Abstract
In response to demands for sustainable domestic fuel sources, research into biofuels has become increasingly important. Many challenges face biofuels in their effort to replace petroleum fuels, but rational strain engineering of algae and photosynthetic organisms offers a great deal of promise. For decades, mutations and stress responses in photosynthetic microbiota were seen to result in production of exciting high-energy fuel molecules, giving hope but minor capability for design. However, ‘-omics’ techniques for visualizing entire cell processing has clarified biosynthesis and regulatory networks. Investigation into the promising production behaviors of the model organism C. reinhardtii and its mutants with these powerful techniques has improved predictability and understanding of the diverse, complex interactions within photosynthetic organisms. This new equipment has created an exciting new frontier for high-throughput, predictable engineering of photosynthetically produced carbon-neutral biofuels.
*These authors contributed equally.
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Abbreviations
- ACCase:
-
Acetyl-CoA carboxylase, E.C. 6.4.1.2
- ACK1:
-
Non-specific protein-tyrosine kinase, E.C. 2.7.10.2
- ACK2:
-
(Acetyl-CoA carboxylase) kinase 2, E.C. 2.7.11.27
- ADH1:
-
Alcohol dehydrogenase 1/Formaldehyde dehydrogenase (FDH1), E.C. 1.1.1.1
- ADH2:
-
Alcohol dehydrogenase (NADP+), E.C. 1.1.1.2
- ADH3:
-
Alcohol dehydrogenase Isoform, E.C. 1.1.1.1
- ADP-Glc PPase:
-
ADP-glucose pyrophosphorylase, E.C. 2.7.7.27
- DGAT:
-
Diacylglycerol acyltransferase, E.C. 2.3.1.20
- FAS:
-
Fatty acid synthase, E.C. 2.3.1.85
- GPAT:
-
Glycerol-3-phosphate acyltransferase, E.C. 2.3.1.15
- HYD1:
-
Ferredoxin hydrogenase, E.C. 1.12.7.2
- HYD2:
-
Ferredoxin hydrogenase Isoform, E.C. 1.12.7.2
- ICL:
-
Isocitrate lyase, E.C. 4.1.3.1
- LDH:
-
Lactate dehydrogenase, E.C. 1.1.1.27
- LPAT:
-
Lysophosphatidic acid acyltransferase, E.C. 2.3.1.51
- MCT:
-
Malonyl acyl carrier protein transferase, E.C. 2.3.1.39
- MLDP:
-
Major lipid droplet protein
- PAT1:
-
Phosphate acetyltransferase, E.C. 2.3.1.8
- PAT2:
-
Phosphate acetyltransferase Isoform, E.C. 2.3.1.8
- PDC3:
-
Pyruvate decarboxylase, E.C. 4.1.1.1
- PDAT:
-
Phospholipid diacylglycerol acyltransferase, E.C. 2.3.1.158
- PDH:
-
Pyruvate dehydrogenase, E.C. 1.2.1.51
- PFL1:
-
Formate C-acetyltransferase, E.C. 2.3.1.54
- DGAT1:
-
Diacylglycerol acyltransferase
- DGTT1:
-
Diacylglycerol acyltransferase
- GPD2:
-
Glycerol-3-phosphate dehydrogenase
- GPD4:
-
Glycerol-3-phosphate dehydrogenase
- LHCBM9:
-
Light Harvesting Complex Chlorophyll a-b binding protein
- LHCSR2:
-
Light Harvesting Complex stress-related 2
- LPAT1:
-
Lysophosphatidic acid acyltransferase
- MLDP1:
-
Major lipid droplet protein
- PDAT1:
-
Phospholipid diacylglycerol acyltransferase
- DAG:
-
Diacylglycerol
- FA:
-
Fatty acid
- FDox:
-
Ferredoxin (oxidized)
- FDred:
-
Ferredoxin (reduced)
- G3P:
-
Glycerol-3-phosphate
- PFR1ox:
-
Pyruvate ferredoxin (oxidized)
- PFR1red:
-
Pyruvate ferredoxin (reduced)
- SQDG:
-
Sulfoquinovovosyl diacylglycerol
- TAG:
-
Triacylglycerol
- Cytb6 :
-
Cytochrome b6 (small subunit of cytochrome b6f complex)
- Cytf:
-
Cytochrome f (large subunit of cytochrome b6f complex)
- Fd:
-
Ferredoxin
- FNR:
-
Ferredoxin – NADP(+) reductase
- LHC:
-
Light Harvesting Complex
- NDH:
-
Plastidial NAD(P)H dehydrogenase complex
- P680:
-
Chlorophyll a P680 (680 nm)
- P700:
-
Chlorophyll a P700 (700 nm)
- Pc:
-
Plastocyanin
- PQ(H)2 :
-
Plastoquinone (reduced)
- PSI:
-
Photosystem I
- PSII:
-
Photosystem II
- PQ0 :
-
Plastoquinone (oxidized)
- 2-DE:
-
2-Dimensional Gel Electrophoresis
- GC/MS:
-
Gas Chromatography/Mass Spectroscopy
- HS:
-
Heat Shock
- LC/MS:
-
Liquid Chromatography/Mass Spectroscopy
- MALDI:
-
Matrix-Assisted Laser Desorption/Ionization
- NMR:
-
Nuclear Magnetic Resonance
- MFA:
-
Metabolite Flux Analysis
- TOF:
-
Time of Flight
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Aucoin, H.R., Gardner, J., Boyle, N.R. (2016). Omics in Chlamydomonas for Biofuel Production. In: Nakamura, Y., Li-Beisson, Y. (eds) Lipids in Plant and Algae Development. Subcellular Biochemistry, vol 86. Springer, Cham. https://doi.org/10.1007/978-3-319-25979-6_18
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