Co-operative effect of the isoforms of type III antifreeze protein expressed in Notched-fin eelpout, Zoarces elongatus Kner

FEBS Journal

Volumn 272, Issue 2, 2005, Pages 482-492

  Nishimiya, Yoshiyuki ^a   Sato, Ryoko ^a   Takamichi, Manabu ^b   Miura, Ai ^a   Tsuda, Sakae ^a,b  

^a NATIONAL INSTITUTE OF ADVANCED INDUSTRIAL SCIENCE AND TECHNOLOGY AIST   (Japan)

^b HOKKAIDO UNIVERSITY   (Japan)

Author keywords

Co operative effect; Notched fin eelpout; Type III antifreeze protein

Indexed keywords

ANTIFREEZE PROTEIN; ISOPROTEIN;

AMINO ACID SEQUENCE; ANIMAL TISSUE; ARTICLE; CONCENTRATION RESPONSE; FISH; FREEZING; HYSTERESIS; LIVER; MOLECULAR CLONING; NONHUMAN; PRIORITY JOURNAL; PROTEIN ISOLATION;

AMINO ACID SEQUENCE; ANIMALS; ANTIFREEZE PROTEINS, TYPE III; CLONING, MOLECULAR; MOLECULAR SEQUENCE DATA; PERCIFORMES; PROTEIN ISOFORMS; RECOMBINANT PROTEINS; SEQUENCE ALIGNMENT;

ANIMALIA; LYCODES TOYAMENSIS; ZOARCES; ZOARCES ELONGATUS;

EID: 12544249736     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2004.04490.x     Document Type: Article

References (34)

1. Knight CA, Cheng CC & DeVries AL (1991) Adsorption of alpha-helical antifreeze peptides on specific ice crystal surface planes. Biophys J 59, 409-418.
2. Raymond JA & DeVries AL (1977) Adsorption inhibition as a mechanism of freezing resistance in polar fishes. Proc Natl Acad Sci USA 74, 2589-2593.
3. Cheng CH & DeVries AL (1989) Structures of antifreeze peptides from the antarctic eel pout, Austrolycicthys brachycephalus. Biochim Biophys Acta 997, 55-64.
4. Schrag JD, Cheng CH, Panico M, Morris HR & DeVries AL (1987) Primary and secondary structure of antifreeze peptides from arctic and antarctic zoarcid fishes. Biochim Biophys Acta 915, 357-370.
5. Hew CL, Slaughter D, Joshi SB, Fletcher GL & Ananthanarayanan VS (1984) Antifreeze polypeptides from the Newfoundland ocean pout, Macrozoarces americanus: presence of multiple and compositionally diverse components. J Comp Physiol B Biochem Syst Environ Physiol 155, 81-88.
6. Scott GK, Hayes PH, Fletcher GL & Davies PL (1988) Wolffish antifreeze protein genes are primarily organized as tandem repeats that each contain two genes in inverted orientation. Mol Cell Biol 8, 3670-3675.
7. Sönnichsen FD, Sykes BD, Chao H & Davies PL (1993) The nonhelical structure of antifreeze protein type III. Science 259, 1154-1157.
8. Jia Z, DeLuca CI, Chao H & Davies PL (1996) Structural basis for the binding of a globular antifreeze protein to ice. Nature 384, 285-288.
9. Sönnichsen FD, DeLuca CI, Davies PL & Sykes BD (1996) Refined solution structure of type III antifreeze protein: hydrophobic groups may be involved in the energetics of the protein-ice interaction. Structure 4, 1325-1337.
10. Yang DS, Hon WC, Bubanko S, Xue Y, Seetharaman J, Hew CL & Sicheri F (1998) Identification of the ice-binding surface on a type III antifreeze protein with a 'flatness function' algorithm. Biophys J 74, 2142-2151.
11. Graether SP, DeLuca CI, Baardsnes J, Hill GA, Davies PL & Jia Z (1999) Quantitative and qualitative analysis of type III antifreeze protein structure and function. J Biol Chem 274, 11842-11847.
12. Antson AA, Smith DJ, Roper DI, Lewis S, Caves LS, Verma CS, Buckley SL, Lillford PJ & Hubbard RE (2001) Understanding the mechanism of ice binding by type III antifreeze proteins. J Mol Biol 305, 875-889.
13. Miura K, Ohgiya S, Hoshino T, Nemoto N, Suetake T, Miura A, Spyracopoulos L, Kondo H & Tsuda S (2001) NMR analysis of type III antifreeze protein intramolecular dimer. Structural basis for enhanced activity. J Biol Chem 276, 1304-1310.
14. Ko TP, Robinson H, Gao YG, Cheng CH, DeVries AL & Wang AH (2003) The refined crystal structure of an eel pout type III antifreeze protein RD1 at 0.62-Å resolution reveals structural microheterogeneity of protein and solvation. Biophys J 84, 1228-1237.
15. Chao H, Sönnichsen FD, DeLuca CI, Sykes BD & Davies PL (1994) Structure-function relationship in the globular type III antifreeze protein: identification of a cluster of surface residues required for binding to ice. Protein Sci 3, 1760-1769.
16. DeLuca CI, Davies PLYe, Q & Jia Z (1998) The effects of steric mutations on the structure of type III antifreeze protein and its interaction with ice. J Mol Biol 275, 515-525.
17. Chen G & Jia Z (1999) Ice-binding surface of fish type III antifreeze. Biophys J 77, 1602-1608.
18. Baardsnes J & Davies PL (2002) Contribution of hydrophobic residues to ice binding by fish type III antifreeze protein. Biochim Biophys Acta 1601, 49-54.
19. Li XM Trinh KY Hew CL Buettner B Baenziger J & Davies PL (1985) Structure of an antifreeze poly peptide and its precursor from the ocean pout, Macrozoarces americanus. J Biol Chem 260, 12904-12909.
20. Hew CL Wang NC Joshi S Fletcher GL Scott GK Hayes PH Buettner B & Davies PL (1988) Multiple genes provide the basis for antifreeze protein diversity and dosage in the ocean pout, Macrozoarces americanus. J Biol Chem 263, 12049-12055.
21. Wang X DeVries AL & Cheng CH (1995) Antifreeze peptide heterogeneity in an antarctic eel pout includes an unusually large major variant comprised of two 7 kDa type III AFPs linked in tandem. Biochim Biophys Acta 1247, 163-172.
22. Chao H Davies PL Sykes BD & Sönnichsen FD (1993) Use of proline mutants to help solve the NMR solution structure of type III antifreeze protein. Protein Sci 2, 1411-1428.
23. DeLuca CI Chao H Sönnichsen FD Sykes BD & Davies PL (1996) Effect of type III antifreeze protein dilution and mutation on the growth inhibition of ice. Biophys J 71, 2346-2355.
24. Houston ME Chao H Hodges RS Sykes BD Kay CM Sönnichsen FD Loewen MC & Davies PL (1998) Binding of an oligopeptide to a specific plane of ice. J Biol Chem 273, 11714-11718.
25. Hew CL & Yang DS (1992) Protein interaction with ice. Eur J Biochem 203, 33-42.
26. Wen D & Laursen RA (1992) A model for binding of an antifreeze polypeptide to ice. Biophys J 63, 1659-1662.
27. Nishimiya Y Ohgiya S & Tsuda S (2003) Artificial multimers of the type III antifreeze protein. Effects on thermal hysteresis and ice crystal morphology. J Biol Chem 278, 32307-32312.
28. Chao H Hodges RS Kay CM Gauthier SY & Davies PL (1996) A natural variant of type I antifreeze protein with four ice-binding repeats is a particularly potent antifreeze. Protein Sci 5, 1150-1156.
29. Leinala EK Davies PL Doucet D Tyshenko MG Walker VK & Jia Z (2002) A beta-helical antifreeze protein isoform with increased activity. Structural and functional insights. J Biol Chem 277, 33349-33352.
30. Baardsnes J Kuiper MJ & Davies PL (2003) Antifreeze protein dimer: when two ice-binding faces are better than one. J Biol Chem 278, 38942-38947.
31. Burcham TS Knauf MJ Osuga DT Feeney RE & Yeh Y (1984) Antifreeze glycoproteins: influence of polymer length and ice crystal habit on activity. Biopolymers 23, 1379-1395.
32. Burcham TS Osuga DT Chino H & Feeney RE (1984) Analysis of antifreeze glycoproteins in fish serum. Anal Biochem 139, 197-204.
33. Fletcher GL Hew CL Li XM Haya K & Kao MH (1985) Year-round presence of high levels of plasma antifreeze peptides in a temperate fish, ocean pout (Macrozoarces americanus). Can J Zool 63, 488-493.
34. Laemmli U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-684.