Structural and functional characterization of osmotically inducible protein C (OsmC) from Thermococcus kodakaraensis KOD1
- Authors
- Park, Seong-Cheol; Pham, Bang Phuong; Van Duyet, Le; Jia, Baolei; Lee, Sangmin; Yu, Rui; Han, Sang Woo; Yang, Jae-Kyung; Hahm, Kyung-Soo; Cheong, Gang-Won
- Issue Date
- May-2008
- Publisher
- ELSEVIER SCIENCE BV
- Keywords
- archaeon; Thermococcus kodakaraensis KOD1; OsmC; electron microscopy
- Citation
- BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS, v.1784, no.5, pp 783 - 788
- Pages
- 6
- Indexed
- SCIE
SCOPUS
- Journal Title
- BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS
- Volume
- 1784
- Number
- 5
- Start Page
- 783
- End Page
- 788
- URI
- https://scholarworks.gnu.ac.kr/handle/sw.gnu/27414
- DOI
- 10.1016/j.bbapap.2008.02.002
- ISSN
- 1570-9639
1878-1454
- Abstract
- 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.
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