Difference between revisions of "Part:BBa K3750000"
| Line 3: | Line 3: | ||
<partinfo>BBa_K3750000 short</partinfo> | <partinfo>BBa_K3750000 short</partinfo> | ||
| − | Profile | + | ===Profile=== |
Gene name: GSHR1 | Gene name: GSHR1 | ||
| − | Protein: Glutathione Reductase | + | <br>Protein: Glutathione Reductase |
| − | Subcellular Localisation: Cytosol | + | <br>Subcellular Localisation: Cytosol |
| − | Base Pairs: 1482 bp | + | <br>Base Pairs: 1482 bp |
| − | Amino acid length: 493 | + | <br>Amino acid length: 493 |
| − | Molecular Weight: 52 kDa | + | <br>Molecular Weight: 52 kDa |
| − | Organism of origin: Chlamydomonas reinhardtii | + | <br>Organism of origin: Chlamydomonas reinhardtii |
| − | + | ===Properties and Biology=== | |
| − | === | + | |
When Glutathione (GSH) neutralises ROS, GSH becomes a radical in the form of oxidised glutathione disulfide (GSSG). Glutathione reductase (GR) regulates cellular glutathione homeostasis by using NADPH and FAD to catalyze the reduction of glutathione disulfide (GSSG) into GSH. Glutathione reductase is highly conserved in aerobic organisms as it is important for cell survival when the organism is subjected to oxidative stress (Carlberg, 1985). | When Glutathione (GSH) neutralises ROS, GSH becomes a radical in the form of oxidised glutathione disulfide (GSSG). Glutathione reductase (GR) regulates cellular glutathione homeostasis by using NADPH and FAD to catalyze the reduction of glutathione disulfide (GSSG) into GSH. Glutathione reductase is highly conserved in aerobic organisms as it is important for cell survival when the organism is subjected to oxidative stress (Carlberg, 1985). | ||
In Chlamydomonas reinhardtii, GR is present in all cellular compartments. This part documents the cytosolic isoform of GR in C. reinhardtii encoded by the gene GSHR1 (Merchant et al., 2007). GR is a homodimeric flavoprotein with a molecular weight of 52-kDa subunits with 493 amino acids. The gene is 1482 base pairs long. GSHR1 has a binding site for 1 FAD and 1 NAD per subunit. | In Chlamydomonas reinhardtii, GR is present in all cellular compartments. This part documents the cytosolic isoform of GR in C. reinhardtii encoded by the gene GSHR1 (Merchant et al., 2007). GR is a homodimeric flavoprotein with a molecular weight of 52-kDa subunits with 493 amino acids. The gene is 1482 base pairs long. GSHR1 has a binding site for 1 FAD and 1 NAD per subunit. | ||
| − | [[File:T--UNSW_Australia--GSHR1.png| | + | [[File:T--UNSW_Australia--GSHR1.png|400x300px|GSHR1 catalysis pathway]] |
| + | ===Usage=== | ||
As part of the 2021 UNSW_Australia project to combat coral bleaching, this gene was included in our plasmid design along with bifunctional glutathione synthetase and glutathione peroxidase to upregulate glutathione production. Glutathione reductase was used to recycle GSH from glutathione disulfide (GSSG) to enhance the efficiency of the glutathione system and to avoid the accumulation of GSSG in our chassis. Due to limited laboratory access resulting from COVID-19 restrictions, we could not perform experiments to characterise GSHR1, but we hope the information documented would be useful for future teams. | As part of the 2021 UNSW_Australia project to combat coral bleaching, this gene was included in our plasmid design along with bifunctional glutathione synthetase and glutathione peroxidase to upregulate glutathione production. Glutathione reductase was used to recycle GSH from glutathione disulfide (GSSG) to enhance the efficiency of the glutathione system and to avoid the accumulation of GSSG in our chassis. Due to limited laboratory access resulting from COVID-19 restrictions, we could not perform experiments to characterise GSHR1, but we hope the information documented would be useful for future teams. | ||
| − | + | ||
| + | ===References=== | ||
| + | CARLBERG, I. & MANNERVIK, B. 1985. Glutathione reductase. Methods Enzymol, 113, 484-90. | ||
| + | |||
| + | MERCHANT, S. S., PROCHNIK, S. E., VALLON, O., HARRIS, E. H., KARPOWICZ, S. J., WITMAN, G. B., TERRY, A., SALAMOV, A., FRITZ-LAYLIN, L. K., MARÉCHAL-DROUARD, L., MARSHALL, W. F., QU, L.-H., NELSON, D. R., SANDERFOOT, A. A., SPALDING, M. H., KAPITONOV, V. V., REN, Q., FERRIS, P., LINDQUIST, E., SHAPIRO, H., LUCAS, S. M., GRIMWOOD, J., SCHMUTZ, J., GRIGORIEV, I. V., ROKHSAR, D. S. & GROSSMAN, A. R. 2007. The Chlamydomonas Genome Reveals the Evolution of Key Animal and Plant Functions. Science, 318, 245-251. | ||
| + | |||
| + | |||
<!-- --> | <!-- --> | ||
<span class='h3bb'>Sequence and Features</span> | <span class='h3bb'>Sequence and Features</span> | ||
Latest revision as of 17:00, 21 October 2021
GSHR1 glutathione reductase (from Chlamydomonas reinhardtii)
Profile
Gene name: GSHR1
Protein: Glutathione Reductase
Subcellular Localisation: Cytosol
Base Pairs: 1482 bp
Amino acid length: 493
Molecular Weight: 52 kDa
Organism of origin: Chlamydomonas reinhardtii
Properties and Biology
When Glutathione (GSH) neutralises ROS, GSH becomes a radical in the form of oxidised glutathione disulfide (GSSG). Glutathione reductase (GR) regulates cellular glutathione homeostasis by using NADPH and FAD to catalyze the reduction of glutathione disulfide (GSSG) into GSH. Glutathione reductase is highly conserved in aerobic organisms as it is important for cell survival when the organism is subjected to oxidative stress (Carlberg, 1985). In Chlamydomonas reinhardtii, GR is present in all cellular compartments. This part documents the cytosolic isoform of GR in C. reinhardtii encoded by the gene GSHR1 (Merchant et al., 2007). GR is a homodimeric flavoprotein with a molecular weight of 52-kDa subunits with 493 amino acids. The gene is 1482 base pairs long. GSHR1 has a binding site for 1 FAD and 1 NAD per subunit.
Usage
As part of the 2021 UNSW_Australia project to combat coral bleaching, this gene was included in our plasmid design along with bifunctional glutathione synthetase and glutathione peroxidase to upregulate glutathione production. Glutathione reductase was used to recycle GSH from glutathione disulfide (GSSG) to enhance the efficiency of the glutathione system and to avoid the accumulation of GSSG in our chassis. Due to limited laboratory access resulting from COVID-19 restrictions, we could not perform experiments to characterise GSHR1, but we hope the information documented would be useful for future teams.
References
CARLBERG, I. & MANNERVIK, B. 1985. Glutathione reductase. Methods Enzymol, 113, 484-90.
MERCHANT, S. S., PROCHNIK, S. E., VALLON, O., HARRIS, E. H., KARPOWICZ, S. J., WITMAN, G. B., TERRY, A., SALAMOV, A., FRITZ-LAYLIN, L. K., MARÉCHAL-DROUARD, L., MARSHALL, W. F., QU, L.-H., NELSON, D. R., SANDERFOOT, A. A., SPALDING, M. H., KAPITONOV, V. V., REN, Q., FERRIS, P., LINDQUIST, E., SHAPIRO, H., LUCAS, S. M., GRIMWOOD, J., SCHMUTZ, J., GRIGORIEV, I. V., ROKHSAR, D. S. & GROSSMAN, A. R. 2007. The Chlamydomonas Genome Reveals the Evolution of Key Animal and Plant Functions. Science, 318, 245-251.
Sequence and Features
- 10INCOMPATIBLE WITH RFC[10]Illegal PstI site found at 556
- 12INCOMPATIBLE WITH RFC[12]Illegal PstI site found at 556
- 21COMPATIBLE WITH RFC[21]
- 23INCOMPATIBLE WITH RFC[23]Illegal PstI site found at 556
- 25INCOMPATIBLE WITH RFC[25]Illegal PstI site found at 556
Illegal NgoMIV site found at 145
Illegal NgoMIV site found at 252 - 1000COMPATIBLE WITH RFC[1000]