Antifreeze proteins

Current Opinion in Structural Biology

Volumn 7, Issue 6, 1997, Pages 828-834

  Davies, Peter L ^a   Sykes, Brian D ^b  

^a QUEEN S UNIVERSITY   (Canada)

^b UNIVERSITY OF ALBERTA   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

ANTIFREEZE PROTEIN; ICE;

FISH; MOLECULAR MODEL; NONHUMAN; PRIORITY JOURNAL; PROTEIN STRUCTURE; PROTEIN TERTIARY STRUCTURE; REVIEW; STRUCTURE ACTIVITY RELATION;

EID: 0031467812     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(97)80154-6     Document Type: Article

References (37)

1. Yeh Y, Feeney RE. Antifreeze proteins: structures and mechanisms of function. of special interest Chem Rev. 96:1996;601-617 A comprehensive review of fish AFPs with an emphasis on the mathematical treatment of freezing-point depression.
2. Knight CA, Cheng CC, DeVries AL. Adsorption of α-helical antifreeze peptides on specific ice crystal surface planes. Biophys J. 59:1991;409-418.
3. Knight CA, DeVries AL, Oolman LD. Fish antifreeze protein and the freezing and recrystallization of ice. Nature. 308:1984;295-296.
4. Sun X, Griffith M, Pasternak JJ, Glick BR. Low temperature growth, freezing survival, and production of antifreeze protein by the plant growth promoting rhizobacterium Pseudomonas putida GR12-2. Can J Microbiol. 41:1995;776-784.
5. 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 new AFP-type described is a homolog of four helix bundle proteins. Although longhorn and shorthorn sculpins are very close relatives, the latter produces the single-type I AFP.
6. 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.
7. Graham LA, Liou L-C, Walker VK, Davies PL. Hyperactive antifreeze protein from beetles. of special interest Nature. 388:1997;727-728 This paper reports that insect AFPs can have up to 100 times the specific activity of fish AFPs, but that they still work by an adsorption/inhibition mechanism.
8. 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 The purification, sequence and expression of an insect AFP is described. Its thermal hysteresis activity is much greater than that obtained with fish AFPs, and its effects on ice crystal morphology are significantly different.
9. Sicheri F, Yang DSC. Ice-binding structure and mechanism of an antifreeze protein from winter flounder. Nature. 375:1995;427-431.
10. Davies PL, Hew CL. Biochemistry of fish antifreeze proteins. FASEB J. 4:1990;2460-2468.
11. Chao H, Hodges RS, Kay CM, Gauthier SY, Davies PL. A natural variant of type I antifreeze protein with four ice-binding repeats is a particulary potent antifreeze. of special interest Protein Sci. 5:1996;1150-1156 A larger AFP isoform with an additional repeat and a different 'ice-binding motif' shows enhanced antifreeze activity.
12. Cheng CC, DeVries AL. The role of antifreeze glycopeptides and peptides in the freezing avoidance of cold-water fish. di Prisco G. In Life Under Extreme Conditions. 1991;1-14 Springer-Verlag.
13. Gong Z, Ewart KV, Hu Z, Fletcher GL, Hew CL. Skin antifreeze protein genes of the winter flounder, Pleuronectes americanus, encode distinct and active polypeptides without the secretory signal and prosequences. of outstanding interest J Biol Chem. 271:1996;4106-4112 This paper explains earlier results on the tissue-specific expression of type 1 AFP. Two subtypes are present in this fish, and the skin subtype appears not to be exported to the circulation.
14. Davies PL, Gauthier SY. Antifreeze protein pseudogenes. Gene. 112:1992;171-178.
15. 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.
16. Sönnichsen FD, Sykes BD, Davies Pl. Comparative modeling of the three-dimensional structure of type II antifreeze protein. Protein Sci. 4:1995;460-471.
17. 2+-dependent lectins. Different divalent metal ions have dramatically different effects on AFP activity and ice crystal morphology.
18. Weis WI, Drickamer K, Henderson WA. Structure of a C-type mannose-binding protein complexed with an oligosaccharide. Nature. 360:1992;127-134.
19. Chao H, DeLuca CI, Davies PL. Mixing antifreeze protein types changes ice crystal morphology without affecting antifreeze activity. FEBS Lett. 357:1995;183-186.
20. Bertrand JA, Pignol D, Bernard JP, Verdier JM, Dagorn JC, Fontecilla-Camps JC. Crystal structure of human lithostathine, the pancreatic inhibitor of stone formation. EMBO J. 15:1996;2678-2684.
21. Patard L, Stoven V, Gharib B, Bontems F, Lallemand J-Y, De Reggi M. What function for human lithostathine? Structural investigations by three-dimensional structure modeling and high resolution NMR spectroscopy. Protein Eng. 9:1996;949-957.
22. Scott GK, Fletcher GL, Davies PL. Fish antifreeze proteins: recent gene evolution. Can J Fish Aquatic Sci. 43:1986;1028-1034.
23. Davies PL, Ewart KV, Fletcher GL. The diversity and distribution of fish antifreeze proteins: new insights into their origins. Mommsen TP, Hochachka PW. In Fish Biochemistry and Molecular Biology. 2:1993;279-291 Elsevier, Amsterdam.
24. 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 Evidence is presented for the recent evolution of notothenioid AFGPs on the basis of recruitment of a trypsinogen gene to provide the noncoding regions and internal amplication of the tripeptide coding sequence.
25. Logsdon JM, Doolittle WF. Origin of antifreeze protein genes: a cool tale in molecular evolution. Proc Natl Acad Sci USA. 94:1997;3485-3487.
26. 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 A fascinating comparison of AFGP genes from fish that are poles apart in their phylogenetic relationships furnishes evidence for a most remarkable example of convergent evolution.
27. Sicheri F, Yang DSC. Structure determination of a lone α-helical antifreeze protein from winter flounder. of outstanding interest Acta Crystallogr D. 52:1996;486-498 The high-resolution X-ray structure of type I AFP [9] is the basis for defining regularly spaced rigid ice-binding motifs along a flat helix and for their proposed match to the ice lattice.
28. Gronwald W, Chao H, Reddy DV, Davies PL, Sykes BD, Sönnichsen FD. NMR characterization of side chain flexibility and backbone structure in the type I antifreeze protein at near freezing temperatures. of special interest Biochemistry. 35:1996;16698-16704 In solution, the putative ice-binding threonines on the helical AFP are shown to be free to sample all rotamer positions.
29. Jia Z, DeLuca CI, Chao H, Davies PL. Structural basis for the binding of a globular antifreeze protein to ice. of outstanding interest Nature. 384:1996;285-288 The 1.5 Å resolution X-ray structure of type III AFP reveals a potential hydrogen bonding match to the prism ice surface. A model for incremental binding is proposed whereby AFP contacts with ice help shape the binding site.
30. Sönnichsen FD, Sykes BD, Chao H, Davies PL. The nonhelical structure of antifreeze protein type III. Science. 259:1993;1154-1157.
31. DeLuca CI, Chao H, Sönnichsen FD, Sykes BD, Davies PL. Effect of type III antifreeze protein dilution and mutation on the growth inhibition of ice. Biophys J. 71:1996;2346-2355.
32. Sönnichsen FD, DeLuca CI, Davies PL, Sykes BD. Refined solution structure of type III antifreeze protein: hydrophobic group may be involved in the energetics of the protein-ice interaction. of outstanding interest Structure. 4:1996;1325-1337 This paper challenges the dominance of the hydrogen-bonding contribution to the energetics of AFP binding to ice and suggests that van der Waals interactions and entropic effects also play an important role.
33. 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.
34. Wang J, Gagne SM, Sykes BD, Ryan RO. Insight into lipid surface recognition and reversible conformational adaptations of an exchangeable apolipoprotein by multidimensional heteronuclear NMR techniques. J Biol Chem. 272:1997;17912-17920.
35. Myers KM, Pace CN. Hydrogen bonding stabilizes globular proteins. Biophys J. 71:1996;2033-2039.
36. Wierzbicki A, Taylor MS, Knight CA, Madura JD, Harrington JP, Sikes CS. Analysis of shorthorn sculpin antifreeze protein stereospecific binding to (2-10) faces of ice. of special interest Biophys J. 71:1996;8-18 A sophisticated computer modeling study of the nonrepetitive type I AFP binding to the ice surface identified by etching techniques.
37. Wang X, DeVries AL, Cheng CHC. Antifreeze peptide heterogeneity in an arctic eel pout includes an unusually large major variant comprised of two 7 kDa III AFPs linked in tandem. Biochim Biophys Acta. 1247:1995;163-172.