofolate reductase: important roles of a flexible loop in the stability and function. J Biochem 116: 703-710.
    • (1994) J Biochem , vol.116 , pp. 703-710
    • Gekko, K.1    Kunori, Y.2    Takeuchi, H.3    Ichihara, S.4    Kodama, M.5    Iwakura, M.6
  • 10
    • 0035060886 scopus 로고    scopus 로고
    • Correlation between phylogenetic structure and function: examples from deep-sea Shewanella
    • Kato C, Nogi Y (2001) Correlation between phylogenetic structure and function: examples from deep-sea Shewanella. FEMS Microbiol Ecol 35: 223-230.
    • (2001) FEMS Microbiol Ecol , vol.35 , pp. 223-230
    • Kato, C.1    Nogi, Y.2
  • 11
    • 0028976429 scopus 로고
    • Isolation and properties of barophilic and barotolerant bacteria from deep-sea mud samples
    • Kato C, Sato T, Horikoshi K (1995) Isolation and properties of barophilic and barotolerant bacteria from deep-sea mud samples. Biodivers Conserv 4: 1-9.
    • (1995) Biodivers Conserv , vol.4 , pp. 1-9
    • Kato, C.1    Sato, T.2    Horikoshi, K.3
  • 12
    • 0031980181 scopus 로고    scopus 로고
    • Extremely barophilic bacteria isolated from the Mariana Trench, Challenger Deep, at a depth of 11, 000 meters
    • Kato C, Li L, Nogi Y, Nakamura Y, Tamaoka J, Horikoshi K (1998) Extremely barophilic bacteria isolated from the Mariana Trench, Challenger Deep, at a depth of 11, 000 meters. Appl Environ Microbiol 64: 1510-1513.
    • (1998) Appl Environ Microbiol , vol.64 , pp. 1510-1513
    • Kato, C.1    Li, L.2    Nogi, Y.3    Nakamura, Y.4    Tamaoka, J.5    Horikoshi, K.6
  • 13
    • 23944518876 scopus 로고    scopus 로고
    • Structure and hydride transfer mechanism of a moderate thermophilic dihydrofolate reductase from Bacillus stearothermophilus and comparison to its mesophilic and hyperthermophilic homologues
    • Kim HS, Damo SM, Lee SY, Wemmer D, Klinman JP (2005) Structure and hydride transfer mechanism of a moderate thermophilic dihydrofolate reductase from Bacillus stearothermophilus and comparison to its mesophilic and hyperthermophilic homologues. Biochemistry 44: 11428-11439.
    • (2005) Biochemistry , vol.44 , pp. 11428-11439
    • Kim, H.S.1    Damo, S.M.2    Lee, S.Y.3    Wemmer, D.4    Klinman, J.P.5
  • 14
    • 0034711091 scopus 로고    scopus 로고
    • High pressure NMR reveals active-site hinge motion of folate-bound Escherichia coli dihydrofolate reductase
    • Kitahara R, Sareth S, Yamada H, Ohmae E, Gekko K, Akasaka K (2000) High pressure NMR reveals active-site hinge motion of folate-bound Escherichia coli dihydrofolate reductase. Biochemistry 39: 12789-12795.
    • (2000) Biochemistry , vol.39 , pp. 12789-12795
    • Kitahara, R.1    Sareth, S.2    Yamada, H.3    Ohmae, E.4    Gekko, K.5    Akasaka, K.6
  • 15
    • 0026005997 scopus 로고
    • Transient intermediates in the folding of dihydrofolate reductase as detected by far-ultraviolet circular dichroism spectroscopy
    • Kuwajima K, Garvey EP, Finn BE, Matthews CR, Sugai S (1991) Transient intermediates in the folding of dihydrofolate reductase as detected by far-ultraviolet circular dichroism spectroscopy. Biochemistry 30: 7693-7703.
    • (1991) Biochemistry , vol.30 , pp. 7693-7703
    • Kuwajima, K.1    Garvey, E.P.2    Finn, B.E.3    Matthews, C.R.4    Sugai, S.5
  • 16
    • 67649610422 scopus 로고    scopus 로고
    • Effect of dimerization on the stability and catalytic activity of dihydrofolate reductase from the hyperthermophile Thermotoga maritime
    • Loveridge EJ, Rodriguez RJ, Swanwick RS, Allemann RK (2009) Effect of dimerization on the stability and catalytic activity of dihydrofolate reductase from the hyperthermophile Thermotoga maritime. Biochemistry 48: 5922-5933.
    • (2009) Biochemistry , vol.48 , pp. 5922-5933
    • Loveridge, E.J.1    Rodriguez, R.J.2    Swanwick, R.S.3    Allemann, R.K.4
  • 17
    • 0022379297 scopus 로고
    • Phylogeny of the Vibrionaceae, and recommendation for two new genera, Listonella and Shewanella
    • MacDonell MT, Colwell RR (1985) Phylogeny of the Vibrionaceae, and recommendation for two new genera, Listonella and Shewanella. Syst Appl Microbiol 6: 171-182.
    • (1985) Syst Appl Microbiol , vol.6 , pp. 171-182
    • Macdonell, M.T.1    Colwell, R.R.2
  • 18
    • 77950611018 scopus 로고    scopus 로고
    • Cloning and characterization of dihydrofolate reductases from deep-sea bacteria
    • Murakami C, Ohmae E, Tate S, Gekko K, Nakasone K, Kato C (2010) Cloning and characterization of dihydrofolate reductases from deep-sea bacteria. J Biochem 147: 591-595.
    • (2010) J Biochem , vol.147 , pp. 591-595
    • Murakami, C.1    Ohmae, E.2    Tate, S.3    Gekko, K.4    Nakasone, K.5    Kato, C.6
  • 19
    • 0031670034 scopus 로고    scopus 로고
    • Taxonomic studies of deep-sea barophilic Shewanella strains and description of Shewanella violacea sp nov., a new balophilic bacterial species
    • Nogi Y, Kato C, Horikoshi K (1998) Taxonomic studies of deep-sea barophilic Shewanella strains and description of Shewanella violacea sp nov., a new balophilic bacterial species. Arch Microbiol 170: 331-338.
    • (1998) Arch Microbiol , vol.170 , pp. 331-338
    • Nogi, Y.1    Kato, C.2    Horikoshi, K.3
  • 20
    • 0036740457 scopus 로고    scopus 로고
    • Psychromonas kaikoae sp nov., a novel from the deepest piezophilic bacterium cold-seep sediments in the Japan Trench
    • Nogi Y, Kato C, Horikoshi K (2002) Psychromonas kaikoae sp nov., a novel from the deepest piezophilic bacterium cold-seep sediments in the Japan Trench. Int J Syst Evol Microbiol 52: 1527-1532.
    • (2002) Int J Syst Evol Microbiol , vol.52 , pp. 1527-1532
    • Nogi, Y.1    Kato, C.2    Horikoshi, K.3
  • 21
    • 0029939820 scopus 로고    scopus 로고
    • Effects of point mutations at the flexible loop glycine-67 of Escherichia coli dihydrofolate reductase on its stability and function
    • Ohmae E, Iriyama K, Ichihara S, Gekko K (1996) Effects of point mutations at the flexible loop glycine-67 of Escherichia coli dihydrofolate reductase on its stability and function. J Biochem 119: 946-953.
    • (1996) J Biochem , vol.119 , pp. 946-953
    • Ohmae, E.1    Iriyama, K.2    Ichihara, S.3    Gekko, K.4
  • 22
    • 0034848452 scopus 로고    scopus 로고
    • Effects of five-tryptophan mutations on structure and function of Escherichia coli dihydrofolate reductase
    • Ohmae E, Sasaki Y, Gekko K (2001) Effects of five-tryptophan mutations on structure and function of Escherichia coli dihydrofolate reductase. J Biochem 130: 439-447.
    • (2001) J Biochem , vol.130 , pp. 439-447
    • Ohmae, E.1    Sasaki, Y.2    Gekko, K.3
  • 23
    • 4644368825 scopus 로고    scopus 로고
    • Pressure-dependent activity of dihydrofolate reductase from a deep-sea bacterium Shewanella violacea strain DSS12
    • Ohmae E, Kubota K, Nakasone K, Kato C, Gekko K (2004) Pressure-dependent activity of dihydrofolate reductase from a deep-sea bacterium Shewanella violacea strain DSS12. Chem Lett 33: 798-799.
    • (2004) Chem Lett , vol.33 , pp. 798-799
    • Ohmae, E.1    Kubota, K.2    Nakasone, K.3    Kato, C.4    Gekko, K.5
  • 24
    • 21044447962 scopus 로고    scopus 로고
    • Effects of mutation at methionine-42 of Escherichia coli dihydrofolate reductase on stability and function: implication of hydrophobic interactions
    • Ohmae E, Fukumizu Y, Iwakura M, Gekko K (2005) Effects of mutation at methionine-42 of Escherichia coli dihydrofolate reductase on stability and function: implication of hydrophobic interactions. J Biochem 137: 643-652.
    • (2005) J Biochem , vol.137 , pp. 643-652
    • Ohmae, E.1    Fukumizu, Y.2    Iwakura, M.3    Gekko, K.4
  • 26
    • 0017927715 scopus 로고
    • Base composition, size and sequence similarities of genoma deoxyribonucleic acids from clinical isolates of Pseudomonas putrefaciens
    • Owen RJ, Legors RM, Lapage SP (1978) Base composition, size and sequence similarities of genoma deoxyribonucleic acids from clinical isolates of Pseudomonas putrefaciens. J Gen Microbiol 104: 127-138.
    • (1978) J Gen Microbiol , vol.104 , pp. 127-138
    • Owen, R.J.1    Legors, R.M.2    Lapage, S.P.3
  • 27
    • 0022555885 scopus 로고
    • Determination and analysis of urea and guanidine hydrochloride denaturation curves
    • C. H. W. Hirs and S. N. Timasheff (Eds.), New York: Academic Press
    • Pace CN (1985) Determination and analysis of urea and guanidine hydrochloride denaturation curves. In: Hirs CHW, Timasheff SN (eds) Methods in enzymology vol 131. Academic Press, New York, pp 267-280.
    • (1985) Methods in Enzymology Vol 131 , pp. 267-280
    • Pace, C.N.1
  • 28
    • 0021872251 scopus 로고
    • Substrate-induced hysteresis in the activity of Escherichia coli dihydrofolate reductase
    • Penner MH, Frieden C (1985) Substrate-induced hysteresis in the activity of Escherichia coli dihydrofolate reductase. J Biol Chem 260: 5366-5369.
    • (1985) J Biol Chem , vol.260 , pp. 5366-5369
    • Penner, M.H.1    Frieden, C.2
  • 29
    • 33846137707 scopus 로고    scopus 로고
    • Cloning and characterization of dihydrofolate reductase from a facultative alkaliphilic and halotolerant bacillus strain
    • Redecke L, Brehm MA, Bredehorst R (2007) Cloning and characterization of dihydrofolate reductase from a facultative alkaliphilic and halotolerant bacillus strain. Extremophiles 11: 75-83.
    • (2007) Extremophiles , vol.11 , pp. 75-83
    • Redecke, L.1    Brehm, M.A.2    Bredehorst, R.3
  • 30
    • 0020466628 scopus 로고
    • Kinetic mechanism of the reaction catalyzed by dihydrofolate reductase from Escherichia coli
    • Stone SR, Morrison JF (1982) Kinetic mechanism of the reaction catalyzed by dihydrofolate reductase from Escherichia coli. Biochemistry 21: 3757-3765.
    • (1982) Biochemistry , vol.21 , pp. 3757-3765
    • Stone, S.R.1    Morrison, J.F.2
  • 31
    • 0027968068 scopus 로고
    • CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson JD, Higgins DG, Gibson TJ (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 22: 4673-4680.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 32
    • 0023055739 scopus 로고
    • Folding of dihydrofolate reductase from Escherichia coli
    • Touchette NA, Perry KM, Matthews CR (1986) Folding of dihydrofolate reductase from Escherichia coli. Biochemistry 25: 5445-5452.
    • (1986) Biochemistry , vol.25 , pp. 5445-5452
    • Touchette, N.A.1    Perry, K.M.2    Matthews, C.R.3
  • 34
    • 0031837399 scopus 로고    scopus 로고
    • Determination of the volume changes for pressure-induced transitions of apomyoglobin between the native, molten globule, and unfolded states
    • Vidugiris GJA, Royer CA (1998) Determination of the volume changes for pressure-induced transitions of apomyoglobin between the native, molten globule, and unfolded states. Biophys J 75: 463-470.
    • (1998) Biophys J , vol.75 , pp. 463-470
    • Vidugiris, G.J.A.1    Royer, C.A.2
  • 35
    • 0018759051 scopus 로고
    • Methotrexate, a high-affinity pseudosubstrate of dihydrofolate reductase
    • Williams JW, Morrison JF, Duggleby RG (1979) Methotrexate, a high-affinity pseudosubstrate of dihydrofolate reductase. Biochemistry 18: 2567-2573.
    • (1979) Biochemistry , vol.18 , pp. 2567-2573
    • Williams, J.W.1    Morrison, J.F.2    Duggleby, R.G.3
  • 36
    • 0036408309 scopus 로고    scopus 로고
    • The effect of salts on the activity and stability of Escherichia coli and Haloferax volcanii dihydrofolate reductases
    • Wright DB, Banks DD, Lohman JR, Hilsenbeck JL, Gloss LM (2002) The effect of salts on the activity and stability of Escherichia coli and Haloferax volcanii dihydrofolate reductases. J Mol Biol 323: 327-344.
    • (2002) J Mol Biol , vol.323 , pp. 327-344
    • Wright, D.B.1    Banks, D.D.2    Lohman, J.R.3    Hilsenbeck, J.L.4    Gloss, L.M.5
  • 37
    • 0042337202 scopus 로고    scopus 로고
    • Moritella cold-active dihydrofolate reductase: are there natural limits to optimization of catalytic efficiency at low temperature?
    • Xu Y, Feller G, Gerday C, Glansdorff N (2003) Moritella cold-active dihydrofolate reductase: are there natural limits to optimization of catalytic efficiency at low temperature? J Bacteriol 185: 5519-5526.
    • (2003) J Bacteriol , vol.185 , pp. 5519-5526
    • Xu, Y.1    Feller, G.2    Gerday, C.3    Glansdorff, N.4


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