A part of ice nucleation protein exhibits the ice-binding ability

被引：45
|
作者：
Kobashigawa, Y
Nishimiya, Y
Miura, K
Ohgiya, S
Miura, A
Tsuda, S
机构：
[1] AIST, Funct Prot Res Grp, Res Inst Genome Based Biofactory, Sapporo, Hokkaido 0628517, Japan
[2] AIST, Express & Mol Regulat Res Grp, Res Inst Genome Based Biofactory, Sapporo, Hokkaido 0628517, Japan
[3] Hokkaido Univ, Grad Sch Sci, Div Biol Sci, Sapporo, Hokkaido 0600808, Japan
来源：
FEBS LETTERS | 2005年 / 579卷 / 06期
关键词：
ice nucleation protein; antifreeze protein; ice-growth inhibition; Pseudomonas syringae;
D O I：
10.1016/j.febslet.2005.01.056
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
We generated a recombinant 96-residue polypeptide corresponding to a sequence Tyr(176)-Gly(273) of ice nucleation protein from Pseudomonas syringae (denoted INP96). INP96 exhibited an ability to shape an ice crystal, whose morphology is highly similar to the hexagonal-bipyramid generally identified for antifreeze protein. INP96 also showed a non-linear, concentration-dependent retardation of ice growth. Additionally, circular dichroism and NMR measurements suggested a local structural construction in INP96, which undergoes irreversible thermal denaturation. These data imply that a part of INP constructs a unique structure so as to interact with the ice crystal surfaces. (C) 2005 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
引用
收藏
页码：1493 / 1497
页数：5
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