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Volumn 6, Issue 5, 2002, Pages 377-383

Comparison of high pressure-induced dissociation of single-stranded DNA-binding protein (SSB) from high pressure-sensitive and high pressure-adapted marine Shewanella species

Author keywords

Piezoadaptation; Piezophile; Pressure; Protein adaptation; Shewanella; Single stranded DNA binding protein; SSB

Indexed keywords

BACTERIA (MICROORGANISMS); SHEWANELLA; SHEWANELLA HANEDAI;

EID: 0036783001     PISSN: 14310651     EISSN: 14334909     Source Type: Journal    
DOI: 10.1007/s00792-002-0267-6     Document Type: Article
Times cited : (21)

References (40)
  • 1
    • 0026078480 scopus 로고
    • Monomer-tetramer equilibrium of the Escherichia coli ssb-1 mutant single strand binding protein
    • Bujalowski W, Lohman TM (1991) Monomer-tetramer equilibrium of the Escherichia coli ssb-1 mutant single strand binding protein. J Biol Chem 266:1616-1626
    • (1991) J Biol Chem , vol.266 , pp. 1616-1626
    • Bujalowski, W.1    Lohman, T.M.2
  • 2
    • 0030788344 scopus 로고    scopus 로고
    • Pressure-induced dissociation of yeast glyceraldehyde-3-phosphate dehydrogenase: Heterogeneous kinetics and perturbations of subunit structure
    • Cioni P, Strambini GB (1997) Pressure-induced dissociation of yeast glyceraldehyde-3-phosphate dehydrogenase: heterogeneous kinetics and perturbations of subunit structure. Biochemistry 36:8586-8593
    • (1997) Biochemistry , vol.36 , pp. 8586-8593
    • Cioni, P.1    Strambini, G.B.2
  • 3
    • 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
  • 4
    • 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
  • 5
    • 0028168288 scopus 로고
    • The single-stranded-DNA-binding proteins (SSB) of Proteus mirabilis and Serratia marcescens
    • DeVries J, Genschel J, Urbanke C, Thole H, Wackernagel W (1994) The single-stranded-DNA-binding proteins (SSB) of Proteus mirabilis and Serratia marcescens. Eur J Biochem 224:613-622
    • (1994) Eur J Biochem , vol.224 , pp. 613-622
    • DeVries, J.1    Genschel, J.2    Urbanke, C.3    Thole, H.4    Wackernagel, W.5
  • 6
    • 0025845307 scopus 로고
    • Oligomeric protein associations: Transition from stochastic to deterministic equilibrium
    • Erijman L, Weber G (1991) Oligomeric protein associations: transition from stochastic to deterministic equilibrium. Biochemistry 30:1595-1599
    • (1991) Biochemistry , vol.30 , pp. 1595-1599
    • Erijman, L.1    Weber, G.2
  • 7
    • 0033580633 scopus 로고    scopus 로고
    • Structural characterization of lactate dehydrogenase dissociation under high pressure studied by synchrotron high-pressure small-angle X-ray scattering
    • Fujisawa T, Kato M, Inoko Y (1999) Structural characterization of lactate dehydrogenase dissociation under high pressure studied by synchrotron high-pressure small-angle X-ray scattering. Biochemistry 38:6411-6418
    • (1999) Biochemistry , vol.38 , pp. 6411-6418
    • Fujisawa, T.1    Kato, M.2    Inoko, Y.3
  • 8
    • 0030571525 scopus 로고    scopus 로고
    • Isolation, sequencing and overproduction of the single-stranded DNA binding protein from Pseudomonas aeruginosa PAO
    • Genschel J, Litz L, Thole H, Roemling U, Urbanke C (1996) Isolation, sequencing and overproduction of the single-stranded DNA binding protein from Pseudomonas aeruginosa PAO. Gene 182:137-143
    • (1996) Gene , vol.182 , pp. 137-143
    • Genschel, J.1    Litz, L.2    Thole, H.3    Roemling, U.4    Urbanke, C.5
  • 9
    • 0024673478 scopus 로고
    • +-ATPase in gills of marine teleosts
    • +-ATPase in gills of marine teleosts. J Exp Biol 143:475-492
    • (1989) J Exp Biol , vol.143 , pp. 475-492
    • Gibbs, A.1    Somero, G.N.2
  • 10
    • 0028220701 scopus 로고
    • Proteins under pressure: The influence of high hydrostatic pressure on structure, function and assembly of proteins and protein complexes
    • Gross M, Jaenicke R (1994) Proteins under pressure: the influence of high hydrostatic pressure on structure, function and assembly of proteins and protein complexes. Eur J Biochem 221:617-630
    • (1994) Eur J Biochem , vol.221 , pp. 617-630
    • Gross, M.1    Jaenicke, R.2
  • 11
    • 0028217082 scopus 로고
    • Pressure stabilization of proteins from extreme thermophiles
    • Hei DJ, Clark DS (1994) Pressure stabilization of proteins from extreme thermophiles. Appl Environ Microbiol 60:932-939
    • (1994) Appl Environ Microbiol , vol.60 , pp. 932-939
    • Hei, D.J.1    Clark, D.S.2
  • 12
    • 0022212241 scopus 로고
    • Pressure inactivation of tetrameric lactate dehydrogenase homologues of confamilial deep-living fishes
    • Hennessey JP Jr, Siebenaller JF (1985) Pressure inactivation of tetrameric lactate dehydrogenase homologues of confamilial deep-living fishes. J Comp Physiol B 155:647-652
    • (1985) J Comp Physiol B , vol.155 , pp. 647-652
    • Hennessey Jr., J.P.1    Siebenaller, J.F.2
  • 13
    • 0031196960 scopus 로고    scopus 로고
    • The molecular biology of barophilic bacteria
    • Kato C, Bartlett DH (1997) The molecular biology of barophilic bacteria. Extremophiles 1:111-116
    • (1997) Extremophiles , vol.1 , pp. 111-116
    • Kato, C.1    Bartlett, D.H.2
  • 14
    • 77957056949 scopus 로고    scopus 로고
    • How do deep-sea microorganisms respond to environmental pressure?
    • Storey KB, Storey J (eds) Elsevier Science, Amsterdam
    • Kato C, Nakasone K, Qureshi M, Horikoshi K (2000) How do deep-sea microorganisms respond to environmental pressure? In: Storey KB, Storey J (eds) Environmental stressors and gene responses. Elsevier Science, Amsterdam, pp 277-291
    • (2000) Environmental Stressors and Gene Responses , pp. 277-291
    • Kato, C.1    Nakasone, K.2    Qureshi, M.3    Horikoshi, K.4
  • 15
    • 0023051846 scopus 로고
    • Conformational drift of dissociated lactate dehydrogenases
    • King L, Weber G (1986) Conformational drift of dissociated lactate dehydrogenases. Biochemistry 25:3632-3637
    • (1986) Biochemistry , vol.25 , pp. 3632-3637
    • King, L.1    Weber, G.2
  • 16
    • 0000057219 scopus 로고
    • Effect of light scattering on ultraviolet difference spectra
    • Leach SJ, Scheraga HA (1960) Effect of light scattering on ultraviolet difference spectra. J Am Chem Soc 82:4790-4792
    • (1960) J Am Chem Soc , vol.82 , pp. 4790-4792
    • Leach, S.J.1    Scheraga, H.A.2
  • 17
    • 0022542165 scopus 로고
    • Salt-dependent changes in the DNA binding co-operativity of Escherichia coli single strand binding protein
    • Lohman TM, Overman LB, Datta S (1986) Salt-dependent changes in the DNA binding co-operativity of Escherichia coli single strand binding protein. J Mol Biol 187:603-615
    • (1986) J Mol Biol , vol.187 , pp. 603-615
    • Lohman, T.M.1    Overman, L.B.2    Datta, S.3
  • 18
    • 0025126497 scopus 로고
    • Reversible inhibition of EcoRI with elevated pressure
    • Macgregor RB Jr (1990) Reversible inhibition of EcoRI with elevated pressure. Biochem Biophys Res Commun 170:775-778
    • (1990) Biochem Biophys Res Commun , vol.170 , pp. 775-778
    • Macgregor Jr., R.B.1
  • 19
    • 0027255479 scopus 로고
    • Structural and genetic analysis of protein stability
    • Matthews BW (1993) Structural and genetic analysis of protein stability. Annu Rev Biochem 62:139-160
    • (1993) Annu Rev Biochem , vol.62 , pp. 139-160
    • Matthews, B.W.1
  • 20
    • 34147224324 scopus 로고
    • The single-stranded DNA-binding protein of Escherichia coli
    • Meyer RR, Laine PS (1990) The single-stranded DNA-binding protein of Escherichia coli. Microbiol Rev 54:342-380
    • (1990) Microbiol Rev , vol.54 , pp. 342-380
    • Meyer, R.R.1    Laine, P.S.2
  • 21
    • 0029832690 scopus 로고    scopus 로고
    • Pressure effects on enzyme activity and stability at high temperature
    • Michels PC, Hei D, Clark DS (1996) Pressure effects on enzyme activity and stability at high temperature. Adv Protein Chem 48:341-376
    • (1996) Adv Protein Chem , vol.48 , pp. 341-376
    • Michels, P.C.1    Hei, D.2    Clark, D.S.3
  • 22
    • 0032143799 scopus 로고    scopus 로고
    • Mechanisms of gene expression controlled by pressure in deep-sea microorganisms
    • Nakasone K, Ikegami A, Kato C, Usami R, Horikoshi K (1998) Mechanisms of gene expression controlled by pressure in deep-sea microorganisms. Extremophiles 2:149-154
    • (1998) Extremophiles , vol.2 , pp. 149-154
    • Nakasone, K.1    Ikegami, A.2    Kato, C.3    Usami, R.4    Horikoshi, K.5
  • 23
    • 0031670034 scopus 로고    scopus 로고
    • Taxonomic studies of deep-sea barophilic Shewanella strains and description of Shewanella violacea sp. nov.
    • Nogi Y, Kato C, 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
  • 24
    • 0028871804 scopus 로고
    • How to measure and predict the molar absorption coefficient of a protein
    • Pace CN, Vajdos F, Fee L, Grimsley G, Gray T (1995) How to measure and predict the molar absorption coefficient of a protein. Protein Sci 4:2411-2423
    • (1995) Protein Sci , vol.4 , pp. 2411-2423
    • Pace, C.N.1    Vajdos, F.2    Fee, L.3    Grimsley, G.4    Gray, T.5
  • 25
    • 0019890116 scopus 로고
    • Pressure-induced reversible dissociation of enolase
    • Paladini AA, Weber G (1981) Pressure-induced reversible dissociation of enolase. Biochemistry 20:2587-2593
    • (1981) Biochemistry , vol.20 , pp. 2587-2593
    • Paladini, A.A.1    Weber, G.2
  • 26
    • 0023130146 scopus 로고
    • Slab gel electrophoresis of oligomeric proteins under high hydrostatic pressure. I. Description of the system and demonstration of the pressure dissociation of a dimer
    • Paladini AA, Silva JL, Weber G (1987) Slab gel electrophoresis of oligomeric proteins under high hydrostatic pressure. I. Description of the system and demonstration of the pressure dissociation of a dimer. Anal Biochem 161:358-364
    • (1987) Anal Biochem , vol.161 , pp. 358-364
    • Paladini, A.A.1    Silva, J.L.2    Weber, G.3
  • 27
    • 0031009811 scopus 로고    scopus 로고
    • Crystal structure of the homo-tetrameric DNA binding domain of Escherichia coli single-stranded DNA-binding protein determined by multiwavelength x-ray diffraction on the selenomethionyl protein at 2.9-A resolution
    • USA
    • Raghunathan S, Ricard CS, Lohman TM, Waksman G (1997) Crystal structure of the homo-tetrameric DNA binding domain of Escherichia coli single-stranded DNA-binding protein determined by multiwavelength x-ray diffraction on the selenomethionyl protein at 2.9-A resolution. Proc Natl Acad Sci USA 94:6652-6657
    • (1997) Proc Natl Acad Sci , vol.94 , pp. 6652-6657
    • Raghunathan, S.1    Ricard, C.S.2    Lohman, T.M.3    Waksman, G.4
  • 28
    • 0028210538 scopus 로고
    • Hydrostatic pressure reverses osmotic pressure effects on the specificity of EcoRI-DNA interactions
    • Robinson CR, Sligar SG (1994) Hydrostatic pressure reverses osmotic pressure effects on the specificity of EcoRI-DNA interactions. Biochemistry 33:3787-3793
    • (1994) Biochemistry , vol.33 , pp. 3787-3793
    • Robinson, C.R.1    Sligar, S.G.2
  • 29
    • 0023051519 scopus 로고
    • Dissociation of the lactose repressor protein tetramer using high hydrostatic pressure
    • Royer CA, Weber G, Daly TJ, Matthews KS (1986) Dissociation of the lactose repressor protein tetramer using high hydrostatic pressure Biochemistry 25:8308-8315
    • (1986) Biochemistry , vol.25 , pp. 8308-8315
    • Royer, C.A.1    Weber, G.2    Daly, T.J.3    Matthews, K.S.4
  • 30
    • 0027180821 scopus 로고
    • Effects of amino acid substitutions on the pressure denaturation of staphylococcal nuclease as monitored by fluorescence and nuclear magnetic resonance spectroscopy
    • Royer CA, Hinck AP, Loh SN, Prehoda KE, Peng X, Jonas J, Markley JL (1993) Effects of amino acid substitutions on the pressure denaturation of staphylococcal nuclease as monitored by fluorescence and nuclear magnetic resonance spectroscopy. Biochemistry 32:5222-5232
    • (1993) Biochemistry , vol.32 , pp. 5222-5232
    • Royer, C.A.1    Hinck, A.P.2    Loh, S.N.3    Prehoda, K.E.4    Peng, X.5    Jonas, J.6    Markley, J.L.7
  • 31
    • 0024276840 scopus 로고
    • Dissociation of yeast hexokinase by hydrostatic pressure
    • Ruan K, Weber G (1988) Dissociation of yeast hexokinase by hydrostatic pressure. Biochemistry 27:3295-3301
    • (1988) Biochemistry , vol.27 , pp. 3295-3301
    • Ruan, K.1    Weber, G.2
  • 32
    • 0024963668 scopus 로고
    • Hysteresis and conformational drift of pressure -dissociated glyceraldehydephosphate dehydrogenase
    • Ruan K, Weber G (1989) Hysteresis and conformational drift of pressure -dissociated glyceraldehydephosphate dehydrogenase Biochemistry 28: 2144-2153
    • (1989) Biochemistry , vol.28 , pp. 2144-2153
    • Ruan, K.1    Weber, G.2
  • 33
    • 0017825931 scopus 로고
    • Pressure-adaptive differences in lactate dehydrogenases of congeneric fishes living at different depths
    • Siebenaller JF, Somero GN (1978) Pressure-adaptive differences in lactate dehydrogenases of congeneric fishes living at different depths. Science 201:255-257
    • (1978) Science , vol.201 , pp. 255-257
    • Siebenaller, J.F.1    Somero, G.N.2
  • 34
    • 0023055734 scopus 로고
    • Pressure dissociation and conformational drift of the beta dimer of tryptophan synthase
    • Silva JL, Miles EW, Weber G (1986) Pressure dissociation and conformational drift of the beta dimer of tryptophan synthase. Biochemistry 25:5780-5786
    • (1986) Biochemistry , vol.25 , pp. 5780-5786
    • Silva, J.L.1    Miles, E.W.2    Weber, G.3
  • 35
    • 0018543508 scopus 로고
    • Inefficient lactate dehydrogenases of deep-sea fishes
    • Somero GN, Siebenaller JF (1979) Inefficient lactate dehydrogenases of deep-sea fishes. Nature 282:100-102
    • (1979) Nature , vol.282 , pp. 100-102
    • Somero, G.N.1    Siebenaller, J.F.2
  • 36
    • 0034989121 scopus 로고    scopus 로고
    • Pressure effects on activity and stability of hyperthermophilic enzymes
    • Sun MM, Clark DS (2001) Pressure effects on activity and stability of hyperthermophilic enzymes. Methods Enzymol 334:316-27
    • (2001) Methods Enzymol , vol.334 , pp. 316-327
    • Sun, M.M.1    Clark, D.S.2
  • 37
    • 0020359569 scopus 로고
    • Polymerization thermodynamics and structural stabilities of skeletal muscle actins from vertebrates adapted to different temperatures and hydrostatic pressures
    • Swezey RR, Somero GN (1982) Polymerization thermodynamics and structural stabilities of skeletal muscle actins from vertebrates adapted to different temperatures and hydrostatic pressures. Biochemistry 21:4496-4503
    • (1982) Biochemistry , vol.21 , pp. 4496-4503
    • Swezey, R.R.1    Somero, G.N.2
  • 39
    • 0021216947 scopus 로고
    • Characterization of the structural and functional defect in the Escherichia coli single-stranded DNA binding protein encoded by the ssb-1 mutant gene: Expression of the ssb-1 gene under lambda pL regulation
    • Williams KR, Murphy JB, Chase JW (1984) Characterization of the structural and functional defect in the Escherichia coli single-stranded DNA binding protein encoded by the ssb-1 mutant gene: expression of the ssb-1 gene under lambda pL regulation. J Biol Chem 259:11804-11811
    • (1984) J Biol Chem , vol.259 , pp. 11804-11811
    • Williams, K.R.1    Murphy, J.B.2    Chase, J.W.3
  • 40
    • 0031023811 scopus 로고    scopus 로고
    • Crystal structure of human mitochondrial single-stranded DNA binding protein at 2.4 Å resolution
    • Yang C, Curth U, Urbanke C, Kang C (1997) Crystal structure of human mitochondrial single-stranded DNA binding protein at 2.4 Å resolution. Nat Struct Biol 4:153-157
    • (1997) Nat Struct Biol , vol.4 , pp. 153-157
    • Yang, C.1    Curth, U.2    Urbanke, C.3    Kang, C.4


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