Thermal stability properties of an antifreeze protein from the desert beetle Microdera punctipennis

Cryobiology

Volumn 60, Issue 2, 2010, Pages 192-197

  Qiu, Li Ming ^a   Ma, Ji ^a   Wang, Jing ^a   Zhang, Fu Chun ^a   Wang, Yan ^a  

^a XINJIANG UNIVERSITY   (China)

Author keywords

Heat incubation; Insect antifreeze protein; Microdera punctipennis; Thermal hysteresis; Thermostability

Indexed keywords

ANTIFREEZE PROTEIN;

AMINO ACID SEQUENCE; ARTICLE; BEETLE; CONTROLLED STUDY; ESCHERICHIA COLI; HYSTERESIS; INCUBATION TEMPERATURE; MICRODERA PUNCTIPENNIS; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN EXPRESSION; PROTEIN PURIFICATION; PROTEIN STRUCTURE; SEQUENCE HOMOLOGY; THERMOSTABILITY; WESTERN BLOTTING;

AMINO ACID SEQUENCE; ANIMALS; ANTIFREEZE PROTEINS; BASE SEQUENCE; BEETLES; DNA PRIMERS; GENES, INSECT; INSECT PROTEINS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; PROTEIN STABILITY; RECOMBINANT FUSION PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; STRUCTURAL HOMOLOGY, PROTEIN; THERMODYNAMICS;

COLEOPTERA; ESCHERICHIA COLI; HEXAPODA; MICRODERA;

EID: 77349092010     PISSN: 00112240     EISSN: 10902392     Source Type: Journal    
DOI: 10.1016/j.cryobiol.2009.10.014     Document Type: Article

References (36)

1. Barrett J. Thermal hysteresis proteins. Int. J. Biochem. Cell B 33 (2001) 105-117
2. Breton G., Danyluk J., Ouellet F., and Sarhan F. Biotechnological applications of plant freezing associated proteins. Biotechnol. Annu. Rev. 6 (2000) 59-101
3. Cheng C.H.C., and DeVries A.L. Structures of antifreeze peptides from the Antarctic eel pout, Austrolycicthys brachycephalus. Biochim. Biophys. Acta 997 (1989) 55-64
4. Chilkoti A., Dreher M.R., and Meyer D.E. Design of thermally responsive, recombinant polypeptide carriers for targeted drug delivery. Adv. Drug. Deliv. Rev. 54 (2002) 1093-1111
5. DeVries A.L. Glycoproteins as biological antifreeze agents in Antarctic fishes. Science 172 (1971) 1152-1155
6. DeVries A.L. Role of glycopeptides and peptides in inhibition of crystallization of water in polar fishes. Philos. Trans. R. Soc. B 304 (1984) 575-588
7. DeVries A.L. Antifreeze glycopeptides and peptides: interactions with ice and water. Methods Enzymol. 127 (1986) 293-303
8. Fiske Associates. Fiske Micro-Osmometer Model 210 User's Guide (2002), Norwood, Massachusetts, USA pp. xii-xiv
9. Graether S.P., and Sykes B.D. Cold survival in freeze-intolerant insects: the structure and function of β-helical antifreeze proteins. Eur. J. Biochem. 271 (2004) 3285-3296
10. Graether S.P., Kuiper M.J., Gagné S.M., Walker V.K., Jia Z., Sykes B.D., and Davies P.L. Beta-helix structure and ice-binding properties of a hyperactive antifreeze protein from an insect. Nature 406 (2000) 325-328
11. Griffith M., and Ewart K.V. Antifreeze proteins and their potential use in frozen foods. Biotechnol. Adv. 13 (1995) 375-402
12. Harding M.M., Anderberg P.I., and Haymet A.D.J. 'Antifreeze' glycoproteins from polar fish [Review]. Eur. J. Biochem. 270 (2003) 1381-1392
13. Hew C.L., and Yang D.S.C. Protein interaction with ice. Invited review. Eur. J. Biochem. 203 (1992) 33-42
14. Huang H., Liu J., and De Marco A. Induced fit of passenger proteins fused to Archaea maltose binding proteins. Biochem. Biophys. Res. Commun. 344 (2006) 25-29
15. Kaiser J. New prospects for putting organs on ice. Science 295 (2002) 1015
16. Kawahara H., Iwanaka Y., Higa S., Muryoi N., Sato M., Honda M., Omura H., and Obata H. A novel, intracellular antifreeze protein in an antarctic bacterium, Flavobacterium xanthum. CryoLetters 28 1 (2007) 39-49
17. Kundu S., and Roy D. Comparative structural studies of psychrophilic, mesophilic protein homologues by molecular dynamics simulation. J. Mol. Graphics Modell. 27 (2009) 871-880
18. Li X., and Hew C.L. Structure and function of an antifreeze polypeptide from ocean pout, Macrozoarces americanus: role of glutamic acid residues in protein stability and antifreeze activity by site-directed mutagenesis. Protein Eng. 4 (1991) 1003-1008
19. Li X., Trinh K.Y., and Hew C.L. 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 (1991) 995-1002
20. Li N., Andorfer C.A., and Duman J.G. Enhancement of insect antifreeze protein activity by solutes of low molecular mass. J. Exp. Biol. 201 (1998) 2243-2251
21. Li N., Chibber B., Castellino F.J., and Duman J.G. Mapping of the disulfide bridges in antifreeze proteins from overwintering larvae of the beetle Dendroides canadensis. Biochemistry 37 (1998) 6343-6350
22. Li S.L., Zhang F.C., Sun L.J., Liu X., and Ma J. Comparison of activities of fusion antifreeze proteins from Microdera punctipenis dzunarica (Coleoptera: Tenebrionidae). Acta Entomol. Sin. 51 (2008) 694-699
23. Marcoa A.D., Casatta E., Savaresi S., and Geerlof A. Recombinant proteins fused to thermostable partners can be purified by heat incubation. J. Biotechnol. 107 (2004) 125-133
24. Marshall C.B., Chakrabartty A., and Davies P.L. Hyperactive antifreeze protein from winter flounder is a very long rod-like dimer of α-helices. J. Biol. Chem. 280 (2005) 17920-17929
25. Meyer D.E., and Chilkoti A. Purification of recombinant proteins by fusion with thermally-responsive polypeptides. Nat. Biotechnol. 17 (1999) 1112-1115
26. Nguyen D.H., Colvin M.E., Yeh Y., Feeney R.E., and Fink W.H. The dynamics, structure, and conformational free energy of proline-containing antifreeze glycoprotein. Biophys. J. 82 (2002) 2892-2905
27. Nosoh Y., and Sekiguchi T. Protein engineering for thermostability. Trends. Biotechnol. 8 (1990) 16-20
28. Olga G.A., Mateo R., Tomczak M.M., Davies P.L., and Mateu M.G. Thermodynamic stability of a cold-adapted protein type III antifreeze protein, and energetic contribution of salt bridges. Protein Sci. 16 (2007) 227-238
29. Park S.M., Jung H.Y., Chung K.C., Rhim H., Park J.H., and Kim J. Stress-induced aggregation profiles of GST-alpha-synuclein fusion proteins: role of the C-terminal acidic tail of alpha-synuclein in protein thermosolubility and stability. Biochemistry 41 (2002) 4137-4146
30. Park S.M., Ahn K.J., Jung H.Y., Park J.H., and Kim J. Effects of novel peptides derived from the acidic tail of synuclein (ATS) on the aggregation and stability of fusion proteins. Protein Eng. Des. Sel. 17 (2004) 251-260
31. Rahman R.N., Leow T.C., Basrib M., and Salleh A.B. Secretory expression of thermostable T1 lipase through bacteriocin release protein. Protein Expr. Purif. 40 (2005) 411-416
32. Salvay A.G., Santos J., and Howard E.I. Electro-optical properties characterization of fish type III antifreeze protein. J. Biol. Phys. 33 (2007) 389-397
33. Sørensen H.P., Sperling-Petersen H.U., and Mortensen K.K. Production of recombinant thermostable proteins expressed in Escherichia coli: completion of protein synthesis is the bottleneck. J. Chromatogr. B 786 (2003) 207-214
34. Tsvetkova N.M., Phillips B.L., Krishnan V.V., Feeney R.E., Fink W.H., Crowe J.H., Risbud S.H., Tablin F., and Yeh Y. Dynamics of antifreeze glycoproteins in the presence of ice. Biophys. J. 82 (2002) 464-473
35. Wharton D.A., Barrett J., Goodall G., Marshall C.J., and Ramløv H. Ice-active proteins from the Antarctic nematode Panagrolaimus davidi. Cryobiology 51 (2005) 198-207
36. Zhao G., Ma J., Xue N., Yang C.G., Zhuan F.F., and Zhang F.C. Cloning of a cDNA encoding antifreeze protein in Microdera punctipenis dzunarica (Coleoptera: Tenebrionidae) and its activity assay. Acta Entomol. Sin. 48 (2005) 667-673