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

页码：1493 / 1497

页数：5

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