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Proteomic Alterations of Antarctic Ice Microalga Chlamydomonas sp. Under Low‐Temperature Stress
Author(s) -
Kan GuangFeng,
Miao JinLai,
Shi CuiJuan,
Li GuangYou
Publication year - 2006
Publication title -
journal of integrative plant biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.734
H-Index - 83
eISSN - 1744-7909
pISSN - 1672-9072
DOI - 10.1111/j.1744-7909.2006.00255.x
Subject(s) - chlamydomonas , proteome , mass spectrometry , biochemistry , polyacrylamide gel electrophoresis , proteomics , gel electrophoresis , chemistry , biology , chromatography , botany , enzyme , gene , mutant
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, pI 6.0) was similar to isopropylmalate/homocitrate/citramalate synthases, which act in the transport and metabolism of amino acids. Protein spot b (25 kDa, pI 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. (Managing editor: Li‐Hui Zhao)