메뉴 건너뛰기




Volumn 63, Issue 3, 2011, Pages 220-228

Heterologous expression, refolding and functional characterization of two antifreeze proteins from Fragilariopsis cylindrus (Bacillariophyceae)

Author keywords

Antifreeze protein; Diatom; Fragilariopsis cylindrus; Heterologous expression; Recrystallization inhibition

Indexed keywords

ANTIFREEZE PROTEIN; BUFFER; PELB LEADER PEPTIDE; SIGNAL PEPTIDE; UNCLASSIFIED DRUG;

EID: 82155196420     PISSN: 00112240     EISSN: 10902392     Source Type: Journal    
DOI: 10.1016/j.cryobiol.2011.08.005     Document Type: Article
Times cited : (24)

References (59)
  • 1
    • 0025350086 scopus 로고
    • An investigation of oligopeptides linking domains in protein tertiary structures and possible candidates for general gene fusion
    • Argos P. An investigation of oligopeptides linking domains in protein tertiary structures and possible candidates for general gene fusion. Journal of Molecular Biology 1990, 211(4):943-958.
    • (1990) Journal of Molecular Biology , vol.211 , Issue.4 , pp. 943-958
    • Argos, P.1
  • 2
    • 77954634710 scopus 로고    scopus 로고
    • Antifreeze proteins in polar sea ice diatoms: diversity and gene expression in the genus Fragilariopsis
    • Bayer-Giraldi M., Uhlig C., John U., Mock T., Valentin K. Antifreeze proteins in polar sea ice diatoms: diversity and gene expression in the genus Fragilariopsis. Environmental Microbiology 2010, 12(4):1041-1052.
    • (2010) Environmental Microbiology , vol.12 , Issue.4 , pp. 1041-1052
    • Bayer-Giraldi, M.1    Uhlig, C.2    John, U.3    Mock, T.4    Valentin, K.5
  • 3
    • 82155173437 scopus 로고    scopus 로고
    • Characterization of an antifreeze protein from the polar diatom Fragilariopsis cylindrus and its relevance in sea ice
    • Bayer-Giraldi M., Weikusat I., Besir H., Dieckmann G. Characterization of an antifreeze protein from the polar diatom Fragilariopsis cylindrus and its relevance in sea ice. Cryobiology 2011, 10.1016/j.cryobiol.2011.08.006.
    • (2011) Cryobiology
    • Bayer-Giraldi, M.1    Weikusat, I.2    Besir, H.3    Dieckmann, G.4
  • 4
    • 0027270959 scopus 로고
    • Use of proline mutants to help solve the NMR solution structure of type III antifreeze protein
    • Chao H., Davies P.L., Sykes B.D., Sönnichsen F.D. Use of proline mutants to help solve the NMR solution structure of type III antifreeze protein. Protein Science 1993, 2(9):1411-1428.
    • (1993) Protein Science , vol.2 , Issue.9 , pp. 1411-1428
    • Chao, H.1    Davies, P.L.2    Sykes, B.D.3    Sönnichsen, F.D.4
  • 5
    • 0001179771 scopus 로고
    • Equations for determining the gas and brine volumes in sea-ice samples
    • Cox G.F.N., Weeks W.F. Equations for determining the gas and brine volumes in sea-ice samples. Journal of Glaciology 1983, 29(102):306-316.
    • (1983) Journal of Glaciology , vol.29 , Issue.102 , pp. 306-316
    • Cox, G.F.N.1    Weeks, W.F.2
  • 6
    • 0030998468 scopus 로고    scopus 로고
    • The chemistry and enzymology of the type I signal peptidases
    • Dalbey R.E., Lively M.O., Bron S., Dijl J.M.V. The chemistry and enzymology of the type I signal peptidases. Protein Science 1997, 6(6):1129-1138.
    • (1997) Protein Science , vol.6 , Issue.6 , pp. 1129-1138
    • Dalbey, R.E.1    Lively, M.O.2    Bron, S.3    Dijl, J.M.V.4
  • 7
    • 0025325036 scopus 로고
    • Biochemistry of fish antifreeze proteins
    • Davies P., Hew C. Biochemistry of fish antifreeze proteins. FASEB Journal 1990, 4(8):2460-2468.
    • (1990) FASEB Journal , vol.4 , Issue.8 , pp. 2460-2468
    • Davies, P.1    Hew, C.2
  • 8
    • 0031934222 scopus 로고    scopus 로고
    • Antifreeze proteins bind independently to ice
    • DeLuca C.I., Comley R., Davies P.L. Antifreeze proteins bind independently to ice. Biophysical Journal 1998, 74(3):1502-1508.
    • (1998) Biophysical Journal , vol.74 , Issue.3 , pp. 1502-1508
    • DeLuca, C.I.1    Comley, R.2    Davies, P.L.3
  • 9
    • 0014666651 scopus 로고
    • Freezing resistance in some Antarctic fishes
    • DeVries A.L., Wohlschlag D. Freezing resistance in some Antarctic fishes. Science 1969, 163:1073-1075.
    • (1969) Science , vol.163 , pp. 1073-1075
    • DeVries, A.L.1    Wohlschlag, D.2
  • 10
    • 67349206215 scopus 로고    scopus 로고
    • The bugs that came in from the cold: molecular adaptations to low temperatures in insects
    • Doucet D., Walker V., Qin W. The bugs that came in from the cold: molecular adaptations to low temperatures in insects. Cellular and Molecular Life Sciences 2009, 66:1404-1418.
    • (2009) Cellular and Molecular Life Sciences , vol.66 , pp. 1404-1418
    • Doucet, D.1    Walker, V.2    Qin, W.3
  • 11
    • 0017118163 scopus 로고
    • Isolation, characterization, and physical properties of protein antifreezes from the winter flounder, Pseudopleuronectes americanus
    • Duman J.G., DeVries A.L. Isolation, characterization, and physical properties of protein antifreezes from the winter flounder, Pseudopleuronectes americanus. Comparative Biochemistry and Physiology Part B: Comparative Biochemistry 1976, 54(3):375-380.
    • (1976) Comparative Biochemistry and Physiology Part B: Comparative Biochemistry , vol.54 , Issue.3 , pp. 375-380
    • Duman, J.G.1    DeVries, A.L.2
  • 12
    • 0000078585 scopus 로고
    • Thermal hysteresis protein activity in bacteria, fungi, and phylogenetically diverse plants
    • Duman J.G., Olsen T.M. Thermal hysteresis protein activity in bacteria, fungi, and phylogenetically diverse plants. Cryobiology 1993, 30(3):322-328.
    • (1993) Cryobiology , vol.30 , Issue.3 , pp. 322-328
    • Duman, J.G.1    Olsen, T.M.2
  • 13
    • 0035052709 scopus 로고    scopus 로고
    • Antifreeze and ice nucleation proteins in terrestrial arthropods
    • Duman J.G. Antifreeze and ice nucleation proteins in terrestrial arthropods. Annual Review of Physiology 2001, 63(1):327-357.
    • (2001) Annual Review of Physiology , vol.63 , Issue.1 , pp. 327-357
    • Duman, J.G.1
  • 14
    • 0032982510 scopus 로고    scopus 로고
    • Structure, function and evolution of antifreeze proteins
    • Ewart K.V., Lin Q., Hew C.L. Structure, function and evolution of antifreeze proteins. Cellular and Molecular Life Sciences 1999, 55(2):271-283.
    • (1999) Cellular and Molecular Life Sciences , vol.55 , Issue.2 , pp. 271-283
    • Ewart, K.V.1    Lin, Q.2    Hew, C.L.3
  • 16
  • 18
    • 0030049438 scopus 로고    scopus 로고
    • Skin antifreeze protein genes of the winter flounder, Pleuronectes americanus, encode distinct and active polypeptides without the secretory signal and prosequences
    • Gong Z., Ewart K.V., Hu Z., Fletcher G.L., Hew C.L. Skin antifreeze protein genes of the winter flounder, Pleuronectes americanus, encode distinct and active polypeptides without the secretory signal and prosequences. Journal of Biological Chemistry 1996, 271(8):4106-4112.
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.8 , pp. 4106-4112
    • Gong, Z.1    Ewart, K.V.2    Hu, Z.3    Fletcher, G.L.4    Hew, C.L.5
  • 19
    • 0034691594 scopus 로고    scopus 로고
    • ß-Helix structure and ice-binding properties of a hyperactive antifreeze protein from an insect
    • Graether S.P., Kuiper M.J., Gagne S.M., Walker V.K., Jia Z., Sykes B.D., Davies P.L. ß-Helix structure and ice-binding properties of a hyperactive antifreeze protein from an insect. Nature 2000, 406(6793):325-328.
    • (2000) Nature , vol.406 , Issue.6793 , pp. 325-328
    • Graether, S.P.1    Kuiper, M.J.2    Gagne, S.M.3    Walker, V.K.4    Jia, Z.5    Sykes, B.D.6    Davies, P.L.7
  • 20
    • 0030760436 scopus 로고    scopus 로고
    • Hyperactive antifreeze protein from beetles
    • Graham L.A., Liou Y.-C., Walker V.K., Davies P.L. Hyperactive antifreeze protein from beetles. Nature 1997, 388(6644):727-728.
    • (1997) Nature , vol.388 , Issue.6644 , pp. 727-728
    • Graham, L.A.1    Liou, Y.-C.2    Walker, V.K.3    Davies, P.L.4
  • 21
    • 39649112169 scopus 로고    scopus 로고
    • Hyperactive antifreeze protein from fish contains multiple ice-binding sites
    • Graham L.A., Marshall C.B., Lin F.-H., Campbell R.L., Davies P.L. Hyperactive antifreeze protein from fish contains multiple ice-binding sites. Biochemistry 2008, 47(7):2051-2063.
    • (2008) Biochemistry , vol.47 , Issue.7 , pp. 2051-2063
    • Graham, L.A.1    Marshall, C.B.2    Lin, F.-H.3    Campbell, R.L.4    Davies, P.L.5
  • 26
    • 0036470053 scopus 로고    scopus 로고
    • Antifreeze proteins an unusual receptor-ligand interaction
    • Jia Z., Davies P.L. Antifreeze proteins an unusual receptor-ligand interaction. Trends in Biochemical Sciences 2002, 27(2):101-106.
    • (2002) Trends in Biochemical Sciences , vol.27 , Issue.2 , pp. 101-106
    • Jia, Z.1    Davies, P.L.2
  • 27
    • 77952430130 scopus 로고    scopus 로고
    • Acquisition of freeze protection in a sea-ice crustacean through horizontal gene transfer?
    • Kiko R. Acquisition of freeze protection in a sea-ice crustacean through horizontal gene transfer?. Polar Biology 2010, 33(4):543-556.
    • (2010) Polar Biology , vol.33 , Issue.4 , pp. 543-556
    • Kiko, R.1
  • 28
    • 0021236688 scopus 로고
    • Fish antifreeze protein and the freezing and recrystallization of ice
    • Knight C.A., De Vries A.L., Oolman L.D. Fish antifreeze protein and the freezing and recrystallization of ice. Nature 1984, 308(5956):295-296.
    • (1984) Nature , vol.308 , Issue.5956 , pp. 295-296
    • Knight, C.A.1    De Vries, A.L.2    Oolman, L.D.3
  • 29
    • 0025959821 scopus 로고
    • Adsorption of alpha-helical antifreeze peptides on specific ice crystal surface planes
    • Knight C.A., Cheng C.C., DeVries A.L. Adsorption of alpha-helical antifreeze peptides on specific ice crystal surface planes. Biophysical Journal 1991, 59(2):409-418.
    • (1991) Biophysical Journal , vol.59 , Issue.2 , pp. 409-418
    • Knight, C.A.1    Cheng, C.C.2    DeVries, A.L.3
  • 31
    • 57349096277 scopus 로고    scopus 로고
    • A new class of ice-binding proteins discovered in a salt-stress-induced cDNA library of the psychrophilic diatom Fragilariopsis cylindrus (Bacillariophyceae)
    • Krell A., Beszteri B., Dieckmann G., Glöckner G., Valentin K., Mock T. A new class of ice-binding proteins discovered in a salt-stress-induced cDNA library of the psychrophilic diatom Fragilariopsis cylindrus (Bacillariophyceae). Journal of Phycology 2008, 43(4):423-433.
    • (2008) Journal of Phycology , vol.43 , Issue.4 , pp. 423-433
    • Krell, A.1    Beszteri, B.2    Dieckmann, G.3    Glöckner, G.4    Valentin, K.5    Mock, T.6
  • 32
    • 0346037119 scopus 로고    scopus 로고
    • High concentrations of exopolymeric substances in Arctic winter sea ice: implications for the polar ocean carbon cycle and cryoprotection of diatoms
    • Krembs C., Eicken H., Junge K., Deming J.W. High concentrations of exopolymeric substances in Arctic winter sea ice: implications for the polar ocean carbon cycle and cryoprotection of diatoms. Deep Sea Research Part I: Oceanographic Research Papers 2002, 49(12):2163-2181.
    • (2002) Deep Sea Research Part I: Oceanographic Research Papers , vol.49 , Issue.12 , pp. 2163-2181
    • Krembs, C.1    Eicken, H.2    Junge, K.3    Deming, J.W.4
  • 33
    • 28744456989 scopus 로고    scopus 로고
    • The mechanism by which fish antifreeze proteins cause thermal hysteresis
    • Kristiansen E., Zachariassen K.E. The mechanism by which fish antifreeze proteins cause thermal hysteresis. Cryobiology 2005, 51(3):262-280.
    • (2005) Cryobiology , vol.51 , Issue.3 , pp. 262-280
    • Kristiansen, E.1    Zachariassen, K.E.2
  • 35
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227(5259):680-685.
    • (1970) Nature , vol.227 , Issue.5259 , pp. 680-685
    • Laemmli, U.K.1
  • 37
    • 60449101833 scopus 로고    scopus 로고
    • Are Fragilariopsis cylindrus and Fragilariopsis nana bipolar diatoms? - morphological and molecular analyses of two sympatric species
    • Lundholm N., Hasle G. Are Fragilariopsis cylindrus and Fragilariopsis nana bipolar diatoms? - morphological and molecular analyses of two sympatric species. Nova Hedwigia. Beiheft 2008, 133:231-250.
    • (2008) Nova Hedwigia. Beiheft , vol.133 , pp. 231-250
    • Lundholm, N.1    Hasle, G.2
  • 38
    • 2442688072 scopus 로고    scopus 로고
    • Hyperactive antifreeze protein in a fish
    • Marshall C.B., Fletcher G.L., Davies P.L. Hyperactive antifreeze protein in a fish. Nature 2004, 429(6988):153.
    • (2004) Nature , vol.429 , Issue.6988 , pp. 153
    • Marshall, C.B.1    Fletcher, G.L.2    Davies, P.L.3
  • 39
    • 17844400955 scopus 로고    scopus 로고
    • Recent advances in sea-ice microbiology
    • Mock T., Thomas D.N. Recent advances in sea-ice microbiology. Environmental Microbiology 2005, 7(5):605-619.
    • (2005) Environmental Microbiology , vol.7 , Issue.5 , pp. 605-619
    • Mock, T.1    Thomas, D.N.2
  • 40
    • 0030614959 scopus 로고    scopus 로고
    • Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
    • Nielsen H., Engelbrecht J., Brunak S., von Heijne G. Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Protein Engineering 1997, 10(1):1-6.
    • (1997) Protein Engineering , vol.10 , Issue.1 , pp. 1-6
    • Nielsen, H.1    Engelbrecht, J.2    Brunak, S.3    von Heijne, G.4
  • 42
    • 84987573982 scopus 로고
    • Composition of a protein antifreeze from larvae of the beetle, Tenebrio molitor
    • Patterson J.L., Duman J.G. Composition of a protein antifreeze from larvae of the beetle, Tenebrio molitor. Journal of Experimental Zoology 1979, 210(2):361-367.
    • (1979) Journal of Experimental Zoology , vol.210 , Issue.2 , pp. 361-367
    • Patterson, J.L.1    Duman, J.G.2
  • 45
    • 0028593276 scopus 로고
    • Release of an ice-active substance by Antarctic sea ice diatoms
    • Raymond J.A., Sullivan C.W., DeVries A.L. Release of an ice-active substance by Antarctic sea ice diatoms. Polar Biology 1994, 14(1):71-75.
    • (1994) Polar Biology , vol.14 , Issue.1 , pp. 71-75
    • Raymond, J.A.1    Sullivan, C.W.2    DeVries, A.L.3
  • 46
    • 0033815338 scopus 로고    scopus 로고
    • Distribution and partial characterization of ice-active molecules associated with sea-ice diatoms
    • Raymond J.A. Distribution and partial characterization of ice-active molecules associated with sea-ice diatoms. Polar Biology 2000, 23(10):721-729.
    • (2000) Polar Biology , vol.23 , Issue.10 , pp. 721-729
    • Raymond, J.A.1
  • 47
    • 0037383396 scopus 로고    scopus 로고
    • Ice binding, recrystallization inhibition, and cryoprotective properties of ice-active substances associated with Antarctic sea ice diatoms
    • Raymond J.A., Knight C.A. Ice binding, recrystallization inhibition, and cryoprotective properties of ice-active substances associated with Antarctic sea ice diatoms. Cryobiology 2003, 46(2):174-181.
    • (2003) Cryobiology , vol.46 , Issue.2 , pp. 174-181
    • Raymond, J.A.1    Knight, C.A.2
  • 49
    • 60549093037 scopus 로고    scopus 로고
    • Ice-binding proteins from enoki and shiitake mushrooms
    • Raymond J.A., Janech M.G. Ice-binding proteins from enoki and shiitake mushrooms. Cryobiology 2009, 58(2):151-156.
    • (2009) Cryobiology , vol.58 , Issue.2 , pp. 151-156
    • Raymond, J.A.1    Janech, M.G.2
  • 50
    • 84859919944 scopus 로고    scopus 로고
    • R Development Core Team, R: A Language and Environment for Statistical Computing ISBN 3-900051-07-0.
    • R Development Core Team, R: A Language and Environment for Statistical Computing ISBN 3-900051-07-0. http://www.R-project.org.
  • 51
    • 84859919945 scopus 로고    scopus 로고
    • Folding proteins in protein function, a practical approach, Ch. Folding proteins, Oxford press
    • R. Rudolph, G. Böhm, H. Lilie, R. Jaenicke, Folding proteins in protein function, a practical approach, Ch. Folding proteins, Oxford press, 1997, pp. 57-99.
    • (1997) , pp. 57-99
    • Rudolph, R.1    Böhm, G.2    Lilie, H.3    Jaenicke, R.4
  • 53
    • 77952397828 scopus 로고    scopus 로고
    • Novel approach of high cell density recombinant bioprocess development: optimisation and scale-up from microlitre to pilot scales while maintaining the fed-batch cultivation mode of E. coli cultures
    • Siurkus J., Panula-Perala J., Horn U., Kraft M., Rimseliene R., Neubauer P. Novel approach of high cell density recombinant bioprocess development: optimisation and scale-up from microlitre to pilot scales while maintaining the fed-batch cultivation mode of E. coli cultures. Microbial Cell Factories 2010, 9(1):35.
    • (2010) Microbial Cell Factories , vol.9 , Issue.1 , pp. 35
    • Siurkus, J.1    Panula-Perala, J.2    Horn, U.3    Kraft, M.4    Rimseliene, R.5    Neubauer, P.6
  • 54
    • 0032161654 scopus 로고    scopus 로고
    • Role of cold-responsive genes in plant freezing tolerance
    • Thomashow M.F. Role of cold-responsive genes in plant freezing tolerance. Plant Physiology 1998, 118:1-7.
    • (1998) Plant Physiology , vol.118 , pp. 1-7
    • Thomashow, M.F.1
  • 55
    • 0026740537 scopus 로고
    • Plant thermal hysteresis proteins, Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
    • M.E. Urrutia, J.G. Duman, C.A. Knight, Plant thermal hysteresis proteins, Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 1121(1-2) (1992) 199-206.
    • (1992) , vol.1121 , Issue.1-2 , pp. 199-206
    • Urrutia, M.E.1    Duman, J.G.2    Knight, C.A.3
  • 56
    • 0027058609 scopus 로고
    • A model for binding of an antifreeze polypeptide to ice
    • Wen D., Laursen R.A. A model for binding of an antifreeze polypeptide to ice. Biophysical Journal 1992, 63(6):1659-1662.
    • (1992) Biophysical Journal , vol.63 , Issue.6 , pp. 1659-1662
    • Wen, D.1    Laursen, R.A.2
  • 57
    • 74549175232 scopus 로고    scopus 로고
    • Comparison of functional properties of two fungal antifreeze proteins from Antarctomyces psychrotrophicus and Typhula ishikariensis
    • Xiao N., Suzuki K., Nishimiya Y., Kondo H., Miura A., Tsuda S., Hoshino T. Comparison of functional properties of two fungal antifreeze proteins from Antarctomyces psychrotrophicus and Typhula ishikariensis. FEBS Journal 2010, 277(2):394-403.
    • (2010) FEBS Journal , vol.277 , Issue.2 , pp. 394-403
    • Xiao, N.1    Suzuki, K.2    Nishimiya, Y.3    Kondo, H.4    Miura, A.5    Tsuda, S.6    Hoshino, T.7
  • 58
    • 0020447804 scopus 로고
    • Antifreeze effect of thermal hysteresis agents protects highly supercooled insects
    • Zachariassen K.E., Husby J.A. Antifreeze effect of thermal hysteresis agents protects highly supercooled insects. Nature 1982, 298(5877):865-867.
    • (1982) Nature , vol.298 , Issue.5877 , pp. 865-867
    • Zachariassen, K.E.1    Husby, J.A.2
  • 59
    • 0029917011 scopus 로고    scopus 로고
    • Linearization of the Bradford protein assay increases its sensitivity: theoretical and experimental studies
    • Zor T., Selinger Z. Linearization of the Bradford protein assay increases its sensitivity: theoretical and experimental studies. Analytical Biochemistry 1996, 236(2):302-308.
    • (1996) Analytical Biochemistry , vol.236 , Issue.2 , pp. 302-308
    • Zor, T.1    Selinger, Z.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.