Structural and functional characterization of osmotically inducible protein C (OsmC) from Thermococcus kodakaraensis KOD1

被引:28
|
作者
Park, Seong-Cheol [1 ]
Pham, Bang Phuong [1 ]
Van Duyet, Le [1 ]
Jia, Baolei [1 ]
Lee, Sangmin [1 ]
Yu, Rui [1 ]
Han, Sang Woo [2 ]
Yang, Jae-Kyung [3 ]
Hahm, Kyung-Soo [5 ,6 ]
Cheong, Gang-Won [1 ,4 ]
机构
[1] Gyeongsang Natl Univ, Div Appl Life Sci, BK21 Program, Jinju 660701, South Korea
[2] Gyeongsang Natl Univ, Dept Chem, Jinju 660701, South Korea
[3] Gyeongsang Natl Univ, Fac Forest Sci, Jinju 660701, South Korea
[4] Gyeongsang Natl Univ, Environm Biotechnol Natl Core Res Ctr, Jinju 660701, South Korea
[5] Chosun Univ, Sch Med, RCPM, Kwangju 501759, South Korea
[6] Chosun Univ, Sch Med, Dept Cellular Mol Med, Kwangju 501759, South Korea
来源
基金
新加坡国家研究基金会;
关键词
archaeon; Thermococcus kodakaraensis KOD1; OsmC; electron microscopy;
D O I
10.1016/j.bbapap.2008.02.002
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
Osmotically inducible protein C (OsmC) is involved in the cellular defense mechanism against oxidative stress caused by exposure to hyperoxides or elevated osmolarity. OsmC was identified by two-dimensional electrophoresis (2DE) analysis as a protein that is overexpressed in response to osmotic stress, but not under heat and oxidative stress, Here, an OsmC gene from T kodakaraensis KOD1 was cloned and expressed in Escherichia coli. TkOsmC showed a homotetrameric structure based on gel filtration and electron microscopic analyses. TkOsmC has a significant peroxidase activity toward both organic and inorganic peroxides in high, but not in low temperature. (c) 2008 Elsevier B.V. All rights reserved.
引用
收藏
页码:783 / 788
页数:6
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