Effect of freezing stress on the proteome expression of Antarctic green microalga

Kwang-Man Choi; Mi-Young Lee

doi:10.1007/s13273-012-0020-x

Molecular & Cellular Toxicology

June 2012, Volume 8, Issue 2, pp 163–169

Effect of freezing stress on the proteome expression of Antarctic green microalga

Authors
Authors and affiliations

Kwang-Man Choi
Mi-Young LeeEmail author

Original Paper

First Online:: 03 July 2012

Received:: 04 April 2011
Accepted:: 25 March 2012

DOI: 10.1007/s13273-012-0020-x

Cite this article as:: Choi, KM. & Lee, MY. Mol. Cell. Toxicol. (2012) 8: 163. doi:10.1007/s13273-012-0020-x

Abstract

The effects of freezing stress on the protein expression profile and enzyme activity change in Antarctic green microalga were examined in this investigation. Antarctic green microalga was cultured at 4°C for optimal growth, and the temperature was reduced near to 0°C in order to apply freezing stress. The resultant differentially expressed proteins induced by freezing stress were analyzed by mass spectrometry following two-dimensional gel electrophoresis (2-DE). In total, about 320 protein spots were detected on the 2-DE gel, and 17 proteins showed a greater than two-fold change in abundance; of these, 5 proteins were up-regulated, and 12 proteins were down-regulated. Moreover, total enzyme activities and isozyme patterns of several antioxidant enzymes, named catalase, superoxide dismutase and aldehyde dehydrogenase were changed upon applying freezing stress.

Keywords

Freezing stress Proteomics Orthologues Antioxidant enzyme Antarctic green microalga

References

1.
Knight, H., Trewavas, A. J. & Knight, M. R. Cold calcium signaling in Arabidopsis involves two cellular pools and a change in calcium signature after acclimation. Plant Cell 8:489–503 (1996).PubMedGoogle Scholar
2.
Lee, J. Y., Joo, H. J., Choy, Y. H., Ha-Lee, Y. M. & Lee, D. H. Using specialized cDNA microarrays to analyze Arabidopsis gene expression under cold stress. Plant Biol 53:240–250 (2010).CrossRefGoogle Scholar
3.
Park, S. K., Jin, E. S. & Lee, M. Y. Expression and antioxidant enzymes in Chatoceros neogracile, an Antarctic alga. CryoLett 29:351–361 (2008).Google Scholar
4.
Kenji, Y., Eiko, I., Eiko, W., Kazuhisa, M. & Kazumasa, H. Mitigation of osmotic and salt stresses by abscisic acid through reduction of stress-derived oxidative damage in Chlamydomonas reinhardtii. Plant Sci 167:1335–1341 (2004).CrossRefGoogle Scholar
5.
Kim, Y. K. & Lee, M. Y. Proteomic approach for discovery of potential biomarkers for Cd toxicity in rice. BioChip J 3:254–260 (2009).Google Scholar
6.
Jeon, Y. M., Son, B. S. & Lee, M. Y. Proteomic identification of the differentially expressed proteins in human lung epithelial cells by airborne particulate matter. J Appl Toxicol 31:45–52 (2010).CrossRefGoogle Scholar
7.
Lello, Z., Sara, R., Paolo, A. & Pier, G. R. Proteomics as a complementary tool for identifying unintended side effects occurring in transgenic maize seeds as a result of genetic modifications. J Proteome Res 7:1850–1861 (2008).CrossRefGoogle Scholar
8.
Jeffrey, C. S. Simultaneous qualitative and quantitative analysis of the Escherichia coli proteome. Mol Cell Proteomics 5:589–607 (2006).Google Scholar
9.
Kan, G. F., Miao, J. L., Shi, C. J. & Li, G. Y. Proteomic alterations of antarctic ice microalga Chlamydomonas sp. under low-temperature stress. J Integr Plant Biol 48:965–970 (2006).CrossRefGoogle Scholar
10.
Smeitink, J. A. M. Cell biological consequences of mitochondrial NADH: ubiquinone oxidoreductase deficiency. Neurovascular Res 1:29–40 (2004).CrossRefGoogle Scholar
11.
Nora, P., Nancy, G., Arnaldo, V. & Robert, B. NADH dehydrogenase in Neurospora crassa contains myristic acid covalently linked to the ND5 subunit peptide. Biochimica Biophysica Acta 1495:223–230 (2000).CrossRefGoogle Scholar
12.
Hashimoto, M. & Komatsu, S. Proteomic analysis of rice seedlings during cold stress. Proteomics 7:1293–1302 (2007).CrossRefPubMedGoogle Scholar
13.
Chenping, X., Wesley, M. G., Joseph, S., Thomas, J. C. & Savithiry, N. Separation and identification of soybean leaf proteins by two-dimension gel electrophoresis and mass spectrometry. Phytochemistry 67:2431–2440 (2006).CrossRefGoogle Scholar
14.
Makino, A., Mae, T. & Ohira, K. Photosynthesis and ribulose-1,5-bisphosphate carboxylase/oxygenase in rice leaves from emergence through senescence. Planta 166:414–420 (1985).CrossRefGoogle Scholar
15.
Joseph, C. V. V., Sanjay, F. G., George, Y. & Maurice, S. B. K. Cold-induced changes in ribulose 1,5-bisphosphate carboxylase-oxygenase and phosphoenolpyruvate carboxylase in citrus. Envir Exp Bot 35:25–31 (1995).CrossRefGoogle Scholar
16.
Reininger, L. et al. NIMA-related protein kinase is essential for completion of the sexual cycle of malaria parasites. Biologi Chem 280:31957–31964 (2005).CrossRefGoogle Scholar
17.
Bradley, B. A. & Quarmby, L. M. A NIMA-related kinase, Cnk2p, regulates both flagellar length and cell size in Chlamydomonas. J Cell Sci 118:3317–3326 (2005).CrossRefPubMedGoogle Scholar
18.
Ana, V., Iris, M., Alicia, M. M., Enrique, F. & Antonia, H. Heterocyst development and diazotrophic metabolism in terminal respiratory oxidase mutants of the cyanobacterium Anabaena sp. Strain PCC 7120. J Bacteriol 189:4425–4430 (2007).CrossRefGoogle Scholar
19.
Herbert, B. Regulation of nitrogen fixation in heterocyst-forming cyanobacteria. Trends Plant Sci 3:346–351 (1998).CrossRefGoogle Scholar
20.
Gao, M. J., Parkin, I., Lydiate, D. & Hannoufa, A. An auxin-responsive SCARECROW-like transcriptional activator interacts with histone deacetylase. Plant Mol Bio 55:417–431 (2004).CrossRefGoogle Scholar
21.
Morohashi, K., Minami, M., Takase, H., Hotta, Y. & Hiratsuka, K. Isolation and characterization of a novel GRAS gene that regulates meiosis-associated gene expression. Biologi Chem 278:20865–20873 (2003).CrossRefGoogle Scholar
22.
Jorg, D., Tobias, G. K. & Jonathan, G. Monoterpene and sesquiterpene synthases and the origin of terpene skeletal diversity in plants. Phytochemistry 70:1621–1637 (2009).CrossRefGoogle Scholar
23.
Shelton, D. et al. Isolation and partial characterisation of a putative monoterpene synthase from Melaleuca alternifolia. Plant Physiol Biochem 42:875–882 (2004).CrossRefPubMedGoogle Scholar
24.
Yasuyuki, A., Qingsong, Z., Masahiro, M., Subbaratnam, M. & Karl, J. K. Properties of catalytic, linker and chitin-binding domains of insect chitinase. Insect Biochem Mol Bio 33:631–648 (2003).CrossRefGoogle Scholar
25.
David, J. S., Geoffrey, B. F., Anthony, H. C. H. & Verena, C. M. Structure and function of cereal and related higher plant (1→4)-β-xylan endohydrolases. J Cereal Sci 37:111–127 (2003).CrossRefGoogle Scholar
26.
Park, S. K., Nam, S. W., Ryu, J. C., Ham, J. H. & Lee, M. Y. Proteomic analysis of rat liver proteins differentially induced by trichloroethylene. BioChip J 4:57–62 (2010).CrossRefGoogle Scholar
27.
Yoshida, K., Igarashi, E., Mukai, M., Hirata, K. & Miyamoto, K. Induction of tolerance to oxidative stress in the green alga, Chlamydomonas reinhardtii, by abscisic acid. Plant Cell Environ 26:451–457 (2003).CrossRefGoogle Scholar
28.
Vega, J. M., Garbayo, I., Domínguez, M. J. & Vigara, J. Effect of abiotic stress on photosynthesis and respiration in Chlamydomonas reinhardtii: Induction of oxidative stress. Enzyme Microbial Tech 40:163–167 (2006).CrossRefGoogle Scholar
29.
de Jesus Pereira, E., Panek, A. & Eleutherio, E. Protection against oxidation during dehydration of yeast. Cell Stress Chaperones 8:120–124 (2003).CrossRefGoogle Scholar
30.
Sunkar, R., Bartels, D. & Kirch, H. H. Overexpression of a stress-inducible aldehyde dehydrogenase gene from Arabidopsis thaliana in transgenic plants improves stress tolerance. Plant J 35:452–464 (2003).CrossRefPubMedGoogle Scholar
31.
Nichols, H. W. & Bold, H. C. Trichosarcina polymorpha gen. et sp. nov. 1:34–38 (1965).Google Scholar
32.
Jeon, Y. M., Park, S. K., Kim, W. J., Ham, J. H. & Lee, M. Y. The effects of TiO₂ nanoparticles on the protein expression in mouse lung. Mol Cell Toxicol 7:283–289 (2011).CrossRefGoogle Scholar
33.
Park, S. K., Seo, J. B. & Lee, M. Y. Proteomic profiling of hempseed proteins from Cheungsam. Biochim Biophys Acta 1824:374–382 (2012).PubMedGoogle Scholar
34.
Shin, H. W. & Lee, M. Y. Cadmium-induced changes in antioxidant enzymes from the marine alga Nannochloropsis oculata. J Appl Phycol 15:13–19 (2003).CrossRefGoogle Scholar
35.
Park, S. K., Jin, E. S., Lee, C. G. & Lee, M. Y. High light-induced changes in the activities of antioxidant enzymes and the accumulation of astaxanthin in the green alga Haematococcus pluvialis. Mol Cell Toxicol 4:300–306 (2008).Google Scholar

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Authors and Affiliations

Kwang-Man Choi
- 1
Mi-Young Lee
- 1
Email author

1.Department of Medical BiotechnologySoonChunHyang UniversityAsan, ChungnamKorea

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Effect of freezing stress on the proteome expression of Antarctic green microalga

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