| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
|
|
|
|||||||
|
|||||||||
The FASEB Journal, Vol 4, 2460-2468, Copyright © 1990 by The Federation of American Societies for Experimental Biology
REVIEWS |
PL Davies and CL Hew
Department of Biochemistry, Queen's University, Kingston, Ontario, Canada.
Four distinct macromolecular antifreezes have been isolated and characterized from different marine fish. These include the glycoprotein antifreezes (Mr 2.5-33 K), which are made up of a repeating tripeptide (Ala-Ala-Thr)n with a disaccharide attached to the threonyl residues, and three antifreeze protein (AFP) types. Type I is an alanine-rich, amphiphilic, alpha-helix (Mr 3-5 K); type II is a larger protein (Mr 14 K) with a high content of reverse turns and five disulfide bridges; and type III is intermediate in size (Mr 6-7 K) with no distinguishing features of secondary structure or amino acid composition. Despite their marked structural differences, all four antifreeze types appear to function in the same way by binding to the prism faces of ice crystals and inhibiting growth along the a-axes. It is suggested that type I AFP binds preferentially to the prism faces as a result of interactions between the helix macrodipole and the dipoles on the water molecules in the ice lattice. Binding is stabilized by hydrogen bonding, and the amphiphilic character of the helix results in the hydrophobic phase of the helix being exposed to the solvent. When the solution temperature is lowered further, ice crystal growth occurs primarily on the uncoated, unordered basal plane resulting in bipyramidal-shaped crystals. The structural features of type I AFP that could contribute to this mechanism of action are reviewed. Current challenges lie in solving the other antifreeze structures and interpreting them in light of what appears to be a common mechanism of action.
This article has been cited by other articles:
|
|
 |
|
  O. Garcia-Arribas, R. Mateo, M. M. Tomczak, P. L. Davies, and M. G. Mateu Thermodynamic stability of a cold-adapted protein, type III antifreeze protein, and energetic contribution of salt bridges Protein Sci., February 1, 2007; 16(2): 227 - 238. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 Y. Mao and Y. Ba Insight into the Binding of Antifreeze Proteins to Ice Surfaces via 13C Spin Lattice Relaxation Solid-State NMR Biophys. J., August 1, 2006; 91(3): 1059 - 1068. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 C. B. Marshall, A. Chakrabartty, and P. L. Davies Hyperactive Antifreeze Protein from Winter Flounder Is a Very Long Rod-like Dimer of {alpha}-Helices J. Biol. Chem., May 6, 2005; 280(18): 17920 - 17929. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 N. Muryoi, M. Sato, S. Kaneko, H. Kawahara, H. Obata, M. W. F. Yaish, M. Griffith, and B. R. Glick Cloning and Expression of afpA, a Gene Encoding an Antifreeze Protein from the Arctic Plant Growth-Promoting Rhizobacterium Pseudomonas putida GR12-2 J. Bacteriol., September 1, 2004; 186(17): 5661 - 5671. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
X. Y. Liu and N. Du Zero-sized Effect of Nano-particles and Inverse Homogeneous Nucleation: PRINCIPLES OF FREEZING AND ANTIFREEZE J. Biol. Chem., February 13, 2004; 279(7): 6124 - 6131. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
N. Du, X. Y. Liu, and C. L. Hew Ice Nucleation Inhibition: MECHANISM OF ANTIFREEZE BY ANTIFREEZE PROTEIN J. Biol. Chem., September 19, 2003; 278(38): 36000 - 36004. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
M. E. Daley and B. D. Sykes The role of side chain conformational flexibility in surface recognition by Tenebrio molitor antifreeze protein Protein Sci., July 1, 2003; 12(7): 1323 - 1331. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
W. Zhang and R. A. Laursen Structure-Function Relationships in a Type I Antifreeze Polypeptide. THE ROLE OF THREONINE METHYL AND HYDROXYL GROUPS IN ANTIFREEZE ACTIVITY J. Biol. Chem., December 25, 1998; 273(52): 34806 - 34812. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 D. Worrall, L. Elias, D. Ashford, M. Smallwood, C. Sidebottom, P. Lillford, J. Telford, C. Holt, and D. Bowles A Carrot Leucine-Rich-Repeat Protein That Inhibits Ice Recrystallization Science, October 2, 1998; 282(5386): 115 - 117. [Abstract] [Full Text]
|
|
|
|
|
|
W.-K. Low, M. Miao, K. V. Ewart, D. S. C. Yang, G. L. Fletcher, and C. L. Hew Skin-type Antifreeze Protein from the Shorthorn Sculpin, Myoxocephalus scorpius. EXPRESSION AND CHARACTERIZATION OF A Mr 9,700 RECOMBINANT PROTEIN J. Biol. Chem., September 4, 1998; 273(36): 23098 - 23103. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
M. E. Houston Jr., H. Chao, R. S. Hodges, B. D. Sykes, C. M. Kay, F. D. Sonnichsen, M. C. Loewen, and P. L. Davies Binding of an Oligopeptide to a Specific Plane of Ice J. Biol. Chem., May 8, 1998; 273(19): 11714 - 11718. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 C. Kaye, L. Neven, A. Hofig, Q.-B. Li, D. Haskell, and C. Guy Characterization of a Gene for Spinach CAP160 and Expression of Two Spinach Cold-Acclimation Proteins in Tobacco Plant Physiology, April 1, 1998; 116(4): 1367 - 1377. [Abstract] [Full Text]
|
|
|
|
 |
|
 J. M. Logsdon Jr. and W. F. Doolittle Origin of antifreeze protein genes: A cool tale in molecular evolution PNAS, April 15, 1997; 94(8): 3485 - 3487. [Full Text] [PDF]
|
|
|
|
|
|
L. Chen, A. L. DeVries, and C.-H. C. Cheng Evolution of antifreeze glycoprotein gene from a trypsinogen gene in Antarctic notothenioid fish PNAS, April 15, 1997; 94(8): 3811 - 3816. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
L. Chen, A. L. DeVries, and C.-H. C. Cheng Convergent evolution of antifreeze glycoproteins in Antarctic notothenioid fish and Arctic cod PNAS, April 15, 1997; 94(8): 3817 - 3822. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
M. Yamashita, N. Ojima, and T. Sakamoto Molecular Cloning and Cold-inducible Gene Expression of Ferritin H Subunit Isoforms in Rainbow Trout Cells J. Biol. Chem., October 25, 1996; 271(43): 26908 - 26913. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
K. V. Ewart, D. S.C. Yang, V. S. Ananthanarayanan, G. L. Fletcher, and C. L. Hew Ca2+-dependent Antifreeze Proteins. MODULATION OF CONFORMATION AND ACTIVITY BY DIVALENT METAL IONS J. Biol. Chem., July 12, 1996; 271(28): 16627 - 16632. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
Z. Gong, K. V. Ewart, Z. Hu, G. L. Fletcher, and C. L. Hew Skin Antifreeze Protein Genes of the Winter Flounder, Pleuronectes americanus, Encode Distinct and Active Polypeptides without the Secretory Signal and Prosequences J. Biol. Chem., February 23, 1996; 271(8): 4106 - 4112. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
F. Sonnichsen, B. Sykes, H Chao, and P. Davies The nonhelical structure of antifreeze protein type III Science, February 19, 1993; 259(5098): 1154 - 1157. [Abstract] [PDF]
|
|
|
|
|
|
K. Miura, S. Ohgiya, T. Hoshino, N. Nemoto, T. Suetake, A. Miura, L. Spyracopoulos, H. Kondo, and S. Tsuda NMR Analysis of Type III Antifreeze Protein Intramolecular Dimer. STRUCTURAL BASIS FOR ENHANCED ACTIVITY J. Biol. Chem., January 5, 2001; 276(2): 1304 - 1310. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
W.-K. Low, Q. Lin, C. Stathakis, M. Miao, G. L. Fletcher, and C. L. Hew Isolation and Characterization of Skin-type, Type I Antifreeze Polypeptides from the Longhorn Sculpin, Myoxocephalus octodecemspinosus J. Biol. Chem., April 6, 2001; 276(15): 11582 - 11589. [Abstract] [Full Text] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
