Lack of isocitrate lyase in Chlamydomonas leads to changes in carbon metabolism and in the response to oxidative stress under mixotrophic growth. (7th January 2014)
- Record Type:
- Journal Article
- Title:
- Lack of isocitrate lyase in Chlamydomonas leads to changes in carbon metabolism and in the response to oxidative stress under mixotrophic growth. (7th January 2014)
- Main Title:
- Lack of isocitrate lyase in Chlamydomonas leads to changes in carbon metabolism and in the response to oxidative stress under mixotrophic growth
- Authors:
- Plancke, Charlotte
Vigeolas, Helene
Höhner, Ricarda
Roberty, Stephane
Emonds‐Alt, Barbara
Larosa, Véronique
Willamme, Remi
Duby, Franceline
Onga Dhali, David
Thonart, Philippe
Hiligsmann, Serge
Franck, Fabrice
Eppe, Gauthier
Cardol, Pierre
Hippler, Michael
Remacle, Claire - Abstract:
- <abstract abstract-type="main" id="tpj12392-abs-0001"> <title>Summary</title> <p>Isocitrate lyase is a key enzyme of the glyoxylate cycle. This cycle plays an essential role in cell growth on acetate, and is important for gluconeogenesis as it bypasses the two oxidative steps of the tricarboxylic acid (TCA) cycle in which CO<sub>2</sub> is evolved. In this paper, a null <italic>icl</italic> mutant of the green microalga <italic>Chlamydomonas reinhardtii</italic> is described. Our data show that isocitrate lyase is required for growth in darkness on acetate (heterotrophic conditions), as well as for efficient growth in the light when acetate is supplied (mixotrophic conditions). Under these latter conditions, reduced acetate assimilation and concomitant reduced respiration occur, and biomass composition analysis reveals an increase in total fatty acid content, including neutral lipids and free fatty acids. Quantitative proteomic analysis by <sup>14</sup>N/<sup>15</sup>N labelling was performed, and more than 1600 proteins were identified. These analyses reveal a strong decrease in the amounts of enzymes of the glyoxylate cycle and gluconeogenesis in parallel with a shift of the TCA cycle towards amino acid synthesis, accompanied by an increase in free amino acids. The decrease of the glyoxylate cycle and gluconeogenesis, as well as the decrease in enzymes involved in β–oxidation of fatty acids in the <italic>icl</italic> mutant are probably major factors that contribute to<abstract abstract-type="main" id="tpj12392-abs-0001"> <title>Summary</title> <p>Isocitrate lyase is a key enzyme of the glyoxylate cycle. This cycle plays an essential role in cell growth on acetate, and is important for gluconeogenesis as it bypasses the two oxidative steps of the tricarboxylic acid (TCA) cycle in which CO<sub>2</sub> is evolved. In this paper, a null <italic>icl</italic> mutant of the green microalga <italic>Chlamydomonas reinhardtii</italic> is described. Our data show that isocitrate lyase is required for growth in darkness on acetate (heterotrophic conditions), as well as for efficient growth in the light when acetate is supplied (mixotrophic conditions). Under these latter conditions, reduced acetate assimilation and concomitant reduced respiration occur, and biomass composition analysis reveals an increase in total fatty acid content, including neutral lipids and free fatty acids. Quantitative proteomic analysis by <sup>14</sup>N/<sup>15</sup>N labelling was performed, and more than 1600 proteins were identified. These analyses reveal a strong decrease in the amounts of enzymes of the glyoxylate cycle and gluconeogenesis in parallel with a shift of the TCA cycle towards amino acid synthesis, accompanied by an increase in free amino acids. The decrease of the glyoxylate cycle and gluconeogenesis, as well as the decrease in enzymes involved in β–oxidation of fatty acids in the <italic>icl</italic> mutant are probably major factors that contribute to remodelling of lipids in the <italic>icl</italic> mutant. These modifications are probably responsible for the elevation of the response to oxidative stress, with significantly augmented levels and activities of superoxide dismutase and ascorbate peroxidase, and increased resistance to paraquat.</p> </abstract> … (more)
- Is Part Of:
- Plant journal. Volume 77:Number 3(2014:Feb.)
- Journal:
- Plant journal
- Issue:
- Volume 77:Number 3(2014:Feb.)
- Issue Display:
- Volume 77, Issue 3 (2014)
- Year:
- 2014
- Volume:
- 77
- Issue:
- 3
- Issue Sort Value:
- 2014-0077-0003-0000
- Page Start:
- 404
- Page End:
- 417
- Publication Date:
- 2014-01-07
- Subjects:
- Plant molecular biology -- Periodicals
Plant cells and tissues -- Periodicals
Botany -- Periodicals
580 - Journal URLs:
- http://onlinelibrary.wiley.com/journal/10.1111/(ISSN)1365-313X ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1111/tpj.12392 ↗
- Languages:
- English
- ISSNs:
- 0960-7412
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 6519.200000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 3071.xml