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Proteomic Alterations of Antarctic Ice Microalga chlamydomonas *** Low-Temperature Stress

Journal of Integrative Plant Biology 2006年第8期48卷 965-970页

作者： Guang-Feng Kan Jin-Lai Miao Cui-Juan Shi Guang-You Li School of the Ocean Harbin Institute of Technology in Weihai Weihai 264209 China Key Laboratory of Marine Bio-active Substances State Oceanic Administration Qingdao 266061 China

Antarctic ice microalga can survive and thrive in cold channels or pores in the Antarctic ice layer. In order to understand the adaptive mechanisms to low temperature, in the present study we compared two-dimensional polyacrylamide gel electrophoresis （2-DE） profiles of normal and low temperature-stressed Antarctic ice microalga chlamydomonas sp. cells. In addition, new protein spots induced by low temperature were identified with peptide mass fingerprinting based on matrix-assisted laser desorption/ionization time-of-flight mass spectrometry （MALDI-TOF-MS） and database searching. Well-resolved and reproducible 2-DE patterns of both normal and low temperature-stressed cells were acquired. A total of 626 spots was detected in control cells and 652 spots were detected in the corresponding low temperature-stressed cells. A total of 598 spots was matched between normal and stressed cells. Two newly synthesized proteins （a and b） in low temperature-stressed cells were characterized. Protein spot A （53 kDa, pl 6.0） was similar to isopropylmalate/homocitrate/citramalate synthases, which act in the transport and metabolism of amino acids. Protein spot b （25 kDa, pl 8.0） was related to glutathione S-transferase, which functions as a scavenger of active oxygen, free radicals, and noxious metabolites. The present study is valuable for the application of ice microalgae, establishing an ice microalga chlamydomonas sp. proteome database, and screening molecular biomarkers for further studies.

关键词： Antarctic ice microalga chlamydomonas sp two-dimensional polyacrylamide gel electrophoresis differentialexpression protein low temperature stress matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF-MS).

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