메뉴 건너뛰기




Volumn 147, Issue 4, 2010, Pages 591-599

Cloning and characterization of dihydrofolate reductases from deep-sea bacteria

Author keywords

Deep sea bacteria; Dihydrofolate reductase; Enzyme activity; High pressure adaptation; Molecular evolution

Indexed keywords

DIHYDROFOLATE REDUCTASE;

EID: 77950611018     PISSN: 0021924X     EISSN: 17562651     Source Type: Journal    
DOI: 10.1093/jb/mvp206     Document Type: Article
Times cited : (29)

References (44)
  • 1
    • 0018677154 scopus 로고
    • Isolation of a deep-sea barophilic bacterium and some of its growth characteristics
    • Yayanos, A.A., Dietz, A.S., and Van Boxtel, R. (1979) Isolation of a deep-sea barophilic bacterium and some of its growth characteristics. Science 205, 805-810
    • (1979) Science , vol.205 , pp. 805-810
    • Yayanos, A.A.1    Dietz, A.S.2    Van Boxtel, R.3
  • 2
    • 0028976429 scopus 로고
    • Isolation and properties of barophilic and barotolerant bacteria from deep-sea mud samples
    • Kato, C., Sato, T., and Horikoshi, K. (1995) Isolation and properties of barophilic and barotolerant bacteria from deep-sea mud samples. Biodiversity and Conservation 4, 1-9
    • (1995) Biodiversity and Conservation , vol.4 , pp. 1-9
    • Kato, C.1    Sato, T.2    Horikoshi, K.3
  • 3
    • 0031670034 scopus 로고    scopus 로고
    • Taxonomic studies of deep-sea barophilic shewanella strains and description of shewanella violacea sp. nov
    • Nogi, Y., Kato, C., and Horikoshi, K. (1998) Taxonomic studies of deep-sea barophilic Shewanella strains and description of Shewanella violacea sp. nov. Arch. Microbiol. 170, 331-338
    • (1998) Arch. Microbiol , vol.170 , pp. 331-338
    • Nogi, Y.1    Kato, C.2    Horikoshi, K.3
  • 4
    • 0036545609 scopus 로고    scopus 로고
    • Transcriptional regulation under pressure conditions by RNA polymerase sigma54 factor with a two-component regulatory system in shewanella violacea
    • Nakasone, K., Ikegami, A., Kawano, H., Kato, C., Usami, R., and Horikoshi, K. (2002) Transcriptional regulation under pressure conditions by RNA polymerase sigma54 factor with a two-component regulatory system in Shewanella violacea. Extremophiles 6, 89-95
    • (2002) Extremophiles , vol.6 , pp. 89-95
    • Nakasone, K.1    Ikegami, A.2    Kawano, H.3    Kato, C.4    Usami, R.5    Horikoshi, K.6
  • 5
    • 0035287703 scopus 로고    scopus 로고
    • Piezoresponse of the cyooperon coding for quinol oxidase subunits in a deep-sea piezophilic bacterium, shewanella violacea
    • Nakasone, K., Yamada, M., Qureshi, M.H., Kato, C., and Horikoshi, K. (2001) Piezoresponse of the cyooperon coding for quinol oxidase subunits in a deep-sea piezophilic bacterium, Shewanella violacea. Biosci. Biotechnol. Biochem. 65, 699-693
    • (2001) Biosci. Biotechnol. Biochem. , vol.65 , pp. 699-693
    • Nakasone, K.1    Yamada, M.2    Qureshi, M.H.3    Kato, C.4    Horikoshi, K.5
  • 6
    • 21744460518 scopus 로고    scopus 로고
    • Pressure-regulated biosynthesis of cytochrome bd in piezo- and psychrophilic deep-sea bacterium Shewanella violacea DSS12
    • Tamegai, H., Kawano, H., Ishii, A., Chikuma, S., Nakasone, K., and Kato, C. (2005) Pressure-regulated biosynthesis of cytochrome bd in piezo- and psychrophilic deep-sea bacterium Shewanella violacea DSS12. Extremophiles 9, 247-253
    • (2005) Extremophiles , vol.9 , pp. 247-253
    • Tamegai, H.1    Kawano, H.2    Ishii, A.3    Chikuma, S.4    Nakasone, K.5    Kato, C.6
  • 7
    • 33846050009 scopus 로고    scopus 로고
    • Bacterial adaptation to high pressure: A respiratory system in the deep-sea bacterium Shewanella violacea DSS12
    • Chikuma, S., Kasahara, R., Kato, C., and Tamegai, H. (2007) Bacterial adaptation to high pressure: a respiratory system in the deep-sea bacterium Shewanella violacea DSS12. FEMS Microbiol. Lett. 267, 105-112
    • (2007) FEMS Microbiol. Lett. , vol.267 , pp. 105-112
    • Chikuma, S.1    Kasahara, R.2    Kato, C.3    Tamegai, H.4
  • 8
    • 8744233998 scopus 로고    scopus 로고
    • Differential pressure resistance in the activity of RNA polymerase isolated from shewanella violacea and escherichia coli
    • Kawano, H., Nakasone, K., Matsumoto, M., Yoshida, Y., Usami, R., Kato, C., and Abe, F. (2004) Differential pressure resistance in the activity of RNA polymerase isolated from Shewanella violacea and Escherichia coli. Extremophiles 8, 367-375
    • (2004) Extremophiles , vol.8 , pp. 367-375
    • Kawano, H.1    Nakasone, K.2    Matsumoto, M.3    Yoshida, Y.4    Usami, R.5    Kato, C.6    Abe, F.7
  • 9
    • 17844370299 scopus 로고    scopus 로고
    • Identification of rpoBC genes encoding for βand β′ subunits of RNA polymerase in a deep-sea piezophilic bacterium, Shewanella violacea strain DSS12
    • DOI 10.1271/bbb.69.575
    • Kawano, H., Nakasone, K., Abe, F., Kato, C., Yoshida, Y., Usami, R., and Horikoshi, K. (2005) Identification of rpoBC genes encoding for beta and beta' subunits of RNA polymerase in a deep-sea piezophilic bacterium, Shewanella violacea strain DSS12. Biosci. Biotechnol. Biochem. 69, 575-582 (Pubitemid 40589118)
    • (2005) Bioscience, Biotechnology and Biochemistry , vol.69 , Issue.3 , pp. 575-582
    • Kawano, H.1    Nakasone, K.2    Abe, F.3    Kato, C.4    Yoshida, Y.5    Usami, R.6    Horikoshi, K.7
  • 10
    • 0024981678 scopus 로고
    • Isolation of a gene regulated by hydrostatic pressure in a deep-sea bacterium
    • Bartlett, D., Wright, M., Yayanos, A.A., and Silverman, M. (1989) Isolation of a gene regulated by hydrostatic pressure in a deep-sea bacterium. Nature 342, 572-574
    • (1989) Nature , vol.342 , pp. 572-574
    • Bartlett, D.1    Wright, M.2    Yayanos, A.A.3    Silverman, M.4
  • 11
    • 0027220616 scopus 로고
    • Sequence of the ompH gene from the deep-sea bacterium photobacterium SS9
    • Bartlett, D.H., Chi, E., and Wright, M.E. (1993) Sequence of the ompH gene from the deep-sea bacterium Photobacterium SS9. Gene 131, 125-128
    • (1993) Gene , vol.131 , pp. 125-128
    • Bartlett, D.H.1    Chi, E.2    Wright, M.E.3
  • 12
    • 0028895181 scopus 로고
    • High pressure influences on gene and protein expression
    • Bartlett, D.H., Kato, C., and Horikoshi, K. (1995) High pressure influences on gene and protein expression. Res. Microbiol. 146, 697-706
    • (1995) Res. Microbiol. , vol.146 , pp. 697-706
    • Bartlett, D.H.1    Kato, C.2    Horikoshi, K.3
  • 13
    • 0030989775 scopus 로고    scopus 로고
    • Evolutionary relationships of cultivated psychrophilic and barophilic deep-sea bacteria
    • Delong, E.F., Franks, D.G., and Yayanos, A.A. (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
  • 14
    • 0037171156 scopus 로고    scopus 로고
    • Pressure effects on in vivo microbial processes
    • Bartlett, D.H. (2002) Pressure effects on in vivo microbial processes. Biochim. Biophys. Acta 1595, 367-381
    • (2002) Biochim. Biophys. Acta , vol.1595 , pp. 367-381
    • Bartlett, D.H.1
  • 15
    • 0027436748 scopus 로고
    • Use of a reporter gene to follow high-pressure signal transduction in the deep-sea bacterium photobacterium sp. strain S9
    • Chi, E. and Bartlett, D.H. (1993) Use of a reporter gene to follow high-pressure signal transduction in the deep-sea bacterium Photobacterium sp. strain SS9. J. Bacteriol. 175, 7533-7540
    • (1993) J. Bacteriol , vol.175 , pp. 7533-7540
    • Chi, E.1    Bartlett, D.H.2
  • 16
    • 0029048335 scopus 로고
    • An rpoE-like locus controls outer membrane protein synthesis and growth at cold temperatures and high pressures in the deep-sea bacterium Photobacterium sp. strain SS9
    • Chi, E. and Bartlett, D.H. (1995) An rpoE-like locus controls outer membrane protein synthesis and growth at cold temperatures and high pressures in the deep-sea bacterium Photobacterium sp. strain SS9. Mol. Microbiol. 17, 713-726
    • (1995) Mol. Microbiol , vol.17 , pp. 713-726
    • Chi, E.1    Bartlett, D.H.2
  • 17
    • 0028831045 scopus 로고
    • OmpH gene expression is regulated by multiple environmental cues in addition to high pressure in the deep-sea bacterium Photobacterium species strain SS9
    • Bartlett, D.H. and Welch, T.J. (1995) ompH gene expression is regulated by multiple environmental cues in addition to high pressure in the deep-sea bacterium Photobacterium species strain SS9. J. Bacteriol. 177, 1005-1016
    • (1995) J. Bacteriol , vol.177 , pp. 1005-1016
    • Bartlett, D.H.1    Welch, T.J.2
  • 18
    • 0031779823 scopus 로고    scopus 로고
    • Identification of a regulatory protein required for pressure-responsive gene expression in the deep-sea bacterium Photobacterium species strain SS9
    • Welch, T.J. and Bartlett, D.H. (1998) Identification of a regulatory protein required for pressure-responsive gene expression in the deep-sea bacterium Photobacterium species strain SS9. Mol. Microbiol. 27, 977-985
    • (1998) Mol. Microbiol , vol.27 , pp. 977-985
    • Welch, T.J.1    Bartlett, D.H.2
  • 20
    • 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., and Horikoshi, K. (1998) Extremely barophilic bacteria isolated from the Mariana Trench, Challenger Deep, at a depth of 11,000 meters. Appl. Environ. Microbiol. 64, 1519-1513
    • (1998) Appl. Environ. Microbiol , vol.64 , pp. 1519-1513
    • Kato, C.1    Li, L.2    Nogi, Y.3    Nakamura, Y.4    Tamaoka, J.5    Horikoshi, K.6
  • 21
    • 0032982459 scopus 로고    scopus 로고
    • Taxonomic studies of extremely barophilic bacteria isolated from the Mariana Trench and description of Moritella yayanosii sp. nov., a new barophilic bacterial isolate
    • Nogi, Y. and Kato, C. (1999) Taxonomic studies of extremely barophilic bacteria isolated from the Mariana Trench and description of Moritella yayanosii sp. nov., a new barophilic bacterial isolate. Extremophiles 3, 71-77
    • (1999) Extremophiles , vol.3 , pp. 71-77
    • Nogi, Y.1    Kato, C.2
  • 22
    • 0031796801 scopus 로고    scopus 로고
    • Moritella japonica sp. nov. a novel barophilic bacterium isolated from a Japan Trench sediment
    • Nogi, Y., Kato, C., and Horikoshi, K. (1998) Moritella japonica sp. nov. a novel barophilic bacterium isolated from a Japan Trench sediment. J Gen. Appl. Microbiol 44, 289-295
    • (1998) J Gen. Appl. Microbiol , vol.44 , pp. 289-295
    • Nogi, Y.1    Kato, C.2    Horikoshi, K.3
  • 24
    • 33645690725 scopus 로고    scopus 로고
    • Amino acid substitutions in malate dehydrogenases of piezophilic bacteria isolated from intestinal contents of deep-sea fishes retrieved from the abyssal zone
    • Saito, R., Kato, C., and Nakayama, A. (2006) Amino acid substitutions in malate dehydrogenases of piezophilic bacteria isolated from intestinal contents of deep-sea fishes retrieved from the abyssal zone. J. Gen. Appl. Microbiol. 52, 9-19
    • (2006) J. Gen. Appl. Microbiol , vol.52 , pp. 9-19
    • Saito, R.1    Kato, C.2    Nakayama, A.3
  • 25
    • 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., and 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
  • 26
    • 52449135534 scopus 로고    scopus 로고
    • Effects of pressure on enzyme function of Escherichia coli dihydrofolate reductase
    • Ohmae, E., Tatsuta, M., Abe, F., Kato, C., Tanaka, N., Kunugi, S., and Gekko, K. (2008) Effects of pressure on enzyme function of Escherichia coli dihydrofolate reductase. Biochim. Biophys. Acta 1784, 1115-1121
    • (2008) Biochim. Biophys. Acta , vol.1784 , pp. 1115-1121
    • Ohmae, E.1    Tatsuta, M.2    Abe, F.3    Kato, C.4    Tanaka, N.5    Kunugi, S.6    Gekko, K.7
  • 27
    • 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., and Gekko, K. (2004) Pressure-dependent activity of dihydrofolate reductase from a deep-sea bacterium Shewanella violacea strain DSS12. Chem. Lett. 33, 795-799
    • (2004) Chem. Lett. , vol.33 , pp. 795-799
    • Ohmae, E.1    Kubota, K.2    Nakasone, K.3    Kato, C.4    Gekko, K.5
  • 28
    • 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., and 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
  • 29
    • 0023668190 scopus 로고
    • Construction and evaluation of the kinetic scheme associated with dihydrofolate reductase from Escherichia coli
    • Fierke, C.A., Johnson, K.A., and Benkovic, S.J. (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
  • 31
    • 0021872251 scopus 로고
    • Substrate-induced hysteresis in the activity of Escherichia coli dihydrofolate reductase
    • Penner, M.H. and 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
  • 32
    • 0020466628 scopus 로고
    • Kinetic mechanism of the reaction catalyzed by dihydrofolate reductase from Escherichia coli
    • Stone, S.R. and Morrison, J.F. (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
  • 33
    • 0018759051 scopus 로고
    • Methotrexate, a high-affinity pseudosubstrate of dihydrofolate reductase
    • Williams, J.W., Morrison, J.F., and Duggleby, R.G. (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
  • 34
    • 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., and 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
  • 35
    • 0034848452 scopus 로고    scopus 로고
    • Effects of five-tryptophan mutations on structure and function of Escherichia coli dihydrofolate reductase
    • Ohmae, E., Sasaki, Y., and 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
  • 36
    • 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., and 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
  • 37
    • 0026005997 scopus 로고
    • Transient intermediates in the folding of dihydrofolate reductase as detected by far-ultraviolet circular dichroism spectroscopy
    • Kuwajima, K., Garvey, E.P., Finn, B.E., Matthews, C.R., and 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
  • 38
    • 0037453227 scopus 로고    scopus 로고
    • Testing the relationship between foldability and the early folding events of dihydrofolate reductase from Escherichia coli
    • Arai, M., Maki, K., Takahashi, H., and Iwakura, M. (2003) Testing the relationship between foldability and the early folding events of dihydrofolate reductase from Escherichia coli. J. Mol. Biol. 328, 273-288
    • (2003) J. Mol. Biol. , vol.328 , pp. 273-288
    • Arai, M.1    Maki, K.2    Takahashi, H.3    Iwakura, M.4
  • 39
    • 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., and 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
  • 41
    • 0022546047 scopus 로고
    • Functional role of aspartic acid-27 in dihydrofolate reductase revealed by mutagenesis
    • Howell, E.E., Villafranca, J.E., Warren, M.S., Oatley, S.J., and Kraut, J. (1986) Functional role of aspartic acid-27 in dihydrofolate reductase revealed by mutagenesis. Science 231, 1123-1128
    • (1986) Science , vol.231 , pp. 1123-1128
    • Howell, E.E.1    Villafranca, J.E.2    Warren, M.S.3    Oatley, S.J.4    Kraut, J.5
  • 42
    • 0031443372 scopus 로고    scopus 로고
    • Evidence for a functional role of the dynamics of glycine-121 of Escherichia coli dihydrofolate reductase obtained from kinetic analysis of a site-directed mutant
    • Cameron, C.E. and Benkovic, S.J. (1997) Evidence for a functional role of the dynamics of glycine-121 of Escherichia coli dihydrofolate reductase obtained from kinetic analysis of a site-directed mutant. Biochemistry 36, 15792-15800
    • (1997) Biochemistry , vol.36 , pp. 15792-15800
    • Cameron, C.E.1    Benkovic, S.J.2
  • 43
    • 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, J.D., Higgins, D.G., and Gibson, T.J. (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
  • 44
    • 0025270551 scopus 로고
    • Crystal structure of Escherichia coli dihydrofolate reductase: The NADP+ holoenzyme and the folate-NADP+ ternary complex. Substrate binding and a model for the transition state
    • Bystroff, C., Oatley, S.J., and Kraut, J. (1990) Crystal structure of Escherichia coli dihydrofolate reductase: The NADP+ holoenzyme and the folate-NADP+ ternary complex. Substrate binding and a model for the transition state. Biochemistry 29, 3263-3277
    • (1990) Biochemistry , vol.29 , pp. 3263-3277
    • Bystroff, C.1    Oatley, S.J.2    Kraut, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.