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Proteomic Alterations of Antarctic Ice Microalga Chlamydomonas sp.Under Low-Temperature Stress 被引量:6
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作者 Guang-Feng Kan jin-lai miao +1 位作者 Cui-Juan Shi Guang-You Li 《Journal of Integrative Plant Biology》 SCIE CAS CSCD 2006年第8期965-970,共6页
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 ... 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. 展开更多
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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