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Proteomic analysis of the response of an acidophilic strain of Chlamydomonas sp. (Chlorophyta) to natural metal‐rich water
Author(s) -
Cid Cristina,
GarciaDescalzo Laura,
CasadoLafuente Victor,
Amils Ricardo,
Aguilera Angeles
Publication year - 2010
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.200900592
Subject(s) - chlamydomonas reinhardtii , chlorophyta , photosynthesis , extremophile , chlamydomonas , algae , botany , biology , rubisco , proteome , mixotroph , phosphoglycerate kinase , biochemistry , chemistry , enzyme , thermophile , bacteria , heterotroph , genetics , gene , mutant
A proteomic approach including 2‐DE and MALDI‐TOF analysis has been developed to identify the soluble proteins of the unicellular photosynthetic algae Chlamydomonas sp. isolated from an extreme acidic environment, Río Tinto (southwest Spain). We have analyzed the soluble proteome obtained from whole cells growing on metal‐rich natural acidic water from the river in comparison with the same strain growing in artificial BG‐11 media. The most drastic effect was the decrease in the abundance of the ribulose‐1,5‐biphosphate carboxylase as well as other enzymes related to photosynthesis. However, phytochrome B, phosphoribulokinase, and phosphoglycerate kinase were upregulated when cells were grown in metal‐rich acidic water. Besides, increased accumulation of two Hsps, Hsp70 and Hsp90 as well as other stress‐related enzymes were also found in the cells growing in natural acidic water. These results suggest that naturally occurring metal‐rich water induces a stress response in acidophilic Chlamydomonas forcing algal cells to reorganize their metabolic pathways as an adaptive response to these environmental conditions.