메뉴 건너뛰기




Volumn 8, Issue 6, 1998, Pages 715-720

Evolution of the diverse antifreeze proteins

Author keywords

[No Author keywords available]

Indexed keywords

ANTIFREEZE PROTEIN; APOLIPOPROTEIN;

EID: 0031771585     PISSN: 0959437X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-437X(98)80042-7     Document Type: Article
Times cited : (122)

References (34)
  • 1
    • 0015219684 scopus 로고
    • Glycoproteins as biological antifreeze agents in Antarctic fishes
    • DeVries AL. Glycoproteins as biological antifreeze agents in Antarctic fishes. Science. 172:1971;1152-1155.
    • (1971) Science , vol.172 , pp. 1152-1155
    • Devries, A.L.1
  • 2
    • 0031026370 scopus 로고    scopus 로고
    • Amino acid sequence of a new type of antifreeze protein, from the longhorn sculpin Myoxocephalus octodecimspinosis
    • of outstanding interest. The authors report the discovery of a new type of fish AFP (type IV). It shares sequence similarity with members of the exchangeable apolioproteins super-family and is unrelated to the type I AFP in the sister species - short-horn and grubby sculpins.
    • Deng G, Andrews DW, Laursen RA. Amino acid sequence of a new type of antifreeze protein, from the longhorn sculpin Myoxocephalus octodecimspinosis. of outstanding interest FEBS Lett. 402:1997;17-20 The authors report the discovery of a new type of fish AFP (type IV). It shares sequence similarity with members of the exchangeable apolioproteins super-family and is unrelated to the type I AFP in the sister species - short-horn and grubby sculpins.
    • (1997) FEBS Lett , vol.402 , pp. 17-20
    • Deng, G.1    Andrews, D.W.2    Laursen, R.A.3
  • 3
    • 0002037107 scopus 로고
    • The role of antifreeze glycopeptides and peptides in the freezing avoidance of cold-water fish
    • di Prisco G. Berlin-Heidelberg: Springer-Verlag
    • Cheng CC, DeVries AL. The role of antifreeze glycopeptides and peptides in the freezing avoidance of cold-water fish. di Prisco G. Life Under Extreme Conditions. 1991;1-14 Springer-Verlag, Berlin-Heidelberg.
    • (1991) Life under Extreme Conditions , pp. 1-14
    • Cheng, C.C.1    Devries, A.L.2
  • 5
    • 0000286513 scopus 로고
    • Comparison of antifreeze glycopeptides from Arctic and Antarctic fishes
    • O'Grady SM, Schrag JD, Raymond JA, DeVries AL. Comparison of antifreeze glycopeptides from Arctic and Antarctic fishes. J Exp Zool. 224:1982;177-185.
    • (1982) J Exp Zool , vol.224 , pp. 177-185
    • O'Grady, S.M.1    Schrag, J.D.2    Raymond, J.A.3    Devries, A.L.4
  • 6
    • 0030970280 scopus 로고    scopus 로고
    • Evolution of antifreeze glycoprotein from a trypsinogen gene in Antarctic notothenioid fish
    • of outstanding interest. The origin of the notothenioid AFGP gene is determined. Sequence analyses show that the protease to AFGP conversion involved recruitment of the two ends of the protease gene and expansion of a 9 nt sequence in the middle to provide the new AFGP coding region.
    • Chen L, DeVries AL, Cheng CHC. Evolution of antifreeze glycoprotein from a trypsinogen gene in Antarctic notothenioid fish. of outstanding interest Proc Natl Acad Sci USA. 94:1997;3811-3816 The origin of the notothenioid AFGP gene is determined. Sequence analyses show that the protease to AFGP conversion involved recruitment of the two ends of the protease gene and expansion of a 9 nt sequence in the middle to provide the new AFGP coding region.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 3811-3816
    • Chen, L.1    Devries, A.L.2    Cheng, C.H.C.3
  • 7
    • 0030890706 scopus 로고    scopus 로고
    • Convergent evolution of antifreeze glycoproteins in Antarctic notothenioid fish and Arctic cod
    • of outstanding interest. Comparative sequence analyses are presented that strongly support a rare case of protein sequence convergence for the near-identical AFGPs in these two unrelated fishes inhabiting opposite poles of the Earth.
    • Chen L, DeVries AL, Cheng CHC. Convergent evolution of antifreeze glycoproteins in Antarctic notothenioid fish and Arctic cod. of outstanding interest Proc Natl Acad Sci USA. 94:1997;3817-3822 Comparative sequence analyses are presented that strongly support a rare case of protein sequence convergence for the near-identical AFGPs in these two unrelated fishes inhabiting opposite poles of the Earth.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 3817-3822
    • Chen, L.1    Devries, A.L.2    Cheng, C.H.C.3
  • 8
    • 0027551726 scopus 로고
    • Herring antifreeze protein: Primary structure and evidence for a C-type lectin evolutionary origin
    • Ewart KV, Fletcher GL. Herring antifreeze protein: primary structure and evidence for a C-type lectin evolutionary origin. Mol Mar Biol Biotech. 2:1993;20-27.
    • (1993) Mol Mar Biol Biotech , vol.2 , pp. 20-27
    • Ewart, K.V.1    Fletcher, G.L.2
  • 9
    • 0030760436 scopus 로고    scopus 로고
    • Hyperactive antifreeze protein from beetles
    • of special interest. First of three complete insect AFP sequences that were reported within months of each other. This Cys-rich repetitive mealworm AFP represents yet another new type in the antifreeze superfamily and is much more active than fish AFPS.
    • Graham LA, Liou LC, Walker VK, Davies PL. Hyperactive antifreeze protein from beetles. of special interest Nature. 388:1997;727-728 First of three complete insect AFP sequences that were reported within months of each other. This Cys-rich repetitive mealworm AFP represents yet another new type in the antifreeze superfamily and is much more active than fish AFPS.
    • (1997) Nature , vol.388 , pp. 727-728
    • Graham, L.A.1    Liou, L.C.2    Walker, V.K.3    Davies, P.L.4
  • 10
    • 0032054774 scopus 로고    scopus 로고
    • Molecular characterization and sequencing of antifreeze proteins from larvae of the beetle Dendroides canadensis
    • of special interest. This beetle larvae AFP shares high sequence identity with the mealworm AFP, and has the same repetitive structure, and thus belongs to the same type.
    • Duman JG, Li N, Verleye D, Goetz FW, Wu DW, Andorfer CA, Benjamin T, Parmelee DC. Molecular characterization and sequencing of antifreeze proteins from larvae of the beetle Dendroides canadensis. of special interest J Comp Physiol B. 168:1998;225-232 This beetle larvae AFP shares high sequence identity with the mealworm AFP, and has the same repetitive structure, and thus belongs to the same type.
    • (1998) J Comp Physiol B , vol.168 , pp. 225-232
    • Duman, J.G.1    Li, N.2    Verleye, D.3    Goetz, F.W.4    Wu, D.W.5    Andorfer, C.A.6    Benjamin, T.7    Parmelee, D.C.8
  • 11
    • 0030828487 scopus 로고    scopus 로고
    • The antifreeze potential of the spruce budworm thermal hysteresis protein
    • of special interest. This paper reports an AFP from a moth larva which, thought similar in amino acid bias as the beetle larvae AFPs, does not have a repeat sequence and thus may not be homologus to the latter.
    • Tyshenko MG, Doucet D, Davies PL, Walker VK. The antifreeze potential of the spruce budworm thermal hysteresis protein. of special interest Nat Biotechnol. 15:1997;887-890 This paper reports an AFP from a moth larva which, thought similar in amino acid bias as the beetle larvae AFPs, does not have a repeat sequence and thus may not be homologus to the latter.
    • (1997) Nat Biotechnol , vol.15 , pp. 887-890
    • Tyshenko, M.G.1    Doucet, D.2    Davies, P.L.3    Walker, V.K.4
  • 12
    • 0028232701 scopus 로고
    • Purification and characterization of a thermal hysteresis protein from a plant, the bittersweet nightshade Solanum dulacamara
    • Duman JG. Purification and characterization of a thermal hysteresis protein from a plant, the bittersweet nightshade Solanum dulacamara. Biochim Biophys Acta. 1206:1994;129-135.
    • (1994) Biochim Biophys Acta , vol.1206 , pp. 129-135
    • Duman, J.G.1
  • 13
    • 0029411516 scopus 로고
    • Antifreeze proteins in winter rye are similar to pathogenesis-related proteins
    • Hon WC, Griffith M, Mlynarz A, Kwok YC, Yang DS. Antifreeze proteins in winter rye are similar to pathogenesis-related proteins. Plant Physiol. 109:1995;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.5
  • 14
    • 0042183228 scopus 로고
    • Adsorption inhibition as a mechanism of freezing resistance in polar fishes
    • Raymond JA, DeVries AL. Adsorption inhibition as a mechanism of freezing resistance in polar fishes. Proc Natl Acad Sci USA. 74:1977;2589-2593.
    • (1977) Proc Natl Acad Sci USA , vol.74 , pp. 2589-2593
    • Raymond, J.A.1    Devries, A.L.2
  • 15
    • 0025959821 scopus 로고
    • Adsorption of α-helical antifreeze peptides on specific ice crystal surface planes
    • Knight CA, Cheng CC, DeVries AL. Adsorption of α-helical antifreeze peptides on specific ice crystal surface planes. Biophys J. 59:1991;409-418.
    • (1991) Biophys J , vol.59 , pp. 409-418
    • Knight, C.A.1    Cheng, C.C.2    Devries, A.L.3
  • 16
    • 0028761625 scopus 로고
    • Effects of a polymeric, non-equilibrium 'antifreeze' upon ice growth from water
    • Knight CA, DeVries AL. Effects of a polymeric, non-equilibrium 'antifreeze' upon ice growth from water. J Crystal Growth. 143:1994;301-310.
    • (1994) J Crystal Growth , vol.143 , pp. 301-310
    • Knight, C.A.1    Devries, A.L.2
  • 17
    • 0000814617 scopus 로고    scopus 로고
    • Structure determination of a lone α-helical antifreeze protein from winter flounder
    • Sichieri F, Yang DSC. Structure determination of a lone α-helical antifreeze protein from winter flounder. Acta Crystallogr D. 52:1996;486-498.
    • (1996) Acta Crystallogr D , vol.52 , pp. 486-498
    • Sichieri, F.1    Yang, D.S.C.2
  • 18
    • 0032485929 scopus 로고    scopus 로고
    • Mapping of disulfide bridges in antifreeze proteins from overwintering larvae of the beetle Dendroides canadensis
    • of outstanding interest. Exhaustive peptide fragment analyses are here used to identify the disulfide linkages of all the 16 Cys residues in this AFP, laying the ground work for future structural and mechanistic studies.
    • Li N, Chibber BAK, Castellino FJ, Duman JG. Mapping of disulfide bridges in antifreeze proteins from overwintering larvae of the beetle Dendroides canadensis. of outstanding interest Biochemistry. 37:1998;6343-6350 Exhaustive peptide fragment analyses are here used to identify the disulfide linkages of all the 16 Cys residues in this AFP, laying the ground work for future structural and mechanistic studies.
    • (1998) Biochemistry , vol.37 , pp. 6343-6350
    • Li, N.1    Chibber, B.A.K.2    Castellino, F.J.3    Duman, J.G.4
  • 19
    • 0023943675 scopus 로고
    • The apolipoprotein multigene family: Biosynthesis, structure, structure-function relationships, and evolution
    • Li WH, Tanimura M, Luo CC, Datta S, Chan L. The apolipoprotein multigene family: biosynthesis, structure, structure-function relationships, and evolution. J Lipid Res. 29:1988;245-271.
    • (1988) J Lipid Res , vol.29 , pp. 245-271
    • Li, W.H.1    Tanimura, M.2    Luo, C.C.3    Datta, S.4    Chan, L.5
  • 20
    • 0030732162 scopus 로고    scopus 로고
    • Crystal structure of truncated human apolipoprotein A-I suggests a lipid-bound conformation
    • Borhani W, Rogers DP, Engler JA, Brouillette CG. Crystal structure of truncated human apolipoprotein A-I suggests a lipid-bound conformation. Proc Natl Acad Sci USA. 94:1997;12291-12296.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 12291-12296
    • Borhani, W.1    Rogers, D.P.2    Engler, J.A.3    Brouillette, C.G.4
  • 21
    • 0025860481 scopus 로고
    • Three-dimensional structure of the LDL receptor binding domain of human apolipoprotein E
    • Wilson C, Wardell MR, Weisgraber KH, Mahley RW, Agard DA. Three-dimensional structure of the LDL receptor binding domain of human apolipoprotein E. Science. 252:1991;1817-1822.
    • (1991) Science , vol.252 , pp. 1817-1822
    • Wilson, C.1    Wardell, M.R.2    Weisgraber, K.H.3    Mahley, R.W.4    Agard, D.A.5
  • 22
    • 0032492659 scopus 로고    scopus 로고
    • The solution structure of type II antifreeze protein reveals a new member of the lectin family
    • of outstanding interest. The paper reports the first NMR solution structure sea raven type II AFP confirming a global fold homologous to the C-type lectins and pancreatic stone proteins. It lays the ground work for identifying the putative ice-binding residues of fish type II AFPs and the structural basis for the binding of ice.
    • Gronwald W, Loewen MC, Lix B, Daugulis A, Sönnichsen F, Davies PL, Sykes BD. The solution structure of type II antifreeze protein reveals a new member of the lectin family. of outstanding interest Biochemistry. 37:1998;4712-4721 The paper reports the first NMR solution structure sea raven type II AFP confirming a global fold homologous to the C-type lectins and pancreatic stone proteins. It lays the ground work for identifying the putative ice-binding residues of fish type II AFPs and the structural basis for the binding of ice.
    • (1998) Biochemistry , vol.37 , pp. 4712-4721
    • Gronwald, W.1    Loewen, M.C.2    Lix, B.3    Daugulis, A.4    Sönnichsen, F.5    Davies, P.L.6    Sykes, B.D.7
  • 23
    • 0026772705 scopus 로고
    • Structural and functional similarity between fish antifreeze proteins and calcium-dependent lectins
    • Ewart KV, Rubinsky B, Fletcher GL. Structural and functional similarity between fish antifreeze proteins and calcium-dependent lectins. Biochem Biophys Res Comm. 185:1992;335-340.
    • (1992) Biochem Biophys Res Comm , vol.185 , pp. 335-340
    • Ewart, K.V.1    Rubinsky, B.2    Fletcher, G.L.3
  • 24
    • 0001044156 scopus 로고    scopus 로고
    • The ice binding site of Atlantic herring antifreeze protein corresponds to the carbohydrate-binding site of C-type lectins
    • 2+-dependent type II fish AFP is localized by site-directed mutagenesis to the sequence segment that is homologous to the carbohydrate-binding site of its evolutionary precursor, the C-type lectins.
    • 2+-dependent type II fish AFP is localized by site-directed mutagenesis to the sequence segment that is homologous to the carbohydrate-binding site of its evolutionary precursor, the C-type lectins.
    • (1998) Biochemistry , vol.37 , pp. 4080-4085
    • Vanda Ewart, K.1    Li, Z.2    Yang, D.S.C.3    Fletcher, G.L.4    Hew, C.L.5
  • 28
    • 0027983037 scopus 로고
    • Convergent evolution: The need to be explicit
    • Doolittle RF. Convergent evolution: the need to be explicit. Trends Biochem Sci. 19:1994;15-18.
    • (1994) Trends Biochem Sci , vol.19 , pp. 15-18
    • Doolittle, R.F.1
  • 29
    • 0000523437 scopus 로고
    • Cenozoic evolution of Antarctic glaciation, the Circum-Antarctic Ocean, and their impact on global paleoceanography
    • Kennett JP. Cenozoic evolution of Antarctic glaciation, the Circum-Antarctic Ocean, and their impact on global paleoceanography. J Geophy Res. 82:1977;3843-3859.
    • (1977) J Geophy Res , vol.82 , pp. 3843-3859
    • Kennett, J.P.1
  • 30
    • 0029668470 scopus 로고    scopus 로고
    • Evolution and adaptive radiation of antarctic fishes
    • Clarke A, Johnston IA. Evolution and adaptive radiation of antarctic fishes. Trends Ecol Evol. 11:1996;212-218.
    • (1996) Trends Ecol Evol , vol.11 , pp. 212-218
    • Clarke, A.1    Johnston, I.A.2
  • 32
    • 0028135688 scopus 로고
    • Molecular evolution at subzero temperature: Mitochondrial and nuclear phylogenies of fishes from Antarctica (suborder Notothenioidei), and the evolution of antifreeze glycopeptides
    • Bargelloni L, Ritchie PA, Patarnello T, Battaglia B, Lambert DM, Meyer A. Molecular evolution at subzero temperature: mitochondrial and nuclear phylogenies of fishes from Antarctica (suborder Notothenioidei), and the evolution of antifreeze glycopeptides. Mol Biol Ecol. 11:1994;854-863.
    • (1994) Mol Biol Ecol , vol.11 , pp. 854-863
    • Bargelloni, L.1    Ritchie, P.A.2    Patarnello, T.3    Battaglia, B.4    Lambert, D.M.5    Meyer, A.6
  • 34
    • 0031419161 scopus 로고    scopus 로고
    • Quaternary history of sea ice and peleoclimate in the Amerasia basin, Arctic Ocean, as recorded in the cyclical strata of Northwind Ridge
    • Phillips RL, Grants A. Quaternary history of sea ice and peleoclimate in the Amerasia basin, Arctic Ocean, as recorded in the cyclical strata of Northwind Ridge. Geol Soc Am Bull. 109:1997;1110-1115.
    • (1997) Geol Soc Am Bull , vol.109 , pp. 1110-1115
    • Phillips, R.L.1    Grants, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.