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Volumn 44, Issue 1, 1998, Pages 64-73

Isolation and characterization of an antifreeze protein with ice nucleation activity from the plant growth promoting rhizobacterium Pseudomonas putida GR12-2

Author keywords

Antifreeze protein; Freezing tolerance; Ice nucleation protein; Plant grow promoting rhizobacteria

Indexed keywords

BACTERIAL PROTEIN;

EID: 0031980952     PISSN: 00084166     EISSN: None     Source Type: Journal    
DOI: 10.1139/cjm-44-1-64     Document Type: Article
Times cited : (103)

References (45)
  • 1
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. 1976. A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72: 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.1
  • 2
    • 0025305519 scopus 로고
    • Surface properties and size of the ice-nucleation site in ice-nucleation active bacteria: Theoretical considerations
    • Burke, M.J., and Lindow, S.E. 1990. Surface properties and size of the ice-nucleation site in ice-nucleation active bacteria: theoretical considerations. Cryobioloby, 27: 80-84.
    • (1990) Cryobioloby , vol.27 , pp. 80-84
    • Burke, M.J.1    Lindow, S.E.2
  • 3
    • 0001222759 scopus 로고
    • Biological antifreeze agents in cold water fishes
    • DeVries, A. 1982. Biological antifreeze agents in cold water fishes. Comp. Biochem. Physiol. 73A: 627-640.
    • (1982) Comp. Biochem. Physiol. , vol.73 A , pp. 627-640
    • DeVries, A.1
  • 4
    • 0022523733 scopus 로고
    • Antifreeze glycopeptides and peptides: Interactions with ice and water
    • DeVries, A. 1986. Antifreeze glycopeptides and peptides: interactions with ice and water. Methods Enzymol. 127: 293-303.
    • (1986) Methods Enzymol. , vol.127 , pp. 293-303
    • DeVries, A.1
  • 5
    • 0014666651 scopus 로고
    • Freezing resistance in some Antarctic fishes
    • Washington, D.C.
    • DeVries, A.L., and Wohlschlag, D.E. 1969. Freezing resistance in some Antarctic fishes. Science (Washington, D.C.), 163: 1073-1075.
    • (1969) Science , vol.163 , pp. 1073-1075
    • DeVries, A.L.1    Wohlschlag, D.E.2
  • 6
    • 0014939615 scopus 로고
    • Chemical and physical properties of freezing point-depressing glycoproteins from Antarctic fishes
    • DeVries, A.L., Komatsu, S.K., and Feeney, R.E. 1970. Chemical and physical properties of freezing point-depressing glycoproteins from Antarctic fishes. J. Biol. Chem. 245: 2901-2908.
    • (1970) J. Biol. Chem. , vol.245 , pp. 2901-2908
    • DeVries, A.L.1    Komatsu, S.K.2    Feeney, R.E.3
  • 7
    • 0023408012 scopus 로고
    • Isolation and composition of the constitutive agglutinins from haploid Saccharomyces cerevisiae cells
    • Dijmons, P.C., Nederbragt, A.J.A., Klis, P.M., and Van-Den-Ende, H. 1987. Isolation and composition of the constitutive agglutinins from haploid Saccharomyces cerevisiae cells. Arch. Microbiol. 148: 208-212.
    • (1987) Arch. Microbiol. , vol.148 , pp. 208-212
    • Dijmons, P.C.1    Nederbragt, A.J.A.2    Klis, P.M.3    Van-Den-Ende, H.4
  • 8
    • 0028232701 scopus 로고
    • Purification and characterization of a thermal hysteresis protein from a plant, the bittersweet night shade Solanum dulcamara
    • Duman, J.G. 1994. Purification and characterization of a thermal hysteresis protein from a plant, the bittersweet night shade Solanum dulcamara. Biochim. Biophys. Acta, 1206: 129-135.
    • (1994) Biochim. Biophys. Acta , vol.1206 , pp. 129-135
    • Duman, J.G.1
  • 9
    • 0000078585 scopus 로고
    • Thermal hysteresis protein activity in bacteria, fungi, and phylogenetically diverse plants
    • Duman, J.G., and Olsen, T.M. 1993. Thermal hysteresis protein activity in bacteria, fungi, and phylogenetically diverse plants. Cryobiology, 30: 322-328.
    • (1993) Cryobiology , vol.30 , pp. 322-328
    • Duman, J.G.1    Olsen, T.M.2
  • 10
    • 0002989998 scopus 로고
    • Purification and composition of an ice nucleating protein from queens of the hornet, Vespula maculata
    • Duman, J.G., Morris, J.P., and Castellino, F.J. 1984. Purification and composition of an ice nucleating protein from queens of the hornet, Vespula maculata. J. Comp. Physiol. B, 154: 79-83.
    • (1984) J. Comp. Physiol. B , vol.154 , pp. 79-83
    • Duman, J.G.1    Morris, J.P.2    Castellino, F.J.3
  • 11
    • 0003032556 scopus 로고
    • Hemolymph proteins involved in insect subzero-temperature tolerance: Ice nucleators and antifreeze proteins
    • Edited by R.E. Lee and D.L. Denlinger. Chapman and Hall, New York
    • Duman, J.G., Xu, L., Neven, L.G., Tursman, D., and Wu, D.W. 1991a. Hemolymph proteins involved in insect subzero-temperature tolerance: ice nucleators and antifreeze proteins. In Insects at low temperature, Edited by R.E. Lee and D.L. Denlinger. Chapman and Hall, New York. pp. 94-127.
    • (1991) Insects at Low Temperature , pp. 94-127
    • Duman, J.G.1    Xu, L.2    Neven, L.G.3    Tursman, D.4    Wu, D.W.5
  • 12
    • 0025788875 scopus 로고
    • Further characterization of the lipoprotein ice nucleutor from freeze tolerant larvae of the cranefly Tipula trivittata
    • Duman, J.G., Wu, D.W., Wolber, P.K., and Mucller, G.M. 1991b. Further characterization of the lipoprotein ice nucleutor from freeze tolerant larvae of the cranefly Tipula trivittata. Comp. Biochem. Physiol. B, 99: 599-607.
    • (1991) Comp. Biochem. Physiol. B , vol.99 , pp. 599-607
    • Duman, J.G.1    Wu, D.W.2    Wolber, P.K.3    Mucller, G.M.4
  • 13
    • 0001446789 scopus 로고
    • Isolation and characterization of antifreeze proteins from smelt (Osmerus mordax) and Atlantic herring (Clupea harengus)
    • Ewart, K.V., and Fletcher, G.L. 1990. Isolation and characterization of antifreeze proteins from smelt (Osmerus mordax) and Atlantic herring (Clupea harengus). Can. J. Zool. 68: 1652-1658.
    • (1990) Can. J. Zool. , vol.68 , pp. 1652-1658
    • Ewart, K.V.1    Fletcher, G.L.2
  • 14
    • 0025858821 scopus 로고
    • Effect of boronic acids on antifreeze proteins
    • Feeney, R.E., Osuga, D.T., and Yeh, Y. 1991. Effect of boronic acids on antifreeze proteins. J. Protein Chem. 10: 167-170.
    • (1991) J. Protein Chem. , vol.10 , pp. 167-170
    • Feeney, R.E.1    Osuga, D.T.2    Yeh, Y.3
  • 15
    • 0000687463 scopus 로고
    • Size of bacterial icenucleation sites measured in situ by radiation inactivation analysis
    • Govindarajan, A.G., and Lindow, S.E. 1988a. Size of bacterial icenucleation sites measured in situ by radiation inactivation analysis. Proc. Natl. Acad. Sci. U.S.A. 85: 1334-1338.
    • (1988) Proc. Natl. Acad. Sci. U.S.A. , vol.85 , pp. 1334-1338
    • Govindarajan, A.G.1    Lindow, S.E.2
  • 16
    • 0028835687 scopus 로고
    • Antifreeze proteins and their potential use in frozen foods
    • Griffith, M., and Ewart, K.V. 1995. Antifreeze proteins and their potential use in frozen foods. Biotechnol. Adv. 13: 375-402.
    • (1995) Biotechnol. Adv. , vol.13 , pp. 375-402
    • Griffith, M.1    Ewart, K.V.2
  • 17
    • 0000047084 scopus 로고
    • Antifreeze protein produced endogenously in winter rye leaves
    • Griffith, M., Ala, P., Yang, D.S.C., Hon, W., and Moffatt, B.A. 1992. Antifreeze protein produced endogenously in winter rye leaves. Plant Physiol. 100: 593-596.
    • (1992) Plant Physiol. , vol.100 , pp. 593-596
    • Griffith, M.1    Ala, P.2    Yang, D.S.C.3    Hon, W.4    Moffatt, B.A.5
  • 18
    • 0027197982 scopus 로고
    • Isolation and characterization of hydroxylamine-induced mutations in the Erwinia herbicola ice nucleation gene that selectively reduce warm temperature ice nucleation activity
    • Gurian-Sherman, D., Lindow, S.E., and Panopoulos, N.J. 1993. Isolation and characterization of hydroxylamine-induced mutations in the Erwinia herbicola ice nucleation gene that selectively reduce warm temperature ice nucleation activity. Mol. Microbial. 9: 383-391.
    • (1993) Mol. Microbial. , vol.9 , pp. 383-391
    • Gurian-Sherman, D.1    Lindow, S.E.2    Panopoulos, N.J.3
  • 19
    • 7144228231 scopus 로고
    • Detection limits in amino acid analysis: An overview
    • Edited by B. Wittmann-Liebold. Springer-Verlag, Berlin
    • Hare, P.E. 1988. Detection limits in amino acid analysis: an overview. In Methods in protein sequence analysis. Edited by B. Wittmann-Liebold. Springer-Verlag, Berlin. pp. 2-9.
    • (1988) Methods in Protein Sequence Analysis , pp. 2-9
    • Hare, P.E.1
  • 20
    • 0028086816 scopus 로고
    • Extraction and isolation of antifreeze proteins from winter rye (Secale cereale L.) leaves
    • Hon, W.C., Griffith, M., Chong, P., and Yang, D.S.C. 1994. Extraction and isolation of antifreeze proteins from winter rye (Secale cereale L.) leaves. Plant Physiol. 104: 971-980.
    • (1994) Plant Physiol. , vol.104 , pp. 971-980
    • Hon, W.C.1    Griffith, M.2    Chong, P.3    Yang, D.S.C.4
  • 21
    • 0029411516 scopus 로고
    • Antifreeze proteins in winter rye are similar to pathogenesis-related proteins
    • Hon, W.C., Griffith, M., Mlynarz, A., Kwok, Y.C., and Yang, D.S.C. 1995. Antifreeze proteins in winter rye are similar to pathogenesis-related proteins. Plant Physiol. 109: 879-889.
    • (1995) Plant Physiol. , vol.109 , pp. 879-889
    • Hon, W.C.1    Griffith, M.2    Mlynarz, A.3    Kwok, Y.C.4    Yang, D.S.C.5
  • 22
    • 0002218784 scopus 로고
    • Inhibition of recrystallization of ice by insect thermal hysteresis proteins: A possible cryoprotective role
    • Knight, C.A., and Duman, J.G. 1986. Inhibition of recrystallization of ice by insect thermal hysteresis proteins: a possible cryoprotective role. Cryobiology, 23: 252-262.
    • (1986) Cryobiology , vol.23 , pp. 252-262
    • Knight, C.A.1    Duman, J.G.2
  • 23
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London), 227: 680-685.
    • (1970) Nature (London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 24
    • 0026331527 scopus 로고
    • Expression and characterization of an active and thermally more stable recombinant antifreeze polypeptide from ocean pout, Macrozoarces americanus, in Escherichia coli: Improved expression by the modification of the secondary structure of the mRNA
    • Li, X., Trinh, K.Y., and Hew, C.L. 1991. Expression and characterization of an active and thermally more stable recombinant antifreeze polypeptide from ocean pout, Macrozoarces americanus, in Escherichia coli: improved expression by the modification of the secondary structure of the mRNA. Protein Eng. 4: 995-1002.
    • (1991) Protein Eng. , vol.4 , pp. 995-1002
    • Li, X.1    Trinh, K.Y.2    Hew, C.L.3
  • 25
  • 26
    • 0002013863 scopus 로고
    • The role of bacterial ice nuclei in frost injury to sensitive plants
    • Edited by P.H. Li and A. Sakai. Academic Press. New York
    • Lindow, S.E., Arny, D.C., and Upper, C.D. 1978. The role of bacterial ice nuclei in frost injury to sensitive plants. In Plant cold hardiness and freezing stress. Edited by P.H. Li and A. Sakai. Academic Press. New York. pp. 249-263.
    • (1978) Plant Cold Hardiness and Freezing Stress , pp. 249-263
    • Lindow, S.E.1    Arny, D.C.2    Upper, C.D.3
  • 27
    • 0021202164 scopus 로고
    • Freezing of living cells: Mechanisms and implications
    • Mazur, P. 1984. Freezing of living cells: mechanisms and implications. Am. J. Physiol. 247: C125-C142.
    • (1984) Am. J. Physiol. , vol.247
    • Mazur, P.1
  • 28
    • 0027326248 scopus 로고
    • High-level expression of ice nuclei in a Pseudomonas syringae strain is induced by nutrient limitation and low temperature
    • Nemecek-Marshall, M., Laduca, R., and Fall, R. 1993. High-level expression of ice nuclei in a Pseudomonas syringae strain is induced by nutrient limitation and low temperature. J. Bacteriol. 175: 4062-4070.
    • (1993) J. Bacteriol. , vol.175 , pp. 4062-4070
    • Nemecek-Marshall, M.1    Laduca, R.2    Fall, R.3
  • 29
    • 0002493509 scopus 로고
    • Purification and characterization of an insect hemolymph lipoprotein ice nucleator: Evidence for the importance of phosphatidylinositol and apolipoprotein in the ice nucleator activity
    • Neven, L.G., Duman, J.G., Low, M.G., Sehl, L.C., and Castellino, F.J. 1989. Purification and characterization of an insect hemolymph lipoprotein ice nucleator: evidence for the importance of phosphatidylinositol and apolipoprotein in the ice nucleator activity. J. Comp. Physiol. B, 159: 71-82.
    • (1989) J. Comp. Physiol. B , vol.159 , pp. 71-82
    • Neven, L.G.1    Duman, J.G.2    Low, M.G.3    Sehl, L.C.4    Castellino, F.J.5
  • 30
    • 0016711037 scopus 로고
    • High resolution two-dimensional electrophoresis of proteins
    • O'Farrell, P.H. 1974. High resolution two-dimensional electrophoresis of proteins. J. Biol. Chem. 250: 4007-4021.
    • (1974) J. Biol. Chem. , vol.250 , pp. 4007-4021
    • O'Farrell, P.H.1
  • 33
    • 0000812774 scopus 로고
    • Winter survival of the gall fly larva, Eurosta solidaginis: Profiles of fuel reserves and cryoprotectants in a natural population
    • Storey, J.M., and Storey, K.B. 1986. Winter survival of the gall fly larva, Eurosta solidaginis: profiles of fuel reserves and cryoprotectants in a natural population. J. Insect Physiol. 32: 594-556.
    • (1986) J. Insect Physiol. , vol.32 , pp. 594-1556
    • Storey, J.M.1    Storey, K.B.2
  • 34
    • 0025602922 scopus 로고
    • Frozen and alive
    • Storey, K.B., and Storey, J.M. 1990. Frozen and alive. Sci. Am. 263(6): 92-97.
    • (1990) Sci. Am. , vol.263 , Issue.6 , pp. 92-97
    • Storey, K.B.1    Storey, J.M.2
  • 35
    • 7144250160 scopus 로고
    • Does the plant growth-promoting rhizobacterium Pseudomonas putida GR12-2 survive cold temperature by synthesizing its own antifreeze protein?
    • Edited by M.H. Ryder, P.M. Stephens, and G.D. Bowen. Commonwealth Scientific and Industrial Research Organization, Adelaide, Australia
    • Sun, X., Griffith, M., Pasternak, J.J., and Glick, B.R. 1994. Does the plant growth-promoting rhizobacterium Pseudomonas putida GR12-2 survive cold temperature by synthesizing its own antifreeze protein? In Improving plant productivity with rhizospere bacteria, Edited by M.H. Ryder, P.M. Stephens, and G.D. Bowen. Commonwealth Scientific and Industrial Research Organization, Adelaide, Australia, pp. 153-155.
    • (1994) Improving Plant Productivity with Rhizospere Bacteria , pp. 153-155
    • Sun, X.1    Griffith, M.2    Pasternak, J.J.3    Glick, B.R.4
  • 36
    • 0028807747 scopus 로고
    • Low temperature growth, freezing survival, and production of antifreeze protein by the plant growth promoting rhizobacterium Pseudomonas putida GR12-2
    • Sun, X., Griffith, M., Pasternak, J.J., and Glick, B.R. 1995. Low temperature growth, freezing survival, and production of antifreeze protein by the plant growth promoting rhizobacterium Pseudomonas putida GR12-2. Can. J. Microbiol. 41: 776-784.
    • (1995) Can. J. Microbiol. , vol.41 , pp. 776-784
    • Sun, X.1    Griffith, M.2    Pasternak, J.J.3    Glick, B.R.4
  • 37
    • 0026010393 scopus 로고
    • Components of ice nucleation structures of bacteria
    • Turner, M.A., Arellano, F., and Kozloff, L.M. 1991. Components of ice nucleation structures of bacteria. J. Bacteriol. 173: 6515-6527.
    • (1991) J. Bacteriol. , vol.173 , pp. 6515-6527
    • Turner, M.A.1    Arellano, F.2    Kozloff, L.M.3
  • 38
    • 0001278148 scopus 로고
    • Quantitative evaluation of experiment results on the heterogeneous freezing nucleation of supercooled liquids
    • Vali, G. 1971. Quantitative evaluation of experiment results on the heterogeneous freezing nucleation of supercooled liquids. J. Atmos. Sci. 28: 402-409.
    • (1971) J. Atmos. Sci. , vol.28 , pp. 402-409
    • Vali, G.1
  • 40
    • 0023056237 scopus 로고
    • Conserved repeats in diverged ice nucleation structural genes from two species of Pseudomonas
    • Warren, G., Corotto, L., and Wolber, P. 1986. Conserved repeats in diverged ice nucleation structural genes from two species of Pseudomonas. Nucleic Acid Res. 14: 8047-8060.
    • (1986) Nucleic Acid Res. , vol.14 , pp. 8047-8060
    • Warren, G.1    Corotto, L.2    Wolber, P.3
  • 41
    • 0026085611 scopus 로고
    • Molecular aspects of microbial ice nucleation
    • Warren, G., and Wolber, P. 1991. Molecular aspects of microbial ice nucleation. Mol. Microbiol. 5: 239-243.
    • (1991) Mol. Microbiol. , vol.5 , pp. 239-243
    • Warren, G.1    Wolber, P.2
  • 43
    • 0019882018 scopus 로고
    • Silver staining of proteins in polyacrylamide gels
    • Wray, W., Boulikas, T., Wray, V.P., and Hancock, R. 1981. Silver staining of proteins in polyacrylamide gels. Anal. Biochem. 118: 197-203.
    • (1981) Anal. Biochem. , vol.118 , pp. 197-203
    • Wray, W.1    Boulikas, T.2    Wray, V.P.3    Hancock, R.4
  • 44
    • 0017159805 scopus 로고
    • Nucleating agents in the haemolymph of insects tolerant to freezing
    • Zachariassen, K.E., and Hammel, H.T. 1976. Nucleating agents in the haemolymph of insects tolerant to freezing. Nature (London), 262: 285-287.
    • (1976) Nature (London) , vol.262 , pp. 285-287
    • Zachariassen, K.E.1    Hammel, H.T.2
  • 45
    • 0024995479 scopus 로고
    • Conserved repetition in the ice nucleation gene inaX from Xanthomonas campestris pv. translucens
    • Zhao, J.L., and Orser, C.S. 1990. Conserved repetition in the ice nucleation gene inaX from Xanthomonas campestris pv. translucens. Mol. Gen. Genet. 223: 163-166.
    • (1990) Mol. Gen. Genet. , vol.223 , pp. 163-166
    • Zhao, J.L.1    Orser, C.S.2


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