Cloning, expression, and activity of type IV antifreeze protein from cultured subtropical olive flounder (Paralichthys olivaceus)
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Antifreeze proteins (AFPs) lower the freezing point but not the melting point of aqueous solutions by inhibiting the growth of ice crystals via an adsorption-inhibition mechanism. However, the function of type IV AFP (AFP IV) is questionable, as its antifreeze activity is on the verge of detectable limits, its physiological concentration in adult fish blood is too low to function as a biological antifreeze, and its homologues are present even in fish from tropic oceans as well as freshwater. Therefore, we speculated that AFP IV may have gained antifreeze activity not by selective pressure but by chance. To test this hypothesis, we cloned, expressed, and assayed AFP IV from cultured subtropical olive flounder (Paralichthys olivaceus), which do not require antifreeze protein for survival. Among the identified expressed sequence tags of the flounder liver sample, a 5′-deleted complementary DNA (cDNA) sequence similar to the afp4 gene of the longhorn sculpin was identified, and its full-length cDNA and genome structure were examined. The deduced amino acid sequence of flounder AFP IV shared 55, 53, 52, and 49 % identity with those of Pleuragramma antarcticum, Myoxocephalus octodecemspinosus, Myoxocephalus scorpius, and Notothenia coriiceps, respectively. Furthermore, the genomic structure of this gene was conserved with those of other known AFP IVs. Notably, the recombinant AFP IV showed a weak but distinct thermal hysteresis of 0.07 ± 0.01 °C at the concentration of 0.5 mg/mL, and ice crystals in an AFP IV solution grew star-shaped, which are very similar to those obtained from other polar AFP IVs. Taken together, our results do not support the hypothesis of evolution of AFP IV by selective pressure, suggesting that the antifreeze activity of AFP IV may have been gained by chance.
Abstract
Antifreeze proteins (AFPs) lower the freezing point but not the melting point of aqueous solutions by inhibiting the growth of ice crystals via an adsorption-inhibition mechanism. However, the function of type IV AFP (AFP IV) is questionable, as its antifreeze activity is on the verge of detectable limits, its physiological concentration in adult fish blood is too low to function as a biological antifreeze, and its homologues are present even in fish from tropic oceans as well as freshwater. Therefore, we speculated that AFP IV may have gained antifreeze activity not by selective pressure but by chance. To test this hypothesis, we cloned, expressed, and assayed AFP IV from cultured subtropical olive flounder (Paralichthys olivaceus), which do not require antifreeze protein for survival. Among the identified expressed sequence tags of the flounder liver sample, a 5′-deleted complementary DNA (cDNA) sequence similar to the afp4 gene of the longhorn sculpin was identified, and its full-length cDNA and genome structure were examined. The deduced amino acid sequence of flounder AFP IV shared 55, 53, 52, and 49 % identity with those of Pleuragramma antarcticum, Myoxocephalus octodecemspinosus, Myoxocephalus scorpius, and Notothenia coriiceps, respectively. Furthermore, the genomic structure of this gene was conserved with those of other known AFP IVs. Notably, the recombinant AFP IV showed a weak but distinct thermal hysteresis of 0.07 ± 0.01 °C at the concentration of 0.5 mg/mL, and ice crystals in an AFP IV solution grew star-shaped, which are very similar to those obtained from other polar AFP IVs. Taken together, our results do not support the hypothesis of evolution of AFP IV by selective pressure, suggesting that the antifreeze activity of AFP IV may have been gained by chance.
참고문헌 (29)
- Bendtsen JD, "Improved prediction of signal peptides: SignalP 3.0", J Mol Biol, 340, pp.783~795 (2004)
- Breton TS, "Identification of ovarian gene expression patterns during vitellogenesis in Atlantic cod(Gadus morhua)", Gen Comp Endocrinol, 179, pp.296~304 (2012)
- Cheng CH, "Evolution of the diverse antifreeze proteins", Curr Opin Genet Dev, 8, pp.715~720 (1998)
- Cheng CC, "Encyclopedia of life support systems (EOLSS)—theme 6.73 extremophiles, developed under the auspices of the UNESCO" (2003), Eolss Publishers
- Cheng CH, "Evolution of an antifreeze glycoprotein", Nature, 401, pp.443~444 (1999)
- Cheng CH, "Functional antifreeze glycoprotein genes in temperate-water New Zealand notothenioid fish infer an Antarctic evolutionary origin", Mol Biol Evol, 20, pp.1897~1908 (2003)
- Choudhury M, "Homologue of mammalian apolipoprotein A-II in non-mammalian vertebrates", Acta Biochim Biophys Sin(Shanghai), 41, pp.370~378 (2009)
- Davies PL, "Biochemistry of fish antifreeze proteins", FSSEB J, 4, pp.2460~2468 (1990)
- Deng G, "Isolation and characterization of an antifreeze protein from the longhorn sculpin, Myoxocephalus octodecimspinosis", Biochim Biophys Acta, 1388, pp.305~314 (1998)
- Deng G, "Amino acid sequence of a new type of antifreeze protein, from the longhorn sculpin Myoxocephalus octodecimspinosis", FEBS Lett, 402, pp.17~20 (1997)
- DeVries AL, "Glycoproteins as biological antifreeze agents in Antarctic fishes", Science, 172, pp.1152~1155 (1971)
- DeVries AL, "Freezing resistance in some Antarctic fishes", Science, 163, pp.1073~1075 (1969)
- Fletcher GL, "Antifreeze proteins of teleost fishes", Annu Rev Physiol, 63, pp.359~390 (2001)
- Gauthier SY, "A re-evaluation of the role of type IV antifreeze protein", Cryobiology, 57, pp.292~296 (2008)
- Goetz FW, "Using global genome approaches to address problems in cod mariculture", ICES J Marine Sci, 63, pp.393~399 (2006)
- Graham LA, "Lateral transfer of a lectin-like antifreeze protein gene in fishes", PLoS One, 3, pp.e2616~ (2008)
- Graham LA, "Helical antifreeze proteins have independently evolved in fishes on four occasions", PLoS One, 8, pp.e81285~ (2013)
- Jia Z, "Antifreeze proteins : an unusual receptor-ligand interaction", Trends Biochem Sci, 27, pp.101~106 (2002)
- 김학준, "Antifreeze Activity in Temperate Fish from the East Sea, Korea", Fisheries and Aquatic Sciences, 18(2), pp.137~142 (2015), 한국수산과학회
- Larkin MA, "ClustalW and ClustalX version 2", Bioinformatics, 23, pp.2947~2948 (2007)
- Lee JK, "Molecular and comparative analyses of type IV antifreeze proteins(AFPIVs)from two Antarctic fishes, Pleuragramma antarcticum and Notothenia coriiceps", Comp Biochem Physiol B Biochem Mol Biol, 159, pp.197~205 (2011)
- Liu JX, "Molecular characterization and expression pattern of AFPIV during embryogenesis in gibel carp(Carassiu auratus gibelio)", Mol Biol Rep, 36, pp.2011~2018 (2009)
- Nishimiya Y, "Mass preparation and technological development of an antifreeze protein", Synthesiology(Engl ed), 1, pp.7~14 (2008)
- Raymond JA, "Adsorption inhibition as a mechanism of freezing resistance in polar fishes", Proc Natl Acad Sci U S A, 74, pp.2589~2593 (1977)
- Wang Y, "Apolipoprotein C1 regulates epiboly during gastrulation in zebrafish", Sci China Life Sci, 56, pp.975~984 (2013)
- Xia JH, "Apo-14 is required for digestive system organogenesis during fish embryogenesis and larval development", Int J Devel Biol, 52, pp.1089~1098 (2008)
- Xiao Q, "Type-IV antifreeze proteins are essential for epiboly and convergence in gastrulation of zebrafish embryos", Int J Biol Sci, 10, pp.715~732 (2014)
- Zhang T, "ApoA-II directs morphogenetic movements of zebrafish embryo by preventing chromosome fusion during nuclear division in yolk syncytial layer", J Biol Chem, 286, pp.9514~9525 (2011)
- Zhao Z, "Cloning and sequencing of cDNA encoding the LS-12 antifreeze protein in the longhorn sculpin, Myoxocephalus octodecimspinosis", Biochim Biophys Acta, 1382, pp.177~180 (1998)